Biosynthesis of frog skin mucins: cysteine-rich shuffled modules, polydispersities and genetic polymorphism

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Biosynthesis of frog skin mucins : cysteine-rich shuffled modules, polydispersities and genetic polymorphism. / Hoffmann, W; Hauser, F.

In: Comparative biochemistry and physiology. B, Comparative biochemistry, Vol. 105, No. 3-4, 1993, p. 465-72.

Research output: Contribution to journal › Review › Research › peer-review

Harvard

Hoffmann, W & Hauser, F 1993, 'Biosynthesis of frog skin mucins: cysteine-rich shuffled modules, polydispersities and genetic polymorphism', Comparative biochemistry and physiology. B, Comparative biochemistry, vol. 105, no. 3-4, pp. 465-72. https://doi.org/10.1016/0305-0491(93)90075-g

APA

Hoffmann, W., & Hauser, F. (1993). Biosynthesis of frog skin mucins: cysteine-rich shuffled modules, polydispersities and genetic polymorphism. Comparative biochemistry and physiology. B, Comparative biochemistry, 105(3-4), 465-72. https://doi.org/10.1016/0305-0491(93)90075-g

Vancouver

Hoffmann W, Hauser F. Biosynthesis of frog skin mucins: cysteine-rich shuffled modules, polydispersities and genetic polymorphism. Comparative biochemistry and physiology. B, Comparative biochemistry. 1993;105(3-4):465-72. https://doi.org/10.1016/0305-0491(93)90075-g

Author

Hoffmann, W ; Hauser, F. / Biosynthesis of frog skin mucins : cysteine-rich shuffled modules, polydispersities and genetic polymorphism. In: Comparative biochemistry and physiology. B, Comparative biochemistry. 1993 ; Vol. 105, No. 3-4. pp. 465-72.

Bibtex

@article{46ad9e81baab44829cea91e16a75ccda,
title = "Biosynthesis of frog skin mucins: cysteine-rich shuffled modules, polydispersities and genetic polymorphism",
abstract = "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.",
keywords = "Alleles, Amino Acid Sequence, Animals, Cysteine/analysis, Glycosylation, Molecular Sequence Data, Mucins/biosynthesis, Polymorphism, Genetic, Skin/metabolism, Xenopus laevis/metabolism",
author = "W Hoffmann and F Hauser",
year = "1993",
doi = "10.1016/0305-0491(93)90075-g",
language = "English",
volume = "105",
pages = "465--72",
journal = "Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology",
issn = "1096-4959",
publisher = "Elsevier",
number = "3-4",

}

RIS

TY - JOUR

T1 - Biosynthesis of frog skin mucins

T2 - cysteine-rich shuffled modules, polydispersities and genetic polymorphism

AU - Hoffmann, W

AU - Hauser, F

PY - 1993

Y1 - 1993

N2 - 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.

AB - 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.

KW - Alleles

KW - Amino Acid Sequence

KW - Animals

KW - Cysteine/analysis

KW - Glycosylation

KW - Molecular Sequence Data

KW - Mucins/biosynthesis

KW - Polymorphism, Genetic

KW - Skin/metabolism

KW - Xenopus laevis/metabolism

U2 - 10.1016/0305-0491(93)90075-g

DO - 10.1016/0305-0491(93)90075-g

M3 - Review

C2 - 8365103

VL - 105

SP - 465

EP - 472

JO - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

JF - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

SN - 1096-4959

IS - 3-4

ER -

ID: 347885946