Collagen biosynthesis

Takaki Koide, Kazuhiro Nagata

Research output: Chapter in Book/Report/Conference proceedingChapter

37 Citations (Scopus)

Abstract

Collagen is synthesized in the endoplasmic reticulum (ER) as procollagen, which is the precursor protein that bears propeptide domains at either end of the triple helical domain. The processes by which procollagen is synthesized in the lumen of the ER include unique steps that are not found in the biosynthesis of globular proteins. First, each polypeptide chain of procollagen (proα-chains) finds its correct partners, which enables the formation of the distinct types of procollagen. Second, triple helix-formation of long Gly-X-Y repeats starts at a defined region, which results in the formation of a correctly aligned triple helix and thereby prevents mis-staggering. The most characteristic step is the formation of the triple helix. This step involves specific post-translational modifications, in particular, the prolyl 4-hydroxylation of the Y-position amino acids that stabilizes the triple helical conformation. The formation of the triple helix is a slow process compared to the folding of globular proteins, including cis-trans isomerization of the many prolyl and hydroxyprolyl peptide bonds. Recent advances have indicated that these processes are assisted by a set of the ER-resident molecular chaperones, such as protein disulfide isomerase (PDI), peptidyl prolyl cis-trans isomerases (PPIases), heat-shock protein (Hsp)47, and prolyl 4-hydroxylase (P4-H). The intracellular trafficking of procollagen molecules has also been shown to involve a pathway distinct from that utilized by small secretory proteins.

Original languageEnglish
Title of host publicationTopics in Current Chemistry
Pages85-114
Number of pages30
Volume247
DOIs
Publication statusPublished - 2005 Apr 12
Externally publishedYes

Publication series

NameTopics in Current Chemistry
Volume247
ISSN (Print)03401022

Fingerprint

Procollagen
Biosynthesis
Collagen
HSP47 Heat-Shock Proteins
Peptidylprolyl Isomerase
Prolyl Hydroxylases
Protein Disulfide-Isomerases
Hydroxylation
Peptides
Proteins
Molecular Chaperones
Protein Precursors
Isomerization
Conformations
Amino Acids
Molecules

Keywords

  • Endoplasmic reticulum
  • Folding
  • Molecular chaperone
  • Procollagen
  • Triple helix

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Koide, T., & Nagata, K. (2005). Collagen biosynthesis. In Topics in Current Chemistry (Vol. 247, pp. 85-114). (Topics in Current Chemistry; Vol. 247). https://doi.org/10.1007/b103820

Collagen biosynthesis. / Koide, Takaki; Nagata, Kazuhiro.

Topics in Current Chemistry. Vol. 247 2005. p. 85-114 (Topics in Current Chemistry; Vol. 247).

Research output: Chapter in Book/Report/Conference proceedingChapter

Koide, T & Nagata, K 2005, Collagen biosynthesis. in Topics in Current Chemistry. vol. 247, Topics in Current Chemistry, vol. 247, pp. 85-114. https://doi.org/10.1007/b103820
Koide T, Nagata K. Collagen biosynthesis. In Topics in Current Chemistry. Vol. 247. 2005. p. 85-114. (Topics in Current Chemistry). https://doi.org/10.1007/b103820
Koide, Takaki ; Nagata, Kazuhiro. / Collagen biosynthesis. Topics in Current Chemistry. Vol. 247 2005. pp. 85-114 (Topics in Current Chemistry).
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