Biosynthesis of frog skin mucins: cysteine-rich shuffled modules, polydispersities and genetic polymorphism
Research output: Contribution to journal › Review › Research › peer-review
1. Frog integumentary mucins (FIM-A.1, FIM-B.1 and FIM-C.1) consist of typical threonine-rich highly O-glycosylated (semi)repetitive domains, and cysteine-rich modules, i.e. the P-domain, the short consensus repeat and a region with high similarity to the C-terminal end of von Willebrand factor (designated here CC29-motif). 2. These modules are thought to be involved in protein-protein interactions and they have been observed in a variety of extracellular proteins. In FIMs, these modules may be involved in oligomerization processes leading to an entangled mucin network. 3. Polydispersities have been detected in FIM-B.1 and FIM-C.1 within single individuals. Multiple transcripts are probably generated by alternative splicing of a huge array of different (semi)repetitive cassettes encoding the threonine-rich domains. 4. Furthermore, genetic polymorphism is observed between different individuals, probably due to allelic variations in the number of (semi)repetitive cassettes.
Original language | English |
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Journal | Comparative biochemistry and physiology. B, Comparative biochemistry |
Volume | 105 |
Issue number | 3-4 |
Pages (from-to) | 465-72 |
Number of pages | 8 |
ISSN | 0305-0491 |
DOIs | |
Publication status | Published - 1993 |
- Alleles, Amino Acid Sequence, Animals, Cysteine/analysis, Glycosylation, Molecular Sequence Data, Mucins/biosynthesis, Polymorphism, Genetic, Skin/metabolism, Xenopus laevis/metabolism
Research areas
ID: 347885946