Use of anti-MAdCAM antibodies for the treatment of coeliac disease and tropical sprue The invention relates to the use of anti-MAdCAM antibodies for the manufacture of a medicament for the treatment of coeliac disease and/or tropical sprue. Mucosal addressin cell adhesion molecule (MAdCAM) is a member of the immunoglobulin superfamily of cell adhesion receptors. It is one of the adhesion molecules involved in the recruitment of lymphocytes to tissues when required, by means of interacting with an integrin molecule on the surfacfe of the lymphocytes. It has been shown that antibodies that inhibit binding of MAdCAM to its integrin binding partner, a4p7, for example anti-MAdCAM antibodies (e.g. MECA-367; US 5,403,919, US 5,538,724) or anti-cc^ antibodies (e.g. Act-1; US 6,551,593), can inhibit leukocyte extravasation into inflamed intestine, and can therefore be beneficial in the treatment of inflammatory bowel disease (IBD). Anti-MAdCAM antibodies such as MECA-367, however, are not therapeutically useful in human patients; MECA-367 binds mouse MAdCAM, and does not show much affinity for the human MAdCAM molecule. In addition, being a rat antibody, it will lead to an immune response in human patients and therefore not be suitable for therapeutic use. Mouse monoclonal antibodies, directed against human MAdCAM have been described (WO 96/24673), but these are also likely to be immunogenic in humans. Recently, therapeutically useful, fully human anti-human MAdCAM antibodies with exquisite specificity and affinity to human and primate MAdCAM have been developed and disclosed in W02005/067620. An inhibitor of the interaction between MAdCAM and a^ integrin, such as a blacking anti-MAdCAM antibody, or an antibody to a4p7 integrin (such as MLN02, which is humanised Act-1 , described in WO 01/078779), has been postulated to be useful in the treatment of inflammatory bowel disease (IBD). However, it has now been found that inhibitors of this interaction including blocking antibodies to MAdCAM, are also useful in the treatment of coeliac disease and tropical sprue. Coeliac disease (also known as gluten-sensitive enteropathy or coeliac sprue) is a condition of the small intestine. The condition affects up to 1 in 300 people in the United Kingdom, Europe and the USA. Coeliac disease is a common condition, and can affect anyone at any age. It was thought to be more common in men, but probably occurs equally in men and women. Gluten, a mixture of two proteins, gliadin and glutenin, is found in wheat, barley and rye. It reacts with the small bowel, causing damage by activating the immune system to attack the delicate lining of the bowel,. which is responsible for absorbing nutrients and vitamins, The condition is often diagnosed in childhood after weaning when cereals are introduced into the diet, although it can be diagnosed at any age. The symptoms can be subtle, and the patient may feel unwell for no reason for some time before the diagnosis is made. First symptoms usually include becoming irritable and miserable, with a poor appetite and failure to gain weight. Stools (bowel motions) can become pale, bulky and smell nasty. Some children start with vomiting and diarrhoea, so they are often given the wrong diagnosis of 'gastroenteritis'. The stomach may become swollen, and the muscles of the arms and legs become wasted and thin, In adults the symptoms may be similar, including weight loss with pale, offensive diarrhoea, or constipation and abdominal bloating with 'wind1. Half of adults with coeliac disease do not have any symptoms from the bowel. They approach their doctor because of extreme tiredness, psychological problems like depression, bone pain and sometimes even fractures (due to thinning of the bones), ulcers in the mouth or a blistering, tlchy skin rash mostly on the elbows and knees (called dermatitis herpetiformis). Some women with coeliac disease have difficulty getting pregnant, and may be diagnosed because of this. Recurrent miscarriage (spontaneous loss of a pregnancy) is sometimes associated with coeliac disease. Some women are diagnosed during pregnancy because their bowel cannot absorb enough iron and vitamins to keep up with the demand of being pregnant, making them severely anaemic, Babies who are small for their age in the womb (intrauterine growth retardation) are more frequently born to mothers with coeliac disease. If left untreated, coeliac disease can lead to anaemia, bone disease and, rarely, some forms of cancer. The most important treatment at present is avoiding all food that contains gluten. This usually results in improvement, or even disappearance, of the damage to the lining of the bowel. However, the damage will recur if gluten is re-introduced into the diet. Although coeliac disease is not preventable, sticking to a gluten-free diet can reverse damage to the small intestine. This requires considerable discipline. There is a need to find a medicament with a low risk of adverse effects that will enable patients to eat a normal diet, and avoid mineral and vitamin deficiencies and other conditions associated with Coeliac disease. Tropical sprue is a digestive problem that occurs in the tropics and subtropics. People with tropical sprue do not absorb nutrients properly, especially vitamin B12 and folic acid. Diarrhea is the main symptom of tropical sprue; people who eat a lot of fatty foods may experience more severe diarrhea than those on diets low in fat. Other symptoms include cramps, nausea, weight loss, gas and indigestion. Tropical sprue affects about one of every 1 million people and occurs from about 30 degrees north of the equator to 30 degrees south of it. It is more common in certain countries, including India, Haiti, Cuba, Puerto Rico and the Dominican Republic, It is rare or absent in Africa, the Bahamas and Jamaica. The condition afflicts residents of the affected countries as well as travelers, though usually it affects only travelers who stay for six months or longer. The cause of tropical sprue has not been identified, but it is probably due to a combination of factors, including infection and poor nutrition,'that act together to damage the lining of the small intestine, making it less able to absorb nutrients. Diagnosis of tropical sprue can be complicated, because many conditions have similar symptoms. Stool and blood tests are performed to rule out other causes of diarrhea. If these are negative and the patient has lived in the tropics for an extended period of time, then tropical sprue is a potential cause for the illness. A biopsy may be performed to examine the villi for the typical flattening of the villi in the small intestine. Certain blood tests also can aid in the diagnosis of tropical sprue. Because the disease blacks certain vitamins and minerals from being absorbed, low levels of albumin, calcium or vitamins D, A, K and E may be observed. The patient may also have anemia due to vitamin B12 and folate deficiencies. In addition, stool specimens may demonstrate an excess amount of fat. Treatment is usually three to six months of antibiotics and folic acid (also called folate) supplements. People with vitamin B12 deficiency will receive vitamin supplements as well. Aspects of the Invention One aspect of the invention is the use of an antibody that specifically binds MAdCAM for the manufacture of a medicament for the treatment of coeliac disease and/or tropical sprue. Another aspect of the invention is a method of treatment of coeliac disease and/or tropical sprue, preferably coeliac disease, using a therapeutically effective amount of an anti-MAdCAM antibody. Another aspect of the invention is the use of an anti-o^p? integrin antibody for the manufacture of a medicament for the treatment of coeliac disease and/or tropical sprue, preferably coeliac disease. Preferably, the anti-oc4p7 integrin antibody is humanised Act-1, also called MLN02. Another aspect of the invention is a method of treatment of coeliac disease and/or tropical sprue, preferably coeliac disease, using a therapeutically effective amount of an anti-a4p7 antibody, preferably MLN02. Another aspect of the invention is the use of an inhibitor of MAdCAM-a4p7 integrin-mediated adhesion for the manufacture of a medicament for the treatment of coeliac disease and/or tropical sprue. Still another aspect of the invention is a method of treatment of coeliac disease and/or tropical sprue, using a therapeutically effective amount of an inhibitor of MAdCAM-a4p7 integrin-mediated adhesion. Preferably the anti-MAdCAM antibody or antigen-binding portion thereof used in the invention specifically binds MAdCAM. Even more preferably, at least the CDR sequences of said antibody are human CDR sequences, or an antigen-binding portion of a human antibody. Preferably the antibody is a human antibody, more preferably a human monoclonal antibody or antigen-binding portion thereof, even more preferably an antibody or antigen-binding portion thereof that acts as a MAdCAM antagonist. Preferably, the antibody or portion possesses at least one of the following properties: (a) binds to human cells; (b) has a selectivity for MAdCAM over VCAM or fibronectin of at least 100 fold; (c) binds to human MAdCAM with a Kd of 3 x 10-10 M or less; or (d) inhibits the binding of a4B7 expressing cells to human MAdCAM. (e) inhibits the recruitment of lymphocytes to gastrointestinal lymphoid tissue. Preferably, the antibody or antigen-binding portion inhibits binding of human MAdCAM to 0^7, and has at least one of the following properties: (a) cross-competes with a reference antibody for binding to MAdCAM; (b) competes with a reference antibody for binding to MAdCAM; (c) binds to the same epitope of MAdCAM as a reference antibody; (d) binds to MAdCAM with substantially the same Kd as a reference antibody; (e) binds to MAdCAM with substantially the same off rate as a reference antibody; wherein the reference antibody is selected from the group consisting of: monoclonal antibody 1.7.2, monoclonal antibody 1.8.2, monoclonal antibody 6.14.2, monoclonal antibody 6.22.2, monoclonal antibody 6.34.2, monoclonal antibody 6.67.1, monoclonal antibody 6.73.2, monoclonal antibody 6.77.1, monoclonal antibody 7.16.6, monoclonal antibody 7.20.5, monoclonal antibody 7.26.4, monoclonal antibody 9.8.2, monoclonal antibody 6.22.2-mod, monoclonal antibody 6.34.2-mod, monoclonal antibody 6,67.1-mod, monoclonal antibody 6.77.1-mod and monoclonal antibody 7.26.4-mod. In another aspect of the invention the heavy chain variable region, the light chain variable region or both of the anti-MAdCAM antibody are at least 90% identical in amino acid sequence to the corresponding region or regions of a monoclonal antibody selected from the group consisting of: monoclonal antibody 1.7.2, monoclonal antibody 1.8.2, monoclonal antibody 6.14.2, monoclonal antibody 6.22.2, monoclonal antibody 6.34.2, monoclonal antibody 6.67.1, monoclonal antibody 6.73.2, monoclonal antibody 6.77.1, monoclonal antibody 7.16.6, monoclonal antibody 7.20.5, monoclonal antibody 7.26.4 monoclonal antibody 9.8.2, monoclonal antibody 6.22.2-mod, monoclonal antibody 6.34.2-mod, monoclonal antibody 6.67.1-mod, monoclonal antibody 6.77.1-mod and monoclonal antibody 7.26.4-mod. Preferably the antibody is selected from the group consisting of: (a) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 2 and SEQ ID NO: 4, without the signal sequences; {b) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 6 and SEQ ID NO: 8, without the signal sequences; (c) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 10 and SEQ ID NO: 12, without the signal sequences; (d) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 14 and SEQ ID NO: 16, without the signal sequences; (e) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 18 and SEQ ID NO: 20, without the signal sequences; (f) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 22 and SEQ ID NO: 24, without the signal sequences; (g) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 26 and SEQ ID NO: 28, without the signal sequences; (h) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 30 and SEQ ID NO: 32, without the signal sequences; (i) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 34 and SEQ ID NO: 36, without the signal sequences; (j) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 38 and SEQ ID NO: 40, without the signal sequences; (k) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 42 and SEQ ID NO: 44, without the signal sequences; (I) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 46 and SEQ ID NO: 48, without the signal sequences; (m) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 52 and SEQ ID NO: 54, without the signal sequences; (n) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 56 and SEQ ID NO: 58, without the signal sequences; (o) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 60 and SEQ ID NO: 62, without the signal sequences; (p) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 64 and SEQ ID NO: 66, without the signal sequences; and (q) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 42 and SEQ ID NO: 68, without the signal sequences. In another aspect of the invention, the monoclonal antibody or an antigen-binding portion thereof is selected from the following antibodies: (a) the heavy chain comprises the heavy chain CDR1, CDR2 and CDR3 amino acid sequences of a reference antibody selected from the group consisting of: 1.7.2, 1.8.2, 6.14.2, 6.22.2, 6.34.2, 6.67.1, 6.73.2, 6.77.1, 7.16.6, 7.20.5, 7.26.4, 9.8.2, 6.22.2-mod, 6.34.2-mod, 6.67.1-mod, 6.77.1-mod and 7.26.4- mod (b) the light chain comprises the light chain CDR1, CDR2 and CDR3 amino acid sequences of a reference antibody selected from the group consisting of: 1.7.2, 1.8.2, 6.14.2, 6.22.2, 6.34.2, 6,67.1, 6.73,2, 6.77.1, 7.16.6, 7.20.5, 7.26.4, 9.8.2, 6.22.2-mod, 6.34.2-mod, 6.67.1-mod, 6.77.1-mod and 7.26.4- mod (c) the antibody comprises a heavy chain of (a) and a light chain of (b); and (d) the antibody of (c) wherein the heavy chain and light chain CDR amino acid sequences are selected from the same reference antibody. In another aspect of the invention, the monoclonal antibody or antigen-binding portion comprises: (a) a heavy chain comprising the heavy chain variable region amino acid sequence of an antibody selected from the group consisting of: 1.7.2 (SEQ ID NO: 2); 1.8.2 (SEQ ID NO: 6); 6.14.2 (SEQ ID NO: 10); 6.22.2 (SEQ ID NO: 14); 6.34.2 (SEQ ID NO: 18); 6.67.1 (SEQ ID NO: 22); 6.73.2 (SEQ ID NO: 26); 6.77.1 (SEQ ID NO: 30); 7.16.6 (SEQ ID NO: 34); 7,20.5 {SEQ ID NO: 38); 7.26.4 (SEQ ID NO: 42); and 9.8.2 (SEQ ID NO: 46); 6.22.2-mod (SEQ ID NO: 52); 6,34.2-mod (SEQ ID NO: 56); 6.67.1-mod (SEQ ID NO: 60); 6.77.1-mod (SEQ ID NO: 64); and 7.26.4-mod (SEQ ID NO: 42); (b) a light chain comprising the light chain variable region amino acid sequence of an antibody selected from the group consisting of: 1.7,2 (SEQ ID NO: 4); 1.8.2 (SEQ ID NO: 8); 6,14.2 (SEQ ID NO: 12); 6.22.2 (SEQ ID NO: 16); 6.34.2 (SEQ ID NO: 20); 6.67.1 (SEQ ID NO: 24); 6.73.2 (SEQ ID NO: 28); 6.77.1 (SEQ ID NO: 32); 7.16.6 (SEQ ID NO: 36); 7.20.5 (SEQ ID NO: 40); 7.26.4 (SEQ ID NO: 44); and 9.8.2 (SEQ ID NO: 48); 6.22.2-mod (SEQ ID NO: 54); 6.34.2-mod (SEQ ID NO: 58); 6.67.1-mod {SEQ ID NO; 62); 6.77.1-mod (SEQ ID NO: 66); and 7,26.4-mod (SEQ ID NO: 68); or (c) the heavy chain of (a) and the light chain of (b). Another aspect of the invention is the use of the heavy and/or light chain of said anti-MAdCAM antibody or the variable region or other antigen-binding portion thereof, or nucleic acid molecules encoding any of the foregoing and a pharmaceutically acceptable carrier. This aspect of the invention includes the use of fragments of any of the foregoing antibodies, Including but not limited to Fab fragments, F(ab')2 fragments, single-chain Fv (scFv) fragments. Preferably, the anti-MAdCAM antibody is a human inhibitory anti-MAdCAM antibody selected from 1.7.2, 1.8.2, 6.14.2, 6.22.2, 6.34.2, 6.67.1, 6.73.2, 6.77.1, 7.16.6, 7.20.5, 7.26.4, 9.8.2, 6.22.2-mod, 6.34.2-mod, 6.67.1-mod, 6.77.1-mod or 7.26.4-mod as described in WO 2005/067620. Preferably, the anti-MAdCAM antibody comprises a light chain comprising an amino acid sequence selected from SEQ ID NO: 4, 8,12, 16, 20, 24, 28, 32, 36, 40, 44, 48, 54, 58, 62, 66 or 68 as shown in WO 2005/067620 (with or without the signal sequence) or the variable region of any one of said amino acid sequences, or one or more CDRs from these amino acid sequences. The antt-MAdCAM antibody preferably comprises a heavy chain comprising an amino acid sequence selected from SEQ ID NO: 2, 6, 10,14, 18, 22, 26, 30, 34, 38, 42, 46, 52, 56, 60 or 64 as shown in WO 2005/067620 (with or without the signal sequence) or the amino acid sequence of the variable region, or of one or more CDRs from said amino acid sequences. The anti-MAdCAM antibody preferably is a human anti-MAdCAM antibody comprising the amino acid sequence from the beginning of the CDR1 to the end of the CDR3 of any one of the above-mentioned sequences. The anti-MAdCAM antibody used in the invention can also be an anti-MAdCAM antibody comprising one or more FR regions of any of the above-mentioned sequences. The anti-MAdCAM antibody used in the invention can also include an anti-MAdCAM antibody comprising one of the afore-mentioned amino acid sequences in which one or more modifications have been made. For example, cysteines In the antibody, which may be chemically reactive, are substituted with another residue, such as, without limitation, alanine or serine. The substitution can be at a non-canonical cysteine or at a canonical cysteine. The substitution can be made in a CDR or framework region of a variable domain or in the constant domain of an antibody. An amino acid substitution may also be made to eliminate potential proteolytic sites in the antibody. Such sites may occur in a CDR or framework region of a variable domain or in the constant domain of an antibody. Substitution of cysteine residues and removal of proteolytic sites may decrease the heterogeneity in the antibody product. Asparagine-glycine pairs, which form potential deamidation sites, may be eliminated by altering one or both of the residues. An amino acid substitution may be made to add or to remove potential giycosylation sites in the variable region of an antibody used in the invention. The C-terminal lysine of the heavy chain of the anti-MAdCAM antibody used the invention may be cleaved. The heavy and light chains of the anti-MAdCAM antibodies may optionally include a signal sequence. Twelve preferred inhibitory human anti-MAdCAM monoclonal antibodies for use in the invention (1.7.2, 1.8.2, 6.14,2, 6.22.2, 6.34.2, 6.67.1, 6.73.2, 6.77.1, 7.16.6, 7.20.5, 7.26.4 and 9.8.2) are described in detail in WO 2005/067620, herein incorporated fully by reference. Class and Subclass of anti-MAdCAM Antibodies The antibody may be an IgG, an IgM, an IgE, an IgA or an IgD molecule. Preferably the antibody is an IgG class and is an IgG-i, lgG2, lgG3 or IgG,, subclass. More preferably, the anti-MAdCAM antibody is subclass lgG2 or lgG4. More preferably, the anti-MAdCAM antibody is the same class and subclass as antibody 1.7.2, 1.8.2, 7.16.6, 7.20,5, 7.26.4, 6,22.2-mod, 6.34.2-mod, 6.67.1-mod, 6.77.1-mod or 7.26.4-mod which is lgG2, or 6.14.2, 6,22.2, 6.34.2, 6.67.1, 6.73.2, 6.77.1 or 9.8.2, which is IgG,, as described in W02005/067620. The class and subclass of anti-MAdCAM antibodies may be determined by any method known in the art. In general, the class and subclass of an antibody may be determined using antibodies that are specific for a particular class and subclass of antibody. Such antibodies are available commercially. ELISA, Western Blot as well as other techniques can determine the class and subclass. Alternatively, the class and subclass may be determined by sequencing all or a portion of the constant domains of the heavy and/or light chains of the antibodies, comparing their amino acid sequences to the known amino acid sequences of various classes and subclasses of immunoglobulins, and determining the class and subclass of the antibodies as the class showing the highest sequence identity. Species and Molecule Selectivity The anti-WIAdCAM antibody used in the invention demonstrates both species and molecule selectivity. The anti-MAdCAM antibody may bind to human, cynomolgus or dog MAdCAM. Other anti-MAdCAM antibodies used in the invention do not bind to a New World monkey species such as a marmoset. One may determine the species selectivity for the anti-MAdCAM antibody using methods well known in the art. For instance, one may determine species selectivity using Western blot, FAGS, ELISA or immunohistochemistry. In a preferred embodiment, one may determine the species selectivity using immunohistochemistry. An anti-MAdCAM antibody used in the invention that specifically binds MAdCAM has selectivity for MAdCAM over VCAM, fibronectin or any other antigen that is at least 10 fold, preferably at least 20, 30, 40, 50, 60, 70, 80 or 90 fold, most preferably at least 100 fold. Preferably the anti-MAdCAM antibody does not exhibit any appreciable binding to VCAM, fibronectin or any other antigen other than MAdCAM. One may determine the selectivity of the anti-MAdCAM antibody for MAdCAM using methods well known in the art following the teachings of the specification. For instance, one may determine the selectivity using Western blot, FACS, ELISA, or immunohistachemistry, Binding Affinity of anti-MAdCAM antibodies to MAdCAM The anti-MAdCAM antibodies used in the invention preferably specifically bind to MAdCAM 'with high affinity. One anti-MAdCAM antibody used in the invention specifically binds to MAdCAM with a Kd of 3 x 10"8 M or less, as measured by surface plasmon resonance, such as BIAcore. Preferably, the antibody specifically binds to MAdCAM with a Kd of 1 x 10"B or less or 1 x 10"9 M or less. More preferably, the antibody specifically binds to MAdCAM with a K part of a larger polypeptide chain, may covalently link the CDR(s) to another polypeptide chain, or may incorporate the CDR(s) noncovalently. The CDRs permit the immunoadhesin to specifically bind to a particular antigen of interest. An antibody may have one or more binding sites. If there is more than one binding site, the binding sites may be identical to one another or may be different. For instance, a naturally-occurring immunoglobulin has two identical binding sites, a single-chain antibody or Fab fragment has one binding site, while a "bispecific" or "bifunctional" antibody (diabody) has two different binding sites. An "isolated antibody" is an antibody that (1) is not associated with naturally-associated components, including other naturally-associated antibodies, that accompany it in its native state, (2) is free of other proteins from the same species, (3) is expressed by a cell from a different species, or (4) does not occur in nature. Examples of isolated antibodies include an anti-MAdCAM antibody that has been affinity purified using MAdCAM, an anti-MAdCAM antibody that has been produced by a hybridoma or other cell line in vitro, and a human anti-MAdCAM antibody derived from a transgenic mammal or plant. As used herein, the term "human antibody" means an antibody in which the variable and constant region sequences are human sequences, The term encompasses antibodies with sequences derived from human genes, but which have been changed, e.g., to decrease possible immunogenicity, increase affinity, eliminate cysteines or glycosylation sites that might cause undesirable folding, etc. The term encompasses such antibodies produced recombinantly in non-human cells which might impart glycosylation. not typical of human cells. The term also emcompasses antibodies which have been raised in a transgenic mouse which comprises some or all of the human immunoglobulin heavy and light chain loci. In one aspect, the invention provides a humanized antibody. In some embodiments, the humanized antibody is an antibody that Is derived from a non-human species, in which certain amino acids In the framework and constant domains of the heavy and light chains have been mutated so as to avoid or abrogate an immune response in humans. In some embodiments, a humanized antibody may be produced by fusing the constant domains from a human antibody to the variable domains of a non-human species. Examples of how to make humanized antibodies may be found in United States Patent Nos. 6,054,297, 5,886,152 and 5,877,293. In some embodiments, a humanized anti-MAdCAM antibody of the invention comprises the amino acid sequence of one or more framework regions of one or more human anti-MAdCAM antibodies of the invention. In another aspect, the invention includes the use of a "chimeric antibody". In some embodiments the chimeric antibody refers to an antibody that contains one or more regions from one antibody and one or more regions from one or more other antibodies. In a preferred embodiment, one or more of the CDRs are derived from a human anti-MAdCAM antibody of the invention. In a more preferred embodiment, all of the CDRs are derived from a human anti-MAdCAM antibody of the invention. In another preferred embodiment, the CDRs from more than one human anti-MAdCAM antibody of the invention are mixed and matched in a chimeric antibody. For instance, a chimeric antibody may comprise a CDRI from the light chain of a first human anti-MAdCAM antibody may be combined with CDR2 and CDRS from the light chain of a second human anti-MAdCAM antibody, and the CDRs from the heavy chain may be derived from a third anti-MAdCAM antibody. Further, the framework regions may be derived from one of the same anti-MAdCAM antibodies, from one or more different antibodies, such as a human antibody, or from a humanized antibody. A "neutralizing antibody," "an inhibitory antibody" or antagonist antibody is an antibody that inhibits the binding of a4fS7 or a4p7-expressing cells, or any other cognate ligand or cognate ligand-expressing cells, to MAdCAM by at least about 20%. In a preferred embodiment, the antibody reduces inhibits the binding of x^integrin or a4p7-expressing cells to MAdCAM by at least 40%, more preferably by 60%, even more areferably by 80%, 85%, 90%, 95% or 100%. The binding reduction may be measured by any means known to one, of ordinary skill in the art, for example, as measured in an in vitro competitive binding assay. An example of measuring the reduction in binding of a^r-expressing cells to MAdCAM is presented in Example I. Fragments or analogs of antibodies can be readily prepared by those of ordinary skill in the art following the teachings of this specification. Preferred amino- and carboxy-termini of fragments or analogs occur near boundaries of functional domains. Structural and functional domains can be identified by comparison of the nucleotide and/or amino acid sequence data to public or proprietary sequence databases. Preferably, computerized comparison methods are used to identify sequence motifs or predicted protein conformation domains that occur in other proteins of known structure and/or function. Methods to identify protein sequences that fold into a known three-dimensional structure are known (Bowie et al. Science, 253:164 (1991)). The term "koff" refers to the off rate constant for dissociation of an antibody from the antibody/antigen complex. The term "K/ refers to the dissociation constant of a particular antibody-antigen interaction. An antibody is said to bind an antigen when the dissociation constant is £1 uM, preferably s 100 nM and most preferably & 10 nM. The term "epitope" includes any protein determinant capable of specific binding to an immunoglobulin or T-cell receptor or otherwise interacting with a molecule. Epitopic determinants usually consist of chemically active surface groupings of molecules such as amino acids or carbohydrate side chains and usually have specific three dimensional structural characteristics, as well as specific charge characteristics. An epitope may be "linear" or "conformational." In a linear epitope, all of the points of interaction between the protein and the interacting molecule (such as an antibody) occur linearally along the primary amino acid sequence of the protein. In a conformational epitope, the points of interaction Dccur across amino acid residues on the protein that are separated from one another. \s used herein, the twenty conventional amino acids and their abbreviations follow conventional usage. See Immunology - A Synthesis (2nd Edition, E.S. Golub and D.R. Gren, Eds., Sinauer Associates, Bunderland, Mass. (1991)), which is incorporated herein by reference. Stereoisomers (e.g., D-amino acids) of the twenty conventional amino acids, unnatural amino acids such as a-, a-dlsubstituted amino acids, N-alkyl amino acids, lactic acid, and other unconventional amino acids may also be suitable :omponents for polypeptides of the present invention. Examples of unconventional amino acids include; l-hydroxyproline, v-carboxyglutamate, e-N,N,N-trimethyllysine, e-N-acetyllysine, 0-phosphoserine, N-icetylserine, N-formylmethionine, 3-methylhistidine, 5-hydroxylysine, s-N-methylarginine, and other .imilar amino acids and imino acids (e.g., 4-hydroxyproline). In the polypeptide notation used herein, the sfthand direction is the amino terminal direction and the righthand direction is the carboxy-terminal iirection, in accordance with standard usage and convention. The term "polynucleotide" as referred to herein means a polymeric form of nucleotides of at least 10 bases in length, either ribonucleotides or deoxynucleotides or a modified form of either type of nucleotide. The term includes single and double stranded forms of DMA. The term "isolated polynucleotide" as used herein shall mean a polynucleotide of genomic, cDNA, or synthetic origin or some combination thereof, which by virtue of its origin the "isolated polynucleotide" (1) is not associated with all or a portion of a polynucleotide in which the "isolated polynucleotide" is found in nature, (2) is operably linked to a polynucleotide which it is not linked to in nature, or (3) does not occur in nature as part of a larger sequence. The term "oligonucleotide" referred to herein includes naturally occurring, and modified nucleotides linked together by naturally occurring, and non-naturally occurring oligonucieotide linkages. Oligonucleotides are a polynucleotide subset generally comprising a length of 200 bases or fewer, Preferably Oligonucleotides are 10 to 60 bases in length and most preferably 12, 13, 14, 15, 16, 17, 18, 19, or 20 to 40 bases in length. Oligonucleotides are usually single stranded, e.g., for probes; although Oligonucleotides may be double stranded, e.g., for use in the construction of a gene mutant. Oligonucleotides of the invention can be either sense or antisense Oligonucleotides. The term "naturally occurring nucleotides" referred to herein includes deoxyribonucleotides and ribonucieotides. The term "modified nucleotides" referred to herein includes nucleotides with modified or substituted sugar groups and the like. The term "oligonucleotide linkages" referred to herein includes Oligonucleotides linkages such as phosphorothioate, phosphorodithioate, phosphoroselenoate, phosphorodiselenoate, phosphoroanilothioate, phoshoraniladate, phosphoroamidate, and the like. See, e.g., LaPlanche et al., Nucl. Acids Res. 14:9081 (1986); Stec et al., J. Am. Chem. Sac. 106:6077(1984); Stein et al., Nucl. Acids Res., 16:3209(1988); Zon et al., Anti-Cancer Drug Design 6:539(1991); Zon et al., Oligonueleotldes and Analogues: A Practical Approach, pp. 87-108 (F. Eckstein, Ed., Oxford University Press, Oxford England(1991)); Stec et al., U.S. Patent No. 5,151,510; Uhlmann and Peyman, Chemical Reviews, 90:543(1990), the disclosures of which are hereby incorporated by reference. An oligonucleotide can include a label for detection, if desired. "Operably linked" sequences include both expression control sequences that are contiguous with the gene of interest and expression control sequences that act in trans or at a distance to control the gene of interest. The term "expression control sequence" as used herein refers to polynucleotide sequences which are necessary to effect the expression and processing of coding sequences to which they are ligated. Expression control sequences include appropriate transcription initiation, termination, promoter and enhancer sequences; efficient RNA processing signals such as splicing and polyadenylation signals; sequences that stabilize cytoplasmic mRNA; sequences that enhance translation efficiency (i.e., Kozak consensus sequence); sequences that enhance protein stability; and when desired, sequences that enhance protein secretion. The nature of such control sequences differs depending upon the host organism; in prokaryotes, such control sequences generally include promoter, ribosomal binding site, and transcription termination sequence; in eukaryotes, generally, such control sequences include promoters and transcription termination sequence. The term "control sequences" is intended to include, at a minimum, all components whose presence is essential for expression and processing, and can also include additional components whose presence is advantageous, for example, leader sequences and fusion partner sequences. The term "vector", as used herein, is intended to refer to a nucleic acid molecule capable of transporting another nucleic acid to which it has been linked. One type of vector is a "plasmid", which refers to a circular double stranded DNA loop into which additional DMA segments may be ligated. Another type of vector is a viral vector, wherein additional DNA segments may be ligated into the viral genome. Certain vectors are capable of autonomous replication in a host cell into which they are introduced (e.g., bacterial vectors having a bacterial origin of replication and episomal mammalian vectors). Other vectors (e.g., non-episomal mammalian vectors) can be integrated into the genome of a host cell upon introduction into the host cell, and thereby are replicated along with the host genome. Moreover, certain vectors are capable of directing the expression of genes to which they are operatively linked. Such vectors are referred to herein as "recombinant expression vectors" (or simply, "expression vectors"), In general, expression vectors of utility in recombinant DNA techniques are often in the form of plasmids. In the present specification, "plasmid" and "vector" may be used interchangeably as the plasmid is the most commonly used form of vector. However, the invention is intended to include such other forms of expression vectors, such as viral vectors (e.g., replication defective retroviruses, adenoviruses and adeno-associated viruses), which serve equivalent functions. The term "recombinant host cell" (or simply "host cell"), as used herein, is intended to refer to a cell into which a recombinant expression vector has been introduced. It should be understood that such terms are intended to refer not only to the particular subject cell but to the progeny of such a cell. Because certain modifications may occur in succeeding generations due to either mutation or environmental influences, such progeny may not, in fact, be identical to the parent cell, but are still included within the scope of the • term "host cell" as used herein. The term "selectively hybridize" referred to herein means to detectably and specifically bind. Polynucleotides, oligonucleotides and fragments thereof in accordance with the invention selectively hybridize to nucleic acid strands under hybridization and wash conditions that minimize appreciable amounts of detectable binding to nonspecific nucleic acids. "High stringency" or "highly stringent" conditions can be used to achieve selective hybridization conditions as known in the art and discussed herein. An example of "high stringency" or "highly stringent" conditions is a method of incubating a polynucleotide with another polynucleotide, wherein one polynucleotlde may be affixed to a solid surface such as a membrane, in a hybridization buffer of 6X SSPE or SSC, 50% formamide, 5X Denhardt's reagent, 0.5% SDS, 100 ug/ml denatured, fragmented salmon sperm DNA at a hybridization temperature of 42°C for 12-16 hours, followed by twice washing at 55°C using a wash buffer of 1X SSC, 0.5% SDS. See also Sambrook et al., supra, pp. 9.50-9.55. The term "percent sequence identity" in the context of nucleotide sequences refers to the residues in two sequences which are the same when aligned for maximum correspondence. The length of sequence identity comparison may be over a stretch of at least about nine nucleotides, usually at least about 18 nucleotides, more usually at least about 24 nucleotides, typically at least about 26 nucleotides, more typically at least about 32 nucleotides, and preferably at least about 36, 48 or more nucleotides. There are a number of different algorithms known in the art which can be used to measure nucleotide sequence identity. For instance, polynucleotide sequences can be compared using FASTA, Gap or Bestfit, which are programs in Wisconsin Package Version 10.3, Accelrys, San Diego, CA. FASTA, which includes, e.g., the programs FASTA2 and FASTA3, provides alignments and percent sequence identity of the regions of the best overlap between the query and search sequences (Pearson, Methods Enzymol., 183: 63-98 (1990); Pearson, Methods Mol. Biot., 132:185-219 (2000); Pearson, Methods Enzymol., 266: 227-258 (1996); Pearson, J. Mol. Biol., 276: 71-84 (1998); herein incorporated by reference). Unless otherwise specified, default parameters for a particular program or algorithm are used. For Instance, percent sequence identity between nucleotide sequences can be determined using FASTA with its default parameters (a word size of 6 and the NOPAM factor for the scoring matrix) or using Gap with its default parameters as provided In Wisconsin Package Version 10.3, herein incorporated by reference. A reference to a nucleotide sequence encompasses its complement unless otherwise specified. Thus, a reference to a nucleic acid molecule having a particular sequence should be understood to encompass its complementary strand, with its complementary sequence. In the molecular biology art, researchers use the terms "percent sequence identity", "percent sequence similarity" and "percent sequence homology" interchangeably. In this application, these terms shall have the same meaning with respect to nucleotide sequences only. The term "substantial similarity" or "substantial sequence similarity," when referring to a nucleic acid or fragment thereof, indicates that, when optimally aligned with appropriate nucleotide insertions or deletions with another nucleic acid (or its complementary strand), there is nucleotide sequence identity in at least about 85%, preferably at least about 90%, and more preferably at least about 95%, 96%, 97%, 98% or 99% of the nucleotide bases, as measured by any well-known algorithm of sequence identity, such as FASTA, BLAST or Gap, as discussed above. As applied to polypeptides, the term "substantial identity" means that two peptide sequences, when optimally aligned, such as by the programs GAP or BESTFIT using default gap weights, share at least 75% or 80% sequence identity, preferably at least 90% or 95% sequence identity, even more preferably at least 98% or 99% sequence identity. Preferably, residue positions that are not identical differ by conservative amino acid substitutions. A "conservative amino acid substitution" is one in which an amino acid residue is substituted by another amino acid residue having a side chain (R group) with similar chemical properties (e.g., charge or hydrophobicity). In general, a conservative amino acid substitution will not substantially change the functional properties of a protein. In cases where two or more amino acid sequences differ from each other by conservative substitutions, the percent sequence identity or degree of similarity may be adjusted upwards to correct for the conservative nature of the substitution. Means for making this adjustment are well-known to those of skill in the art. See, e.g., Pearson, Methods Mol. 6/b/., 24: 307-31 (1994), herein incorporated by reference. Examples of groups of amino acids that have side chains with similar chemical properties include 1) aliphatic side chains: glycine, alanine, valine, leucine and isoleucine; 2) aliphatic-hydroxyl side chains: serine and threonine; 3) amide-containing side chains: asparagine and glutamine; 4) aromatic side chains: phenylalanine, tyrosine, and tryptophan; 5) basic side chains: lysine, arginine, and histidine; and 6) sulfur-containing side chains are cysteine and methionine. Preferred conservative amino acids substitution groups are: valine-leucine-istileucine, phenylalanine-tyrosine, lysine-arginine, alanine-valine, glutamate-aspartate, and asparagine-glutamine. Alternatively, a conservative replacement is any change having a positive value in the PAM250 log-likelihood matrix disclosed in Gonnet et al., Science, 256: 1443-45 (1992), herein incorporated by reference. A "moderately conservative" replacement is any change having a nonnegative value in the PAM250 log-likelihood matrix. Sequence similarity for polypeptides Is typically measured using sequence analysis software. Protein analysis software matches similar sequences using measures of similarity assigned to various substitutions, deletions and other modifications, including conservative amino acid substitutions. For instance, GCG contains programs such as "Gap" and "Bestfit" which can be used with default parameters to determine sequence homology or sequence identity between closely related polypeptides, such as homologous polypeptides from different species of organisms or. between a wild type protein and a mutein thereof. See, e.g., Wisconsin package Version 10.3. Polypeptide sequences also can be compared using FASTA using default or recommended parameters, a program in Wisconsin package Version 10.3. FASTA (e.g., FASTA2 and FASTA3) provides alignments and percent sequence identity of the regions of the best overlap between the query and search sequences (Pearson (1990); Pearson (2000)). Another preferred algorithm when comparing a sequence of the invention to a database containing a large number of sequences from different organisms is the computer program BLAST, especially blastp ortblastn, using default parameters. See, e.g., Altschul et al., J. Mol. Bio]. 215:403-410 (1990); Altschul et al., Nucleic Acids Res. 25:3389-402 (1997); herein incorporated by reference. The length of polypeptide sequences compared for homology will generally be at least about 16 amino acid residues, usually at least about 20 residues, more usually at least about 24 residues, typically at least about 28 residues, and preferably more than about 35 residues. When searching a database containing sequences from a large number of different organisms, it is preferable to compare amino acid sequences. As used herein, the terms "label" or "labeled" refers to incorporation of another molecule in the antibody. In one embodiment, the label is a detectable marker, e.g., incorporation of a radiolabeled amino acid or attachment to a polypeptide of biotinyl moieties that can be detected by marked avidin (e.g., streptavidin containing a fluorescent marker or enzymatic activity that can be detected by optical or colorimetric methods). In another embodiment, the label or marker can be therapeutic, e.g., a drug conjugate or toxin. Various methods of labeling polypeptides and glycoproteins are known in the art and may be used. Examples of labels for polypeptides include, but are not limited to, the following: radioisotopes or radionuclides (e.g., 3H, 14C, 15N, 35S, 90Y, 99Tc, 111ln, 1251,131I), fluorescent labels {e.g., FITC, rhodamine, lanthanide phosphors), enzymatic labels (e.g., horseradish peroxidase, p-galactosidase, luciferase, alkaline phosphatase), chemiluminescent markers, biotinyl groups, predetermined polypeptide epitopes recognized by a secondary reporter (e.g., leucine zipper pair sequences, binding sites for secondary antibodies, metal binding domains, epitope tags), magnetic agents, such as gadolinium chelates, toxins such as pertussis toxin, taxol, cytochalasin B, gramicidin D, ethidium bromide, emetine, mitomycin, etoposide, tenoposide, vincristine, vinblastine, colchicin, doxorubicin, daunorubicin, dihydroxy anthracin dione, mitoxantrone, mithramycin, actinomycin D, 1-dehydrotestosterone, glucocorticoids, procaine, tetracaine, lidocaine, propranolol, and puromycin and analogs or homologs thereof. In some embodiments, labels are attached by spacer arms of various lengths to reduce potential steric hindrance. Claims 1. Use of an anti-MAdCAM antibody or antigen binding portion thereof for the manufacture of a medicament for the treatment of coeliac disease and/or tropical sprue, 2. The use of claim 1, wherein the medicament is for the treatment of coeliac disease, 3. The use of claim 1 or claim 2, wherein the anti-MAdCAM antibody is a human monoclonal antiBody. 4. The use of claim 3, wherein the antibody or portion possesses at least one of the following properties: (a) binds to human cells; (b) has a selectivity for MAdCAM over VCAM or fibronectin of at least 100 fold; (c) binds to human MAdCAM with a Kd of 3 x 10-10 M or less; or (d) inhibits the binding of cup? expressing cells to human MAdCAM, (e) inhibits the recruitment of lymphocytes to gastrointestinal lymphoid tissue. 5. The use according to any of claims 1 to 4, wherein said antibody or antigen-binding portion inhibits binding of human MAdCAM to a4p7, and wherein the antibody or portion thereof has at least one of the following properties: (a) cross-competes with a reference antibody for binding to MAdCAM; (b) competes with a reference antibody for binding to MAdCAM; (c) binds to the same epitope of MAdCAM as a reference antibody; (d) binds to MAdCAM with substantially the same Kd as a reference antibody; (e) binds to MAdCAM with substantially the same off rate as a reference antibody; wherein the reference antibody is selected from the group consisting of: monoclonal antibody 1.7.2, monoclonal antibody 1.8.2, monoclonal antibody 6.14.2, monoclonal antibody. 6.22.2, monoclonal antibody 6.34.2, monoclonal antibody 6.67.1, monoclonal antibody 6.73.2, monoclonal antibody 6.77.1, monoclonal antibody 7.16.6, monoclonal antibody 7.20.5, monoclonal antibody 7.26.4, monoclonal antibody 9.8.2, monoclonal antibody 6.22.2-mod, monoclonal antibody 6.34.2-mod, monoclonal antibody 6.67.1-mod, monoclonal antibody 6.77.1-mod and monoclonal antibody 7.26.4-mod, 6. The use according to any of claims 1 to 5, wherein the heavy chain variable region, the light chain variable region or both of the anti-MAdCAM antibody are at least 90% identical in amino acid sequence to the corresponding region or regions of a monoclonal antibody selected from the group consisting of: monoclonal antibody 1.7.2, monoclonal antibody 1.8.2, monoclonal antibody 6.14.2, monoclonal antibody 6.22.2, monoclonal antibody 6.34.2, monoclonal antibody 6.67.1, monoclonal antibody 6.73.2, monoclonal antibody 6.77.1, monoclonal antibody 7,16.6, monoclonal antibody 7.20.5, monoclonal antibody 7.26.4 monoclonal antibody 9.8.2, monoclonal antibody 6.22.2-mod, monoclonal antibody 6.34.2-mod, monoclonal antibody 6.67.1-mod, monoclonal antibody 6.77.1-mod and monoclonal antibody 7.26.4-mod. 7. The use according to any of claims 1 to 6, wherein the antibody is selected from the group consisting of: (a) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 2 and SEQ ID NO: 4, without the signal sequences; (b) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 6 and SEQ ID NO: 8, without the signal sequences; (c) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 10 and SEQ ID NO: 12, without the signal sequences; (d) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 14 and SEQ ID NO: 16, without the signal sequences; (e) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 18 and SEQ ID NO: 20, without the signal sequences; (f) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 22 and SEQ ID NO: 24, without the signal sequences; (g) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 26 and SEQ ID NO: 28, without the signal sequences; (h) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 30 and SEQ ID NO: 32, without the signal sequences; (i) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 34 and SEQ ID NO: 36, without the signal sequences; 0) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 38 and SEQ ID NO: 40, without the signal sequences; (k) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 42 and SEQ ID NO: 44, without the signal sequences; (I) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 46 and SEQ ID NO: 48, without the signal sequences; (m) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 52 and SEQ ID NO: 54, without the signal sequences; (n) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 56 and SEQ ID NO: 58, without the signal sequences; (o) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 60 and SEQ ID NO: 62, without the signal sequences; (p) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 64 and SEQ ID NO: 66, without the signal sequences; and (q) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 42 and SEQ ID NO: 68, without the signal sequences. 8. The use according to any of claims 1 to 7, wherein the heavy chain C-terminal lysine is cleaved from the anti-MAdCAM antibody. 9. The use according to any of claims 1 to 8, wherein the monoclonal antibody or an antigen-binding portion thereof is selected from the following antibodies: (a) the heavy chain comprises the heavy chain CDR1, CDR2 and CDR3 amino acid sequences of a reference antibody selected from the group consisting of; 1.7.2, 1.8.2, 6.14.2, 6.22.2, 6.34.2, 6.67.1, 6.73.2, 6.77.1, 7.16.6, 7.20.5, 7.26.4, 9.8.2, 6.22.2-mod, 6.34.2-mod, 6.67.1-mod, 6.77.1-mod and 7.26.4- mod (b) the light chain comprises the light chain CDR1, CDR2 and CDR3 amino acid sequences of a reference antibody selected from the group consisting of: 1.7.2, 1.8.2, 6.14.2, 6.22.2, 6.34.2," 6.67.1, 6.73.2, 6.77.1, 7.16.6, 7.20.5, 7.26.4, 9.8.2, 6.22.2-mod, 6.34.2-mod, 6.67.1-mod, 6.77.1-mod and 7.26.4- mod (c) the antibody comprises a heavy chain of (a) and a light chain of {b); and (d) the antibody of (c) wherein the heavy chain and light chain CDR amino acid sequences are selected from the same reference antibody. 10. The use of any of claims 1 to 9, wherein the monoclonal antibody or antigen-binding portion comprises: (a) a heavy chain comprising the heavy chain variable region amino acid sequence of an antibody selected from the group consisting of: 1.7.2 (SEQ ID NO: 2); 1.8.2 (SEQ ID NO: 6); 6.14.2 (SEQ ID NO: 10); 6.22.2 (SEQ ID NO: 14); 6.34.2 (SEQ ID NO: 18); 6.67.1 (SEQ ID NO: 22); 6.73.2 (SEQ ID NO: 26); 6.77.1 (SEQ ID NO: 30); 7.16.6 (SEQ ID NO: 34); 7.20.5 (SEQ ID NO: 38); 7.26.4 (SEQ ID NO: 42); and 9.8.2 (SEQ ID NO: 46); 6.22.2-mod (SEQ ID NO: 52); 6.34.2-mod (SEQ ID NO: 56); 6.67.1-mod (SEQ ID NO: 60); 6.77.1-mod (SEQ ID NO: 64); and 7.26.4-mod (SEQ ID NO: 42); (b) a light chain comprising the light chain variable region amino acid sequence of an antibody selected from the group consisting of: 1.7.2 (SEQ ID NO: 4); 1.8.2 (SEQ ID NO: 8); 6.14.2 (SEQ ID NO: 12); 6.22.2 (SEQ ID NO: 18); 6.34.2 (SEQ ID NO: 20); 6.67.1 (SEQ ID NO: 24); 6.73.2 (SEQ ID NO: 28); 6.77.1 (SEQ ID NO: 32); 7.16.6 (SEQ ID NO: 36); 7.20.5 (SEQ ID NO: 40); 7.26.4 (SEQ ID NO: 44); and 9.8.2 (SEQ ID NO: 48); 6.22.2-mod (SEQ ID NO: 54); 6.34.2-mod (SEQ ID NO: 58); 6.67.1-mod (SEQ ID NO: 62); 6.77.1-mod (SEQ ID NO: 66); and 7.26.4-mod (SEQ ID NO: 68); or (c) the heavy chain of (a) and the light chain of (b). 11. Use of an anti-o^By integrin antibody or antigen binding portion thereof for the manufacture of a medicament for the treatment of coeliac disease and/or tropical sprue.