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 Printable version |
The metalloprotease-directed shedding of BP 180 (collagen XVII) from human keratinocytes in culture is unaffected by ceramide and cell-matrix interaction |
European Journal of Dermatology. Volume 12, Number 3, 240-6, May - June 2002, Rapports d'investigature
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 Free Article
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Author(s) : Anne-Laure LABROUSSE, Nathalie BUISSON-LEGENDRE, William HORNEBECK, Philippe BERNARD |
Summary : The constitutive shedding of BP180 (collagen XVII) from human keratinocytes in culture was totally prevented by batimastat (5 muM), a wide spectrum matrix metalloprotease (MMP) inhibitor. However, keratinocytes did not express active MMP and generation of active Gelatinase A (MMP-2) and Gelatinase B (MMP-9) at the cell plasma membrane by increasing the ceramide content of keratinocytes did not influence BP180 processing to a 120 kDa species. A disintegrin and metalloprotease (ADAM) is probably involved in such a shedding event since release of 120 kDa polypeptide was inhibited by Decanoyl-Arg-Val-Lys-Arg CH2Cl (30 muM), a specific furin convertase inhibitor ; culturing cells on to several matrix substrata i.e. type I collagen, type IV collagen, laminin-1 or laminin-5 had no effect on BP180 processing.
Overall our data indicated that the metalloprotease-mediated shedding of BP180 from keratinocytes in culture is insensitive either to agents which activate MAP kinase pathway (ceramide) or to cell-matrix interactions. |
Keywords : ceramide, collagen XVII, keratinocytes, matrix metalloproteases. |
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