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

Access to Document

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

Cite this

@article{258805346b654756b073235d058a1770,

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.",

author = "Brownell, {Anna G.} and Arthur Veis",

year = "1975",

month = mar,

day = "17",

doi = "10.1016/0006-291X(75)90698-1",

language = "English (US)",

volume = "63",

pages = "371--377",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "2",

}

TY - JOUR

T1 - The intracellular location of the glycosylation of hydroxylysine of collagen

AU - Brownell, Anna G.

AU - Veis, Arthur

PY - 1975/3/17

Y1 - 1975/3/17

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.

UR - http://www.scopus.com/inward/record.url?scp=0016609511&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0016609511&partnerID=8YFLogxK

U2 - 10.1016/0006-291X(75)90698-1

DO - 10.1016/0006-291X(75)90698-1

M3 - Article

C2 - 1168465

AN - SCOPUS:0016609511

SN - 0006-291X

VL - 63

SP - 371

EP - 377

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 2

ER -

The intracellular location of the glycosylation of hydroxylysine of collagen

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this