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Titolo:
BINDING-SITE IN HUMAN PLASMA FIBRONECTIN TO HL-60 CELLS LOCALIZES IN THE C-TERMINAL HEPARIN-BINDING REGION INDEPENDENTLY OF RGD AND CS1
Autore:
FUJITA H; MOHRI H; KANAMORI H; IWAMATSU A; OKUBO T;
Indirizzi:
YOKOHAMA CITY UNIV,SCH MED,DEPT INTERNAL MED 1,KANAZAWA KU,3-9 FUKUURA YOKOHAMA KANAGAWA 236 JAPAN YOKOHAMA CITY UNIV,SCH MED,DEPT INTERNAL MED 1,KANAZAWA KU YOKOHAMA KANAGAWA 236 JAPAN KIRIN BREWERY,CENT LABS KEY TECHNOL YOKOHAMA KANAGAWA JAPAN
Titolo Testata:
Experimental cell research
fascicolo: 2, volume: 217, anno: 1995,
pagine: 484 - 489
SICI:
0014-4827(1995)217:2<484:BIHPFT>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
EXTRACELLULAR-MATRIX; INTEGRIN ALPHA-4-BETA-1; SULFATE PROTEOGLYCAN; RECOGNITION SIGNAL; ADHESION; IDENTIFICATION; RECEPTORS; MELANOMA; SEQUENCE; DOMAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
43
Recensione:
Indirizzi per estratti:
Citazione:
H. Fujita et al., "BINDING-SITE IN HUMAN PLASMA FIBRONECTIN TO HL-60 CELLS LOCALIZES IN THE C-TERMINAL HEPARIN-BINDING REGION INDEPENDENTLY OF RGD AND CS1", Experimental cell research, 217(2), 1995, pp. 484-489

Abstract

A 29-kDa monomeric dispase-digestive fragment of human plasma fibronectin has been purified by heparin affinity chromatography. The NH2-terminal sequence was determined as Ala(1687)-Val-Thr-Thr-Ile-Pro-Ala-Pro. By mass spectrometry the molecular weight was determined to be 30,241.9 with standard deviation of 3.9 amu. Therefore, we defined the C-terminal sequence of the 29-kDa fragment as Arg(l957)-Lys-Lys-Thr-Gly-Gln-Glu, This indicates that the fragment is composed of 277 amino acids. I-125-fibronectin and the I-125-labeled 29-kDa fragment bound to HL-60 (human acute promyelocytic leukemia) cells in a time-dependent, saturable, and reversible manner. Approximately 120 min was required to reach maximal binding. There were no differences in quantity or rate ofbinding of labeled fibronectin and 29-kDa fragment at temperatures of4 degrees, 22 degrees, and 37 degrees C. The number of binding sites per HL-60 cell of fibronectin and the 29-kDa fragment were 140,000 with a K-d of 133 nM and 108,000 with a K-d of 250 nM, respectively. The binding of fibronectin to HL-60 cells was completely inhibited by thisfragment, and by the peptides of RGDS and CS1 with IC(50)s of 3.6, 840, and 670 mu M, respectively. Native fibronectin inhibited the directbinding of the 29-kDa fragment to HL-60 cells; however, RGDS peptide,peptide CS1, or two melanoma cell adhesion-promoting domain peptides in this 29-kDa fragment (peptide I; Tyr(1906)-Val(1924), peptide II; Asp(1946)-Thr(1960)) did not block this binding. Neither heparitinase nor chondroitinase treatment of cells had any effect on these bindings. These results indicate that the C-terminal cell- and heparin-binding domain of fibronectin mediates HL-60 cell binding by direct interaction independently of RGD, CS1, and melanoma cell adhesion domains in this fragment. (C) 1995 Academic Press, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/21 alle ore 04:13:24