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First published online June 18, 2008

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Boning up on transglutaminases

The calcification of the extracellular matrix (ECM) is crucial for bone formation, and inappropriate calcification is a hallmark of osteoarthritis. Mature chondrocytes (which have undergone hypertrophic differentiation) stimulate calcification and ECM remodelling, but the factors that drive chondrocyte maturation remain poorly understood. Chondrocyte transglutaminase (TG) enzymes, particularly TG2, are known to have an important role in hypertrophic differentiation, and Kristen Johnson and colleagues (p. 2256) now show that TG2 acts in concert with another chondrocyte TG, Factor XIIIA (FXIIIA). The authors show that exogenous FXIIIA induces hypertrophic differentiation in chondrocytes, even when its TG catalytic activity is abolished by site-directed mutagenesis. FXIIIA stimulates the rapid relocation of TG2 to the cell surface (a process that is known to be necessary for TG2-dependent differentiation), as well as the phosphorylation of p38 MAP kinase. Moreover, exogenous FXIIIA engages the 1-integrin subunit, and crosslinking between 1- and β1-integrin stimulates TG2 relocation even when FXIIIA is absent, which indicates that FXIIIA acts via an 1β1-integrin-dependent pathway. Thus, TG2 and FXIIIA comprise a functional network that accelerates chondrocyte maturation.

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Related articles in JCS:

Factor XIIIA mobilizes transglutaminase 2 to induce chondrocyte hypertrophic differentiation

Kristen A. Johnson, David M. Rose, and Robert A. Terkeltaub
JCS 2008 121: 2256-2264. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?