Biosynthesis of rat MUC2 in colon and its analogy with human MUC2

K. M. Tytgat; F. J. Bovelander; F. J. Opdam; A. W. Einerhand; H. A. Büller; J. Dekker

doi:https://doi.org/10.1042/bj3090221

Biosynthesis of rat MUC2 in colon and its analogy with human MUC2

K. M. Tytgat, F. J. Bovelander, F. J. Opdam, A. W. Einerhand, H. A. Büller, J. Dekker

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Abstract

In order to identify the mucins synthesized and secreted in the rat colon, we studied their biochemical characteristics and biosynthesis and evaluated their analogy to human colonic mucins. Purified mucin from both species appeared similar with respect to composition, buoyant density and mobility on SDS/PAGE. Isolated rat colonic mucin (RCM) was used to elicit a polyclonal antiserum, which was used in metabolic labelling studies to identify mucins and mucin precursors. RCM is synthesized as a 600 kDa precursor protein, which oligomerizes before O-glycosylation. The mature, high-molecular mass mucin is secreted and displays an anomalous molecular mass on SDS/PAGE of approximately 650 kDa. Polymorphism in precursor size was found among different rats, suggesting genetic heterogeneity. Molecular mass, biosynthesis and secretion of RCM appeared similar to human MUC2. Moreover, RCM precursor could be immunoprecipitated using specific anti-(human MUC2) antisera, indicating that the RCM can be designated rat MUC2. This study describes the biosynthesis of two homologous mucins in two different species. The high degree of similarity suggests functional analogy

Original language	English
Pages (from-to)	221-229
Journal	Biochemical journal
Volume	309 ( Pt 1)
DOIs	https://doi.org/10.1042/bj3090221
Publication status	Published - 1995

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https://doi.org/10.1042/bj3090221

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@article{8f28da7bc98b4f0ebac88da3f96e414f,

title = "Biosynthesis of rat MUC2 in colon and its analogy with human MUC2",

abstract = "In order to identify the mucins synthesized and secreted in the rat colon, we studied their biochemical characteristics and biosynthesis and evaluated their analogy to human colonic mucins. Purified mucin from both species appeared similar with respect to composition, buoyant density and mobility on SDS/PAGE. Isolated rat colonic mucin (RCM) was used to elicit a polyclonal antiserum, which was used in metabolic labelling studies to identify mucins and mucin precursors. RCM is synthesized as a 600 kDa precursor protein, which oligomerizes before O-glycosylation. The mature, high-molecular mass mucin is secreted and displays an anomalous molecular mass on SDS/PAGE of approximately 650 kDa. Polymorphism in precursor size was found among different rats, suggesting genetic heterogeneity. Molecular mass, biosynthesis and secretion of RCM appeared similar to human MUC2. Moreover, RCM precursor could be immunoprecipitated using specific anti-(human MUC2) antisera, indicating that the RCM can be designated rat MUC2. This study describes the biosynthesis of two homologous mucins in two different species. The high degree of similarity suggests functional analogy",

author = "Tytgat, {K. M.} and Bovelander, {F. J.} and Opdam, {F. J.} and Einerhand, {A. W.} and B{\"u}ller, {H. A.} and J. Dekker",

year = "1995",

doi = "https://doi.org/10.1042/bj3090221",

language = "English",

volume = "309 ( Pt 1)",

pages = "221--229",

journal = "Biochemical journal",

issn = "0264-6021",

publisher = "Portland Press Ltd.",

}

TY - JOUR

T1 - Biosynthesis of rat MUC2 in colon and its analogy with human MUC2

AU - Tytgat, K. M.

AU - Bovelander, F. J.

AU - Opdam, F. J.

AU - Einerhand, A. W.

AU - Büller, H. A.

AU - Dekker, J.

PY - 1995

Y1 - 1995

N2 - In order to identify the mucins synthesized and secreted in the rat colon, we studied their biochemical characteristics and biosynthesis and evaluated their analogy to human colonic mucins. Purified mucin from both species appeared similar with respect to composition, buoyant density and mobility on SDS/PAGE. Isolated rat colonic mucin (RCM) was used to elicit a polyclonal antiserum, which was used in metabolic labelling studies to identify mucins and mucin precursors. RCM is synthesized as a 600 kDa precursor protein, which oligomerizes before O-glycosylation. The mature, high-molecular mass mucin is secreted and displays an anomalous molecular mass on SDS/PAGE of approximately 650 kDa. Polymorphism in precursor size was found among different rats, suggesting genetic heterogeneity. Molecular mass, biosynthesis and secretion of RCM appeared similar to human MUC2. Moreover, RCM precursor could be immunoprecipitated using specific anti-(human MUC2) antisera, indicating that the RCM can be designated rat MUC2. This study describes the biosynthesis of two homologous mucins in two different species. The high degree of similarity suggests functional analogy

AB - In order to identify the mucins synthesized and secreted in the rat colon, we studied their biochemical characteristics and biosynthesis and evaluated their analogy to human colonic mucins. Purified mucin from both species appeared similar with respect to composition, buoyant density and mobility on SDS/PAGE. Isolated rat colonic mucin (RCM) was used to elicit a polyclonal antiserum, which was used in metabolic labelling studies to identify mucins and mucin precursors. RCM is synthesized as a 600 kDa precursor protein, which oligomerizes before O-glycosylation. The mature, high-molecular mass mucin is secreted and displays an anomalous molecular mass on SDS/PAGE of approximately 650 kDa. Polymorphism in precursor size was found among different rats, suggesting genetic heterogeneity. Molecular mass, biosynthesis and secretion of RCM appeared similar to human MUC2. Moreover, RCM precursor could be immunoprecipitated using specific anti-(human MUC2) antisera, indicating that the RCM can be designated rat MUC2. This study describes the biosynthesis of two homologous mucins in two different species. The high degree of similarity suggests functional analogy

U2 - https://doi.org/10.1042/bj3090221

DO - https://doi.org/10.1042/bj3090221

M3 - Article

C2 - 7619060

SN - 0264-6021

VL - 309 ( Pt 1)

SP - 221

EP - 229

JO - Biochemical journal

JF - Biochemical journal

ER -