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Cell Immunol. 1994 Jan;153(1):94-104.

12-O-tetradecanoylphorbol 13-acetate stimulates human T-lymphocyte adherence to the fibronectin RGD domain and the laminin IKVAV domain.

Author information

1
Laboratory of Developmental Biology, National Institute of Dental Research, National Institutes of Health, Bethesda, Maryland 20892.

Abstract

In order for T cells to exit the circulatory system, these cells must attach to extracellular matrix proteins. We have used 12-O-tetradecanoylphorbol 13-acetate (TPA) to study the ability of human T cells to adhere to fibronectin or laminin or to specific domains on these extracellular matrix proteins. Both primary human T-lymphocytes and a T-cell line (H-9) adhered and spread well on solid-phase fibronectin and laminin in the presence of TPA, with maximum activity at 3 hr of treatment. Furthermore, attachment of both cell populations to fibronectin was inhibited using a soluble RGD-containing synthetic peptide or by pretreating the fibronectin with antibodies that block the RGD domain. A synthetic peptide from the CSI alternatively spliced region of fibronectin did not inhibit attachment to fibronectin. The H-9 cells also attached to the laminin A chain IKVAV-containing synthetic peptide, but not to the laminin-derived YIGSR- or RGD-containing sequences. Immunoprecipitation of 32P-labeled H-9 cells with antibodies to the beta 1 integrin subunit demonstrated phosphorylation of an alpha integrin subunit after treatment with TPA. These data demonstrate that TPA activates T-cell adherence to laminin and to fibronectin via specific sites on each protein and that this adhesion may be associated with integrin phosphorylation.

PMID:
8287495
DOI:
10.1006/cimm.1994.1008
[Indexed for MEDLINE]

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