| Autor: |
Labrousse AL; Department of dermatology, CNRS FRE 2260, IFR 53 Biomolecules, Faculty of Medicine, 51, rue Cognacq-Jay, 51095 Reims Cedex, France., Buisson-Legendre N, Hornebeck W, Bernard P |
| Jazyk: |
angličtina |
| Zdroj: |
European journal of dermatology : EJD [Eur J Dermatol] 2002 May-Jun; Vol. 12 (3), pp. 240-6. |
| Abstrakt: |
The constitutive shedding of BP180 (collagen XVII) from human keratinocytes in culture was totally prevented by batimastat (5 microM), 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 microM), 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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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