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J Biol Chem, Vol. 274, Issue 3, 1729-1735, January 15, 1999
From the Department of Biochemistry and Biotechnology, University
of Kuopio, FIN-70210 Kuopio, Finland
Osteopontin, a major noncollagenous bone protein,
is an in vitro and in vivo substrate of tissue
transglutaminase, which catalyzes formation of cross-linked protein
aggregates. The roles of the enzyme and the polymeric osteopontin are
presently not fully understood. In this study we provide evidence that
transglutaminase treatment significantly increases the binding of
osteopontin to collagen. This was tested with an enzyme-linked
immunosorbent assay. The results also show that this increased
interaction is clearly calcium-dependent and specific to
osteopontin. In dot blot overlay assay 1 µg of collagen type I was
able to bind 420 ng of in vitro prepared and purified
polymeric osteopontin and only 83 ng of monomeric osteopontin, indicating that the transglutaminase treatment introduces a 5-fold amount of osteopontin onto collagen. Assays using a reversed situation showed that the collagen binding of the polymeric form of osteopontin appears to be dependent on its conformation in solution. Circular dichroism analysis of monomeric and polymeric osteopontin indicated that transglutaminase treatment induces a conformational change in
osteopontin, probably exposing motives relevant to its interactions with other extracellular molecules. This altered collagen binding property of osteopontin may have relevance to its biological functions in tissue repair, bone remodeling, and collagen fibrillogenesis.
Cross-linking of Osteopontin by Tissue Transglutaminase Increases
Its Collagen Binding Properties
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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