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

Benjamin S. Weeks, Eva Holloway, Paul E. Klotman, Steven K. Akiyama, H. William Schnaper, Hynda K. Kleinman

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

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 32 P-labeled H-9 cells with antibodies to the β1 integrin subunit demonstrated phosphorylation of an α 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.

Original languageEnglish (US)
Pages (from-to)94-104
Number of pages11
JournalCellular Immunology
Volume153
Issue number1
DOIs
StatePublished - Jan 1994

ASJC Scopus subject areas

  • Immunology

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