The intracellular location of the glycosylation of hydroxylysine of collagen

Anna G. Brownell; Arthur Veis

doi:10.1016/0006-291X(75)90698-1

The intracellular location of the glycosylation of hydroxylysine of collagen

Anna G. Brownell^*, Arthur Veis

^*Corresponding author for this work

Cell & Developmental Biology

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

22 Scopus citations

Abstract

The subcellular location at which hydroxylysine residues of collagen are glycosylated was studied in chick embryo fibroblasts. Ribosomes were isolated from ¹⁴C-lysine pulse-labeled cells in tissue culture. Alkaline hydrolysis followed by amino acid analysis and scintillation counting of the effluent showed that glucosylgalactosyl hydroxylysine and galactosyl hydroxylysine as well as hydroxylysine and lysine were the major ¹⁴C-labeled components. Acid hydrolysis destroyed the glycoconjugates and yielded only free ¹⁴C-hydroxylysine and ¹⁴C-lysine. These data indicate that glycosylation of peptide-bound hydroxylysine is initiated while the polypeptide chain is still in the stages of assembly on the ribosome.

Original language	English (US)
Pages (from-to)	371-377
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	63
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(75)90698-1
State	Published - Mar 17 1975

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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title = "The intracellular location of the glycosylation of hydroxylysine of collagen",

abstract = "The subcellular location at which hydroxylysine residues of collagen are glycosylated was studied in chick embryo fibroblasts. Ribosomes were isolated from 14C-lysine pulse-labeled cells in tissue culture. Alkaline hydrolysis followed by amino acid analysis and scintillation counting of the effluent showed that glucosylgalactosyl hydroxylysine and galactosyl hydroxylysine as well as hydroxylysine and lysine were the major 14C-labeled components. Acid hydrolysis destroyed the glycoconjugates and yielded only free 14C-hydroxylysine and 14C-lysine. These data indicate that glycosylation of peptide-bound hydroxylysine is initiated while the polypeptide chain is still in the stages of assembly on the ribosome.",

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AU - Brownell, Anna G.

AU - Veis, Arthur

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N2 - The subcellular location at which hydroxylysine residues of collagen are glycosylated was studied in chick embryo fibroblasts. Ribosomes were isolated from 14C-lysine pulse-labeled cells in tissue culture. Alkaline hydrolysis followed by amino acid analysis and scintillation counting of the effluent showed that glucosylgalactosyl hydroxylysine and galactosyl hydroxylysine as well as hydroxylysine and lysine were the major 14C-labeled components. Acid hydrolysis destroyed the glycoconjugates and yielded only free 14C-hydroxylysine and 14C-lysine. These data indicate that glycosylation of peptide-bound hydroxylysine is initiated while the polypeptide chain is still in the stages of assembly on the ribosome.

AB - The subcellular location at which hydroxylysine residues of collagen are glycosylated was studied in chick embryo fibroblasts. Ribosomes were isolated from 14C-lysine pulse-labeled cells in tissue culture. Alkaline hydrolysis followed by amino acid analysis and scintillation counting of the effluent showed that glucosylgalactosyl hydroxylysine and galactosyl hydroxylysine as well as hydroxylysine and lysine were the major 14C-labeled components. Acid hydrolysis destroyed the glycoconjugates and yielded only free 14C-hydroxylysine and 14C-lysine. These data indicate that glycosylation of peptide-bound hydroxylysine is initiated while the polypeptide chain is still in the stages of assembly on the ribosome.

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The intracellular location of the glycosylation of hydroxylysine of collagen

Abstract

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