Development of anti-human colonic mucin monoclonal antibodies. Characterization of multiple colonic mucin species.

Podolsky, Daniel K.; Fournier, Deborah A.; Lynch, Kathy E.

doi:10.1172/jci112428

Cited by 43 publications

(14 citation statements)

References 35 publications

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“…Samples of colonic and small intestinal mucosa were obtained from outbred rats (Charles River Breeding Laboratories, Wilmington, MA) and New Zealand white rabbits, after sacrifice by intraperitoneal injection of sodium pentobarbital; samples from cotton-top tamarins (S. oedipus) were obtained after anesthetization as previously described (19). All samples were promptly processed for immunofluorescent studies as described below.…”

Section: Methodsmentioning

confidence: 99%

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Human colonic goblet cells. Demonstration of distinct subpopulations defined by mucin-specific monoclonal antibodies.

1986

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We studied glycoprotein content of human colonic goblet cells, using a library of monoclonal antibodies (MAbs) Anti-HCM MAbs stained goblet cells from other sites within the gastrointestinal tract to a varying extent. Anti-HCM MAbs also showed extensive cross-reactivity with rodent, rabbit, and monkey colonic mucosa. However, several anti-HCM MAbs stained only human colonic mucosa. These data show that human colonic mucosa contains discrete subpopulations of goblet cells that produce distinctive combinations of specific mucin glycoprotein species.

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Section: Methodsmentioning

confidence: 99%

“…Recent work in this laboratory has shown that the colonic mucosa collectively produces a complex mixture of at least six compositionally and structurally distinct mucin glycoproteins (mucin species I-VI) (9,18,19). However, the cellular basis of mucin glycoprotein heterogeneity remains unknown.…”

Section: Introductionmentioning

confidence: 99%

Human colonic goblet cells. Demonstration of distinct subpopulations defined by mucin-specific monoclonal antibodies.

1986

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“…The development ofa library ofmonoclonal antibodies with defined, anti-mucin species specificity has provided some insight into the cellular basis of colonic mucin glycoprotein heterogeneity. Studies using indirect immunofluorescent-staining techniques suggest that there may be a previously unappreciated diversity within the large population of morphologically indistinguishable goblet cells in colonic mucosa (18,20). Staining of colonic goblet cells using monoclonal antibodies that recognize different mucin glycoprotein species indicate that particular combinations of the glycoprotein species are found in distinct subpopulations of goblet cells.…”

Section: Discussionmentioning

confidence: 99%

“…Studies in this laboratory have demonstrated the presence of substantial heterogeneity in colonic mucosal mucin glycoproteins (14)(15). At least six glycoprotein fractions initially separated by DEAEcellulose chromatography were shown to represent structurally distinct glycoprotein species (I-VI) (16)(17)(18)(19). Whereas the functional significance of this heterogeneity remains unclear, the bi-ologic relevance ofthese chromatographically distinguished species is underscored by the observation that the colonic mucosal content of one species (IV) is selectively diminished in specific association with UC.…”

Section: Introductionmentioning

confidence: 99%

Biosynthesis and secretion of human colonic mucin glycoproteins.

Smith¹,

Podolsky

1987

J. Clin. Invest.

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Synthesis and secretion of colonic mucin glycoprotein species were assessed during in vitro culture of colonic mucosal explants. DEAE-cellulose chromatography of endogenously labeled mucin glycoproteins from explant tissue demonstrated the presence of six mucin species (I-VI) similar to those identified earlier in surgical specimens of human colonic tissue. The relative proportions of mucin species I-VI in tissue explants remained constant throughout a 30-h culture period. However, the proportional representation of the various mucin species in media was significantly different from that found in tissue, which suggests that some mucin species (I, II, and III) are differentially secreted, whereas others (IV and V) are retained within intracellular pools. Radiolabeled precursors were incorporated into nucin species 1,1, and m at a 2.0-2.6-fold greater rate than their concentration in tissue, supporting the concept that these glycoproteins were both synthesized and secreted at a greater rate than species IV and V.Colonic mucosal explants from patients with ulcerative colitis showed > 90% reduction of species IV. However, the amount of species IV recovered from culture media of ulcerative colitis explants was comparable to normal controls. It appears that mucin species IV is differentially secreted rather than retained within intracellular pools in mucosa of patients with ulcerative colitis.

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“…We also used a probe corresponding to the N-terminal sequence of the rat link peptide on rat Peyer's patches and the cecal patch; again, no labeling of M cells could be detected, although goblet cells were intensely stained. Finally, we used the MAb WE9 (25), which recognizes the peptidic core of human, rat, and mouse Muc2 (32). We did not detect any signal in the FAE of rat Peyer's and cecal patches, but goblet cells from adjacent villi were labeled.…”

Section: Vol 69 2001 Apical Membrane Glycoconjugates Of Intestinal mentioning

confidence: 99%

Glycocalyx on Rabbit Intestinal M Cells Displays Carbohydrate Epitopes from Muc2

et al. 2001

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It is essential to investigate the apical surface properties of both M cells and dome enterocytes to understand the mechanisms involved in the binding of pathogens to M cells. In rabbit appendix tissue, monoclonal antibodies (MAbs) highlight differences between M cells (MAb 58) and dome enterocytes (MAb 214). Such antibodies ultimately recognized intestinal mucin-related epitopes. To further characterize these differences, the labeling patterns obtained with these MAbs were compared to those obtained with other antibodies to intestinal mucins on dissected domes from all gut-associated lymphoid tissues. A glycoprotein recognized by MAb 58 was purified on a CsCl isopycnic density gradient and microsequenced, and its mRNA expression was localized by in situ hybridization. It was identified as the rabbit homologue of human Muc2, i.e., the major mucin secreted in intestine tissue. Two other Muc2 carbohydrate epitopes were also expressed on M cells, although Muc2 mRNA was not detected. All results indicated that M cells express, on their apical membrane, glycoconjugates bearing at least three glycosidic epitopes from Muc2. MAb 214 and MAb 6G2, which recognized a partially characterized mucin expressed on dome enterocytes, were negative markers for M cells in rabbit gut-associated lymphoid tissues. We propose that the presence, on the surface of M cells, of carbohydrates also expressed on Muc2, together with the absence of an enterocyte-associated mucin, could favor pathogen attachment and accessibility to the M-cell luminal membrane.

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Development of anti-human colonic mucin monoclonal antibodies. Characterization of multiple colonic mucin species.

Cited by 43 publications

References 35 publications

Human colonic goblet cells. Demonstration of distinct subpopulations defined by mucin-specific monoclonal antibodies.

Human colonic goblet cells. Demonstration of distinct subpopulations defined by mucin-specific monoclonal antibodies.

Biosynthesis and secretion of human colonic mucin glycoproteins.

Glycocalyx on Rabbit Intestinal M Cells Displays Carbohydrate Epitopes from Muc2

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