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PMID: 6870820 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Synthesis of hyaluronate in differentiated teratocarcinoma cells. Mechanism of chain growth.

The Biochemical journal ·Vol. 211 ·No. 1 ·1983-04-01 ·Pages 191-8

Prehm P

Abstract

Hyaluronate could be labelled in vivo with [32P]phosphate. [32P]UDP in an alpha-glycosidic linkage constituted the reducing end of membrane-bound hyaluronate. The UDP is liberated during further chain elongation, indicating that chain growth occurs at the reducing end. [3H]Uridine could be incorporated into hyaluronate during synthesis on the isolated membraneous fraction from [3H]UDP-GlcNAc and [3H]UDP-GlcA, confirming the identification of UDP as a constituent of membrane-bound hyaluronate. These results led to a model of hyaluronate chain elongation at the reducing end by alternate addition of the chains to the substrates. Membrane-bound pyrophosphatases or 5'-nucleotidase are suggested as modulators of hyaluronate synthesis.

MeSH Terms
Cell Membrane/metabolism Cell Transformation, Neoplastic Cells, Cultured Electrophoresis, Polyacrylamide Gel Hyaluronic Acid/biosynthesis Phosphorus Radioisotopes Teratoma/metabolism Uridine/metabolism Uridine Diphosphate N-Acetylgalactosamine/metabolism Uridine Diphosphate N-Acetylglucosamine/metabolism
Chemicals
Phosphorus Radioisotopes Uridine Diphosphate N-Acetylglucosamine Uridine Diphosphate N-Acetylgalactosamine Hyaluronic Acid Uridine
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Prehm P
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42 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2110191
Published
1983-04-01
Pages
191-8
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1154343
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2110191 PMC Full Text View journal details
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