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Histological identification of active matrix metalloproteinases at sites of cartilage resorption in the developing rat tibial epiphysis

The replacement of the hyaline cartilage model by bone tissue during osseous development involves an extensive resorption of cartilage. The current study examines the role played by matrix metalloproteinases (MMPs) in cartilage resorption in the tibial epiphysis of 8 and 10 day old rats. The entry of cellular, highly vascularized channels requires the degradation of cartilage components. As a first step, aggrecan is cleaved by an unidentified MMP along the edges of the channel walls, as detected by an antiserum directed to a cleavage fragment retained in the tissue; the presence of an active MMP at the channel edge is confirmed by the binding of a recombinant MMP inhibitor, TIMP-2. Second, using histozymography, the collagen component of cartilage is degraded by another MMP, identified as gelatinase B by inhibition studies, at similar channel sites. Thus, two proteinases combine their efforts to produce the resorption associated with channel invasion preceding the appearance of the secondary ossification center in the rat tibial epiphysis.

Identiferoai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.21535
Date January 1999
CreatorsDavoli, Maria Antonietta.
ContributorsLee, Eunice R. (advisor)
PublisherMcGill University
Source SetsLibrary and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada
LanguageEnglish
Detected LanguageEnglish
TypeElectronic Thesis or Dissertation
Formatapplication/pdf
CoverageMaster of Science (Division of Surgical Research.)
RightsAll items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated.
Relationalephsysno: 001652820, proquestno: MQ50748, Theses scanned by UMI/ProQuest.

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