PMID- 11136537
OWN - NLM
STAT- MEDLINE
DCOM- 20010322
LR  - 20190831
IS  - 0171-967X (Print)
IS  - 0171-967X (Linking)
VI  - 67
IP  - 5
DP  - 2000 Nov
TI  - Expression of cathepsins B, H, K, L, and S and matrix metalloproteinases 9 and 13 
      during chondrocyte hypertrophy and endochondral ossification in mouse fracture 
      callus.
PG  - 382-90
AB  - Fracture repair provides an interesting model for chondrogenesis and osteogenesis 
      as it recapitulates in an adult organism the same steps encountered during 
      embryonic skeletal development and growth. The fracture callus is not only a site 
      of rapid production of cartilage and bone, but also a site of extensive 
      degradation of their extracellular matrices. The present study was initiated to 
      increase our understanding of the roles of different proteolytic enzymes, 
      cysteine cathepsins B, H, K, L, and S, and matrix metalloproteinases (MMPs) 9 and 
      13, during fracture repair, as this aspect of bone repair has previously received 
      little attention. Northern analysis revealed marked upregulation of cathepsin K, 
      MMP-9, and MMP-13 mRNAs during the first and second weeks of healing. The 
      expression profiles of these mRNAs were similar with that of osteoclastic marker 
      enzyme tartrate-resistant alkaline phosphatate (TRAP). The changes in the mRNA 
      levels of cathepsins B, H, L, and S were smaller when compared with those of the 
      other enzymes studied. Immunohistochemistry and in situ hybridization confirmed 
      the predominant localization of cathepsin K and MMP-9 and their mRNA in 
      osteoclasts and chondroclasts at the osteochondral junction. MMP-13 was present 
      in osteoblasts and individual hypertrophic chondrocytes near the cartilage-bone 
      interphase. In cartilaginous callus, the expression of cathepsins B, H, L, and S 
      was mainly related to chondrocyte hypertrophy. During bone remodeling both 
      osteoblasts and osteoclasts contained these cathepsins. The present data 
      demonstrate that degradation and remodeling of extracellular matrices during 
      fracture healing involves activation of MMP-13 production in hypertrophic 
      chondrocytes and osteoblasts, and cathepsin K and MMP-9 production in osteoclasts 
      and chondroclasts.
FAU - Uusitalo, H
AU  - Uusitalo H
AD  - Skeletal Research Program, Department of Medical Biochemistry and Molecular 
      Biology, University of Turku, Finland.
FAU - Hiltunen, A
AU  - Hiltunen A
FAU - Soderstrom, M
AU  - Soderstrom M
FAU - Aro, H T
AU  - Aro HT
FAU - Vuorio, E
AU  - Vuorio E
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Calcif Tissue Int
JT  - Calcified tissue international
JID - 7905481
RN  - EC 3.4.- (Cathepsins)
RN  - EC 3.4.- (Endopeptidases)
RN  - EC 3.4.22.- (Cysteine Endopeptidases)
RN  - EC 3.4.22.1 (Cathepsin B)
RN  - EC 3.4.22.15 (Cathepsin L)
RN  - EC 3.4.22.15 (Ctsl protein, mouse)
RN  - EC 3.4.22.16 (Cathepsin H)
RN  - EC 3.4.22.16 (Ctsh protein, mouse)
RN  - EC 3.4.22.27 (cathepsin S)
RN  - EC 3.4.22.38 (Cathepsin K)
RN  - EC 3.4.22.38 (Ctsk protein, mouse)
RN  - EC 3.4.24.- (Collagenases)
RN  - EC 3.4.24.- (Matrix Metalloproteinase 13)
RN  - EC 3.4.24.- (Mmp13 protein, mouse)
RN  - EC 3.4.24.35 (Matrix Metalloproteinase 9)
SB  - IM
MH  - Animals
MH  - Blotting, Northern/methods
MH  - Bony Callus/*metabolism
MH  - Cathepsin B/biosynthesis
MH  - Cathepsin H
MH  - Cathepsin K
MH  - Cathepsin L
MH  - Cathepsins/*biosynthesis
MH  - Chondrocytes/metabolism
MH  - Collagenases/*biosynthesis/genetics
MH  - Cysteine Endopeptidases/biosynthesis
MH  - *Endopeptidases
MH  - Fracture Healing/*physiology
MH  - Fractures, Bone/metabolism
MH  - Hyperostosis/*metabolism
MH  - Male
MH  - Matrix Metalloproteinase 13
MH  - Matrix Metalloproteinase 9/*biosynthesis/genetics
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Mice, Inbred DBA
MH  - Tissue Distribution
EDAT- 2001/01/03 11:00
MHDA- 2001/03/27 10:01
CRDT- 2001/01/03 11:00
PHST- 2001/01/03 11:00 [pubmed]
PHST- 2001/03/27 10:01 [medline]
PHST- 2001/01/03 11:00 [entrez]
AID - 10.1007/s002230001152 [pii]
AID - 10.1007/s002230001152 [doi]
PST - ppublish
SO  - Calcif Tissue Int. 2000 Nov;67(5):382-90. doi: 10.1007/s002230001152.