Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2001-1-26
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin B, http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin H, http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin K, http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin L, http://linkedlifedata.com/resource/pubmed/chemical/Cathepsins, http://linkedlifedata.com/resource/pubmed/chemical/Collagenases, http://linkedlifedata.com/resource/pubmed/chemical/Ctsh protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Ctsk protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Ctsl protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 13, http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 9, http://linkedlifedata.com/resource/pubmed/chemical/Mmp13 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/cathepsin S
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0171-967X
pubmed:author
pubmed:issnType
Print
pubmed:volume
67
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
382-90
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11136537-Animals, pubmed-meshheading:11136537-Blotting, Northern, pubmed-meshheading:11136537-Bony Callus, pubmed-meshheading:11136537-Cathepsin B, pubmed-meshheading:11136537-Cathepsin H, pubmed-meshheading:11136537-Cathepsin K, pubmed-meshheading:11136537-Cathepsin L, pubmed-meshheading:11136537-Cathepsins, pubmed-meshheading:11136537-Chondrocytes, pubmed-meshheading:11136537-Collagenases, pubmed-meshheading:11136537-Cysteine Endopeptidases, pubmed-meshheading:11136537-Endopeptidases, pubmed-meshheading:11136537-Fracture Healing, pubmed-meshheading:11136537-Fractures, Bone, pubmed-meshheading:11136537-Hyperostosis, pubmed-meshheading:11136537-Male, pubmed-meshheading:11136537-Matrix Metalloproteinase 13, pubmed-meshheading:11136537-Matrix Metalloproteinase 9, pubmed-meshheading:11136537-Mice, pubmed-meshheading:11136537-Mice, Inbred C57BL, pubmed-meshheading:11136537-Mice, Inbred DBA, pubmed-meshheading:11136537-Tissue Distribution
pubmed:year
2000
pubmed:articleTitle
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.
pubmed:affiliation
Skeletal Research Program, Department of Medical Biochemistry and Molecular Biology, University of Turku, Finland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't