Versican, a major hyaluronan-binding component in the dermis, loses its hyaluronan-binding ability in solar elastosis.

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Hasegawa K, Yoneda M, Kuwabara H, Miyaishi O, Itano N, Ohno A, Zako M, Isogai Z

Versican, a major hyaluronan-binding component in the dermis, loses its hyaluronan-binding ability in solar elastosis.

J Invest Dermatol. 2007 Jul;127(7):1657-63. doi: 10.1038/sj.jid.5700754. Epub 2007 Mar 15.

PubMed ID

17363913 [ View in PubMed

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Abstract

Versican interacts with hyaluronan (HA) at its N-terminus and with fibrillin-1 at its C terminus. As versican in the dermis connects microfibrils to the HA-rich matrix for viscoelasticity, dermal diseases may involve destruction of these complexes. A recombinant versican protein, rVN, covering the HA binding region (HABR) of human versican and a polyclonal antibody, 6084, against rVN were prepared and characterized. Blotting analyses of skin extracts with 6084 and biotin-conjugated HA revealed that versican was a major HA-binding component in the dermis. Matrix metalloprotease-12, which is expressed in areas of solar elastosis, degraded versican and abrogated its HA-binding ability. Immunohistochemical analyses revealed that the elastic materials in solar elastosis lesions were negative for 6084, but positive for 2B1, an antibody recognizing the C-terminus of versican, indicating loss of the HABR in the aggregated elastic fibers. This loss of the HA-binding ability of versican followed by HA exclusion may be responsible for the pathological and phenotypical changes observed in solar elastosis.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Hyaluronic acid	Versican core protein	Protein	Humans	Unknown	Binder	Details