Hsp and chaperone distribution during endochondral bone development in mouse embryo

Cell Stress Chaperones. 1998 Dec;3(4):237-44. doi: 10.1379/1466-1268(1998)003<0237:hacdde>2.3.co;2.

Abstract

The process of endochondral bone formation was examined with regard to expression of seven heat shock proteins (Hsps): two small Hsps, the constitutive and the inducible forms of the 70 and the 90 Hsp families, the collagen chaperone Hsp47, and a cytosolic chaperone, TCP-1alpha, using immunohistochemistry. Around day 15.5 of embryogenesis the calcification of the long endochondral bones occurs through progressive replacement of the cartilaginous scaffold (rich in type II collagen) with an ossified matrix (rich in type I collagen), and thus a longitudinal section of limb bone recapitulates all the steps of chondrogenesis and the early steps of osteogenesis. We observed that all these Hsps and chaperones are differentially expressed during bone development in a stage-specific pattern reaching very high levels at some specific stages. The involvement of chaperones during these important differentiation steps will be discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bone Development
  • Bone and Bones / embryology*
  • Bone and Bones / metabolism*
  • Chaperonin Containing TCP-1
  • Chaperonins / metabolism
  • Collagen / metabolism
  • Female
  • HSP47 Heat-Shock Proteins
  • HSP70 Heat-Shock Proteins / metabolism
  • HSP90 Heat-Shock Proteins / metabolism
  • Heat-Shock Proteins / metabolism*
  • Mice
  • Molecular Chaperones / metabolism*
  • Osteogenesis
  • Pregnancy
  • Signal Transduction
  • Tissue Distribution

Substances

  • HSP47 Heat-Shock Proteins
  • HSP70 Heat-Shock Proteins
  • HSP90 Heat-Shock Proteins
  • Heat-Shock Proteins
  • Molecular Chaperones
  • Serpinh1 protein, mouse
  • Collagen
  • Chaperonin Containing TCP-1
  • Chaperonins