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The synergy peptide PHSRN and the adhesion peptide RGD mediate cell adhesion through a common mechanism.
- Source :
-
Biochemistry [Biochemistry] 2004 Dec 21; Vol. 43 (50), pp. 15811-21. - Publication Year :
- 2004
-
Abstract
- This work reports on the role of the synergy peptide PHSRN in mediating the adhesion of cells. The attachment of baby hamster kidney cells and 3T3 Swiss fibroblasts to model substrates presenting either GRGDS or PHSRN was evaluated using self-assembled monolayers of alkanethiolates on gold presenting the peptide ligands mixed with tri(ethylene glycol) groups. These substrates permit rigorous control over the structures and densities of peptide ligands and at the same time prevent nonspecific interactions with adherent cells. Both cell types attached efficiently to monolayers presenting either the RGD or the PHSRN peptide but not to monolayers presenting scrambled peptide GRDGS or HRPSN. Cell attachment was comparable on substrates presenting either peptide ligand but less efficient than on substrates presenting the protein fibronectin. The degree of cell spreading, however, was substantially higher on substrates presenting RGD relative to PHSRN. Staining of 3T3 fibroblasts with anti-vinculin and phalloidin revealed clear cytoskeletal filaments and focal adhesions for cells attached by way of either RGD or PHSRN. Inhibition experiments showed that the attachment of 3T3 fibroblasts to monolayers presenting RGD could be inhibited completely by a soluble RGD peptide and partially by a soluble PHSRN peptide. IMR 90 fibroblast attachment to monolayers presenting PHSRN could be inhibited with anti-integrin alpha(5) or anti-integrin beta(1) antibody. This work demonstrates unambiguously that PHSRN alone can support the attachment of cells and that the RGD and PHSRN bind competitively to the integrin receptors.
- Subjects :
- Actin Cytoskeleton chemistry
Actin Cytoskeleton metabolism
Animals
Antibodies immunology
Binding, Competitive
Cricetinae
Fibroblasts chemistry
Fibroblasts drug effects
Fibronectins chemistry
Integrin alphaV drug effects
Integrin alphaV immunology
Integrin alphaV physiology
Integrin beta1 drug effects
Integrin beta1 immunology
Integrin beta1 physiology
Integrins immunology
Integrins physiology
Mice
Oligopeptides chemistry
Peptide Fragments chemistry
Swiss 3T3 Cells
Cell Adhesion
Fibronectins pharmacology
Integrins drug effects
Oligopeptides pharmacology
Peptide Fragments pharmacology
Subjects
Details
- Language :
- English
- ISSN :
- 0006-2960
- Volume :
- 43
- Issue :
- 50
- Database :
- MEDLINE
- Journal :
- Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 15595836
- Full Text :
- https://doi.org/10.1021/bi049174+