Retention of Nonhelical Procollagen Containing cis-Hydroxyproline in Rough Endoplasmic Reticulum

Fibroblasts freshly isolated from embryonic tendons were incubated with a proline analog, cis-4-hydroxy-L-proline, which is incorporated into protein and which leads to the intracellular accumulation of nonhelical procollagen. Evidence is presented here that the nonhelical procollagen containing the...

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Veröffentlicht in:Science (American Association for the Advancement of Science) 1975-12, Vol.190 (4220), p.1202-1204
Hauptverfasser: Uitto, Jouni, Hoffmann, Hans-Peter, Prockop, Darwin J.
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container_issue 4220
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container_title Science (American Association for the Advancement of Science)
container_volume 190
creator Uitto, Jouni
Hoffmann, Hans-Peter
Prockop, Darwin J.
description Fibroblasts freshly isolated from embryonic tendons were incubated with a proline analog, cis-4-hydroxy-L-proline, which is incorporated into protein and which leads to the intracellular accumulation of nonhelical procollagen. Evidence is presented here that the nonhelical procollagen containing the analog is retained within the rough endoplasmic reticulum and does not pass to the smooth endoplasmic reticulum or Golgi vacuoles at a normal rate.
doi_str_mv 10.1126/science.1198105
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source MEDLINE; Science Magazine; JSTOR Archive Collection A-Z Listing
subjects Animals
Biochemistry
Biological Transport
Cell membranes
Chick Embryo
Collagen - metabolism
Collagens
Diploidy
Endoplasmic Reticulum - metabolism
Fibroblasts - metabolism
Fibroblasts - ultrastructure
Hydroxyproline - metabolism
Luminescence
Protein Conformation
Protein Precursors - metabolism
Rough endoplasmic reticulum
Smooth endoplasmic reticulum
Somatic cells
Structure-Activity Relationship
Tendons
Tendons - embryology
Tendons - metabolism
Vacuoles
title Retention of Nonhelical Procollagen Containing cis-Hydroxyproline in Rough Endoplasmic Reticulum
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