Dermatopontin, a novel player in the biology of the extracellular matrix

O Okamoto, S Fujiwara - Connective tissue research, 2006 - Taylor & Francis
O Okamoto, S Fujiwara
Connective tissue research, 2006Taylor & Francis
Dermatopontin is a widely distributed small molecular weight protein in the extracellular
matrix (ECM) and today its homologues are known in five mammals and several
invertebrates. The structures of these homologues are relatively well conserved among the
species. In the skin, dermatopontin is located mainly on the surface of the collagen fibers. It
is found in the conditioned medium and also in the cytoplasm of cultured fibroblasts. Early
studies focused on ECM assembly (collagen fibrillogenesis) and interactions (with the …
Dermatopontin is a widely distributed small molecular weight protein in the extracellular matrix (ECM) and today its homologues are known in five mammals and several invertebrates. The structures of these homologues are relatively well conserved among the species. In the skin, dermatopontin is located mainly on the surface of the collagen fibers. It is found in the conditioned medium and also in the cytoplasm of cultured fibroblasts. Early studies focused on ECM assembly (collagen fibrillogenesis) and interactions (with the proteoglycan decorin). Subsequently, a targeted disruption of dermatopontin resulted in a phenotype similar to Ehlers-Danlos syndrome. In addition, a cell adhesion activity of this protein for dermal fibroblasts and several other cells was found, and this activity might suggest this protein's involvement in wound healing. The expression of dermatopontin around an infarct zone of experimental myocardial infarction may support this possibility. In invertebrates, dermatopontin homologues act mainly as adhesion/agglutination molecules. In addition, we found that transforming growth factor-β1 interacts with dermatopontin and the function of this cytokine is modified by dermatopontin. Recently, the involvement of this protein in cell proliferation has been indicated. In this review we describe the reported functions of this protein and speculate on the multiple roles of this largely uncharacterized matrix molecule.
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