Bone proteinases

Teruyo Nakatani, Nicola C. Partridge

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

This chapter surveys our knowledge of the functions of the proteinases expressed in bone. The osteoclast secretes abundant lysosomal cysteine proteinases, especially cathepsin K, and produces some of the neutral proteinases, e.g., matrix metalloproteinase-9. However, osteoblasts and osteocytes, like their related cells, fibroblasts, are able to secrete a host of proteinases, including neutral proteinases such as serine proteinases, plasminogen activators, and metalloproteinases such as matrix metalloproteinase-13, as well as lysosomal proteinases, e.g., cathepsins. Thus, osteoblasts and osteocytes, like fibroblasts, have the capacity not only to synthesize a range of matrix proteins, including type I collagen, but also to remodel their own extracellular matrix via the secretion of a range of proteinases.

Original languageEnglish (US)
Title of host publicationPrinciples of Bone Biology
PublisherElsevier
Pages379-399
Number of pages21
ISBN (Electronic)9780128148419
DOIs
StatePublished - Jan 1 2019

Keywords

  • Aspartic proteinases
  • Cathepsin K
  • Cathepsins
  • Cysteine proteinases
  • Matrix metalloproteinases
  • Osteoblasts
  • Osteoclasts
  • Osteocytes
  • Plasminogen activators
  • Serine proteinases

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Medicine(all)

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