Interaction of heparin with synthetic peptides corresponding to the C-terminal domain of intestinal mucins.

Interaction of heparin with synthetic peptides corresponding to the C-terminal domain of intestinal mucins. Research Abstract Details 

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Interaction of heparin with synthetic peptides corresponding to the C-terminal domain of intestinal mucins. Abstract Text:

G Xu,G G Forstner,J F Forstner,

Unlike most other mucins described to date, two intestinal mucins, rat MLP (rat Muc 2) and human MUC2 have a C-terminal tail that is enriched in cationic amino acids. The distribution of charge in each case resembles that of several well known heparin binding proteins. Peptides designated E20-14 and F13-15, corresponding to the C-terminal 14 amino acids of the two mucins, were synthesized and shown to bind 3 H-labelled heparin by a process that was saturable and mediated by strong electrostatic interactions, giving Kd values of 10 (-7) to 10 (-8) M. Using turbidometric analyses and native gel electrophoresis, we observed that peptide-heparin mixtures formed polydisperse aggregates that dissociated with a progressive increase in the concentration of heparin. Under certain conditions heparin protected the peptide from proteolysis by trypsin. Both heparin and dextran sulfate, the latter a highly sulfated synthetic polysaccharide, were potent inhibitors of 3 H-heparin binding to peptide E20-14, while less sulfated glycosaminoglycans were poorly- or non-inhibitory. Mucin in tissue dispersions and homogenates, or purified from rat intestine, did not bind to heparin, and failed to interact with an antibody specific for the peptide E20-14. Both mucin samples however, reacted with antibodies that recognize regions upstream of the C-terminal 14 amino acids. Immunofluorescent localization of E20-14 was confined to the basal perinuclear regions of goblet cells, whereas localization of an antibody to a flanking sequence on the N-terminal side of the C-tail, localized to mature mucin storage granules. These findings suggest that the heparin -binding C-tail of the mucin may be removed at an early stage of biosynthesis. Heparin-mucin complexes, if they form in vivo, are thus likely to be confined to the ER and/or Golgi compartments.

Interaction of heparin with synthetic peptides corresponding to the C-terminal domain of intestinal mucins. Publishing Authors By Initials

G Xu,GG Forstner,JF Forstner,

For similar animals: chordata: vertebrates: mammals: rodentia: muridae: murinae: rats research abstracts see: animals: chordata: vertebrates: mammals: rodentia: muridae: murinae: rats research

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Interaction of heparin with synthetic peptides corresponding to the C-terminal domain of intestinal mucins. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Glycoconjugate journal

VOLUME: 13

Page Numbers: 81-90

Journal Abbreviation: Glycoconj. J.

ISSN: 0282-0080

DAY: 30

MONTH: Feb

YEAR: 1996

Interaction of heparin with synthetic peptides corresponding to the C-terminal domain of intestinal mucins. Information

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LANGUAGE: eng

NlmUniqueID: 8603310

Interaction of heparin with synthetic peptides corresponding to the C-terminal domain of intestinal mucins. Keywords Mesh Terms:

KEYWORDS: Rats

MESH TERMS: metabolism

Chemical & Substance for Abstract: Interaction of heparin with synthetic peptides corresponding to the C-terminal domain of intestinal mucins. Information

Substance Name: Heparin

Registry Number: 9005-49-6

Grant and Affiliation Information for Interaction of heparin with synthetic peptides corresponding to the C-terminal domain of intestinal mucins.

AFFILIATION: Hospital for Sick Children, Toronto, Canada.

Country: ENGLAND

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MEDLINETA: Glycoconj J

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