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A synthetic peptide, FN-C/H-V, from the C-terminal heparin-binding domain of fibronectin promotes adhesion of PMA stimulated U937 cells.
Biochem Biophys Res Commun. 1997 Oct 09; 239(1):205-11.BB

Abstract

Hematopoietic cells differentially bind to the C-terminal heparin-binding domain of fibronectin depending on the activation state of integrin alpha 4 beta 1. In this study, we have identified a synthetic peptide derived from the C-terminal heparin-binding domain of fibronectin that promotes adhesion of PMA-treated U937 cells (a monocytic cell line) in a dose-dependent manner. A peptide (FN-C/H-V; residues Gln1892 to Gly1910) was active to inhibit adhesion of PMA-treated U937 cells to the 29-kDa fragment comprising the C-terminal heparin-binding domain of fibronectin. A peptide with scrambled version of FN-C/H-V lost the inhibitory activity on the adhesion. Furthermore, the IgG-conjugated FN-C/H-V promoted the adhesion of PMA-treated U937 cells to an extent comparable to that of the 29-kDa fragment. The adhesion of PMA-treated U937 cells on IgG-conjugated FN-C/H-V was inhibited both by anti-alpha 4 beta 1 antibody and by glycosaminoglycans including chondroitin sulfate and heparan sulfate. The other peptide, FN-C/H-II, was also a weak adhesion-promoting domain. These results suggest that the amino acid sequence defined by peptide FN-C/H-V contributes to the main adhesion-promoting activity of the 29-kDa fragment of fibronectin to stimulated U937 cells. The regulation of interactions of alpha 4 beta 1 integrin and glycosaminoglycans with ligands in fibronectin may have important implications for the migration and function of U937 cells.

Authors+Show Affiliations

First Department of Internal Medicine, Yokohama City University School of Medicine, Japan.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

9345296

Citation

Kato, K, et al. "A Synthetic Peptide, FN-C/H-V, From the C-terminal Heparin-binding Domain of Fibronectin Promotes Adhesion of PMA Stimulated U937 Cells." Biochemical and Biophysical Research Communications, vol. 239, no. 1, 1997, pp. 205-11.
Kato K, Mohri H, Tamura T, et al. A synthetic peptide, FN-C/H-V, from the C-terminal heparin-binding domain of fibronectin promotes adhesion of PMA stimulated U937 cells. Biochem Biophys Res Commun. 1997;239(1):205-11.
Kato, K., Mohri, H., Tamura, T., & Okubo, T. (1997). A synthetic peptide, FN-C/H-V, from the C-terminal heparin-binding domain of fibronectin promotes adhesion of PMA stimulated U937 cells. Biochemical and Biophysical Research Communications, 239(1), 205-11.
Kato K, et al. A Synthetic Peptide, FN-C/H-V, From the C-terminal Heparin-binding Domain of Fibronectin Promotes Adhesion of PMA Stimulated U937 Cells. Biochem Biophys Res Commun. 1997 Oct 9;239(1):205-11. PubMed PMID: 9345296.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A synthetic peptide, FN-C/H-V, from the C-terminal heparin-binding domain of fibronectin promotes adhesion of PMA stimulated U937 cells. AU - Kato,K, AU - Mohri,H, AU - Tamura,T, AU - Okubo,T, PY - 1997/11/5/pubmed PY - 1997/11/5/medline PY - 1997/11/5/entrez SP - 205 EP - 11 JF - Biochemical and biophysical research communications JO - Biochem Biophys Res Commun VL - 239 IS - 1 N2 - Hematopoietic cells differentially bind to the C-terminal heparin-binding domain of fibronectin depending on the activation state of integrin alpha 4 beta 1. In this study, we have identified a synthetic peptide derived from the C-terminal heparin-binding domain of fibronectin that promotes adhesion of PMA-treated U937 cells (a monocytic cell line) in a dose-dependent manner. A peptide (FN-C/H-V; residues Gln1892 to Gly1910) was active to inhibit adhesion of PMA-treated U937 cells to the 29-kDa fragment comprising the C-terminal heparin-binding domain of fibronectin. A peptide with scrambled version of FN-C/H-V lost the inhibitory activity on the adhesion. Furthermore, the IgG-conjugated FN-C/H-V promoted the adhesion of PMA-treated U937 cells to an extent comparable to that of the 29-kDa fragment. The adhesion of PMA-treated U937 cells on IgG-conjugated FN-C/H-V was inhibited both by anti-alpha 4 beta 1 antibody and by glycosaminoglycans including chondroitin sulfate and heparan sulfate. The other peptide, FN-C/H-II, was also a weak adhesion-promoting domain. These results suggest that the amino acid sequence defined by peptide FN-C/H-V contributes to the main adhesion-promoting activity of the 29-kDa fragment of fibronectin to stimulated U937 cells. The regulation of interactions of alpha 4 beta 1 integrin and glycosaminoglycans with ligands in fibronectin may have important implications for the migration and function of U937 cells. SN - 0006-291X UR - https://www.unboundmedicine.com/medline/citation/9345296/A_synthetic_peptide_FN_C/H_V_from_the_C_terminal_heparin_binding_domain_of_fibronectin_promotes_adhesion_of_PMA_stimulated_U937_cells_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(97)97259-4 DB - PRIME DP - Unbound Medicine ER -