Human keratinocytes adhere to and spread on synthetic peptide FN-C/H-V derived from fibronectin.
In a previous study, we reported that two synthetic peptides derived from the 33-kD carboxyl terminal cell/heparin-binding 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.
Wilke
M S
MS
Department of Laboratory Medicine and Pathology, University of Minnesota Medical School, Minneapolis 55455-0315.
Vespa
J
J
Skubitz
A P
AP
Furcht
L T
LT
McCarthy
J B
JB
D000595:Amino Acid Sequence; D002448:Cell Adhesion / Q000187:drug effects*; D002455:Cell Division / Q000187:drug effects; D003094:Collagen; D005353:Fibronectins / Q000737:chemistry* / Q000494:pharmacology*; D006801:Humans; D015603:Keratinocytes / Q000187:drug effects*; D007797:Laminin; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000235:genetics / Q000494:pharmacology*
D005353:Fibronectins; D007797:Laminin; D010446:Peptide Fragments; D003094:Collagen