Premium
The expression of integrin α2β1 and attachment to type I collagen of melanoma cells are preferentially induced by tumour promoter, TPA (12‐ O ‐tetradecanoyl phorbol‐13‐acetate)
Author(s) -
EGUCHI H.,
HORIKOSHI T.
Publication year - 1996
Publication title -
british journal of dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.304
H-Index - 179
eISSN - 1365-2133
pISSN - 0007-0963
DOI - 10.1046/j.1365-2133.1996.d01-749.x
Subject(s) - integrin , calphostin c , protein kinase c , laminin , extracellular matrix , chemistry , collagen receptor , forskolin , microbiology and biotechnology , cell adhesion , cancer research , phorbol , receptor , cell , signal transduction , biology , biochemistry
Summary The adhesion of melanoma cells to the extracellular matrix (ECM) protein is likely to be essential in their invasive metastatic processes. Treatment with 12‐ O ‐tetradecanoyl phorbol‐13‐acetate (TPA), a potent protein kinase C (PKC) activator, preferentially induced the expression of α2β1 integrin, the receptor for collagen/laminin. The number of cells attached to type I collagen, but not laminin, was increased by treatment with TPA. Prior exposure to PKC inhibitors such as H‐7 (20 μmol/1) and calphostin C (50μmol/1) had no effect on TPA‐induced α2β1 integrin expression and cell attachment to type I collagen, whereas prior exposure to the calmodulin antagonist W‐7(50 μmol/1) inhibited these TPA‐induced events. The augmented adhesion was also inhibited by anti‐α2 antibody. These data suggest that the increased attachment of melanoma cells to type I collagen appears to be mediated by the preferential augmentation of integrin α2β1, and the activation of calmodulin kinase, but not via the activation of PKC. Analysis of the expression of integrins and of cell attachment to ECMs is important in elucidating the mechanisms involved in the progression and metastasis of malignant melanoma.