Human mucin glycoproteins: varied structures predict diverse properties and specific functions

It has been clear for some time now that mucin glycoproteins have extensive, highly glycosylated tandem repeat domains. What is becoming increasingly apparent, however, is the diversity of unique sequences present on different mucins. Variations in mucin-unique sequences clearly result in major diff...

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Bibliographic Details
Published inBiochemical Society transactions Vol. 23; no. 4; p. 795
Main Author Gum, Jr, J R
Format Journal Article
LanguageEnglish
Published England 01.11.1995
Subjects
Amino Acid Sequence
Gene Expression
Glycosylation
Humans
Intestinal Mucosa - metabolism
Molecular Sequence Data
Molecular Structure
Mucin-2
Mucin-3
Mucins - chemistry
Mucins - genetics
Mucoproteins - chemistry
Mucoproteins - genetics
Mucoproteins - metabolism
Neoplasm Proteins - chemistry
Neoplasm Proteins - genetics
von Willebrand Factor - chemistry
von Willebrand Factor - genetics
von Willebrand Factor - metabolism
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Summary:It has been clear for some time now that mucin glycoproteins have extensive, highly glycosylated tandem repeat domains. What is becoming increasingly apparent, however, is the diversity of unique sequences present on different mucins. Variations in mucin-unique sequences clearly result in major differences in physical and biological properties. MUC1-unique sequences are needed for membrane binding, while MUC2-unique sequences apparently mediate polymerization. As the sequences of other mucins are determined, undoubtedly additional structures will be determined that confer specific properties and functions upon this interesting class of glycoconjugates.
ISSN:0300-5127
DOI:10.1042/bst0230795