Collagen biosynthesis

Takaki Koide, Kazuhiro Nagata*

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapter

43 Citations (Scopus)


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 publicationCollagen
Subtitle of host publicationPrimer in Structure, Processing and Assembly
EditorsJurgen Brinckmann, P.K. Mueller, Holger Notbohm
Number of pages30
Publication statusPublished - 2005 Apr 12
Externally publishedYes

Publication series

NameTopics in Current Chemistry
ISSN (Print)0340-1022


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

ASJC Scopus subject areas

  • Chemistry(all)


Dive into the research topics of 'Collagen biosynthesis'. Together they form a unique fingerprint.

Cite this