Human keratinocytes adhere to and spread on synthetic peptide FN-C/H-V derived from fibronectin

Mark S. Wilke, Jeff Vespa, Amy P Skubitz, Leo T Furcht, James B Mc Carthy

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11 Scopus citations

Abstract

In a previous study, we reported that two synthetic peptides derived from the 33-kD carboxyl terminal cell/heparinbinding fragment of fibronectin A chain promoted keratinocyte adhesion but not spreading. Because keratinocytes are capable of spreading on the 33 66-kD fragments, we focused on identifying additional chemically synthesized peptides from the cell/heparin-binding fragments of fibronectin that might promote cell spreading. When plastic substrata were coated with peptide FN-C/H-V (WQPPRARI), which is derived from the carboxyl-terminal heparin-binding domain of all plasma fibronectin isoforms, keratinocytes adhered and displayed a spread morphology. In solution, soluble peptide FN-C/H-V inhibited cell spreading on intact fibronectin and on the 33 66-kD fragments. Furthermore, polyclonal antibodies raised against peptide FN-C/H-V also inhibited keratinocyte spreading on fibronectin and the 33 66-kD fragments. These data support the hypothesis that keratinocyte cell adhesion and cell spreading on fibronectin are mediated by multiple distinct domains and different regulatory processes.

Original languageEnglish (US)
Pages (from-to)43-48
Number of pages6
JournalJournal of Investigative Dermatology
Volume101
Issue number1
DOIs
StatePublished - Jul 1993

Bibliographical note

Funding Information:
This work was supported by tlte National Cat/cer itlstittlte/National Itlstitutes oj Health (NCI/NIH) grallts CA08843 to MSW, CA21463 to LTF, and CA43924 to JBM; grants from the Graduate School and theJ ohn Bittner Research Flmd to APNS; and Leukemia Task Force gratlts to LTF alld JBM.

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