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PMID: 1054508 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Cell-cell interactions: enhancement of glycosyl transferase ectoenzyme systems during Chlamydomonas gametic contact.

McLean RJ, Bosmann HB

Abstract

Glycosyl transferase ectoenzyme systems that transfer galactose, glucose, N-acetylglucosamine, N-acetylneuraminic acid, mannose, and fucose have been detected on vegetative cells and gametes of Chlamydomonas moewusii. Gametes have higher levels of activity of the transferase ectoenzyme systems than morphologically identical vegetative cells, as determined by transfer of monosaccharide onto endogenous cell surface acceptors. When (plus) and (minus) gametes are mixed, there is a significant increase in the activity of transferase ectoenzyme systems. No enhancement in activity of transferase ectoenzyme systems occurs when (plus) and (minus) vegetative cells are mixed. Flagellar membrane vesicles obtained from (plus) and (minus) gametes show high activity of transferase ectoenzyme systems per mg of protein and also demonstrate enhanced activity upon mixing. Therefore, glycosyl transferases and acceptors seem to be located on the flagellar membrane and appear to have a function particularly related to gametic cells. The mechanism of cellular adhesion or recognition proposed by Roseman (1970, Chem. Phys. Lipids 5, 270-297), involving glycosyl transferases and acceptors, is strongly suggested by our data for the mating reaction in Chlamydomonas.

MeSH Terms
Binding Sites Cell Adhesion Cell Membrane/enzymology Chlamydomonas/cytology,enzymology Fucose/metabolism Galactose/metabolism Glucosamine/metabolism Glucose/metabolism Hexosyltransferases/metabolism Mannose/metabolism Neuraminic Acids/metabolism Plant Proteins/metabolism
Chemicals
Neuraminic Acids Plant Proteins Fucose Hexosyltransferases Glucose Glucosamine Mannose Galactose
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
McLean R J
Bosmann H B
References (20)
20 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1975-01-00
Pages
310-3
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC432294
Subset
IM
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