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Titolo:
INVOLVEMENT OF PHENYLALANINE-23 IN THE BINDING OF IGF-1 TO THE INSULIN AND TYPE-I IGF RECEPTOR
Autore:
HODGSON DR; MAY FEB; WESTLEY BR;
Indirizzi:
UNIV NEWCASTLE UPON TYNE,DEPT PATHOL,ROYAL VICTORIA INFIRM NEWCASTLE TYNE NE1 4LP TYNE & WEAR ENGLAND UNIV NEWCASTLE UPON TYNE,DEPT PATHOL,ROYAL VICTORIA INFIRM NEWCASTLE TYNE NE1 4LP TYNE & WEAR ENGLAND
Titolo Testata:
Regulatory peptides
fascicolo: 3, volume: 66, anno: 1996,
pagine: 191 - 196
SICI:
0167-0115(1996)66:3<191:IOPITB>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
GROWTH FACTOR-I; BREAST-CANCER CELLS; HIGH-AFFINITY BINDING; MUTANT HUMAN INSULIN; RETINOIC ACID; RESONANCE; MUTATIONS; PROTEINS; REGION; CHAIN;
Keywords:
RECEPTOR; BINDING-PROTEIN; C-DOMAIN; MITOGENESIS; INSULIN-LIKE GROWTH FACTOR 1; INSULIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
28
Recensione:
Indirizzi per estratti:
Citazione:
D.R. Hodgson et al., "INVOLVEMENT OF PHENYLALANINE-23 IN THE BINDING OF IGF-1 TO THE INSULIN AND TYPE-I IGF RECEPTOR", Regulatory peptides, 66(3), 1996, pp. 191-196

Abstract

The hydrophobic residue Phe-23 lies on a surface of insulin like growth factor 1 (IGF-1) which may be involved in binding to the type I IGFand insulin receptors. The possibility that Phe-23 participates directly in binding to these receptors has been investigated by comparing the properties of [F23G]IGF-1, a mutant of insulin-like growth factor 1in which Phe-23 has been replaced by Gly, with those of IGF-1 and insulin. [F23G]IGF-I has a 48-fold lower affinity for the type I IGF receptor, a markedly reduced affinity for the insulin receptor and a 100-fold reduced affinity for insulin-like growth factor binding proteins (IGFBPs) compared to IGF-1. [F23G]IGF-1 is a full IGF-1 agonist as measured by its ability to stimulate cell proliferation. Its potency was only 4.5-fold less than IGF-1, probably because its bioavailability wasincreased as a result of its reduced affinity for IGFBPs. The large reduction in the affinity of [F23G]IGF-1 for the type I IGF receptor and insulin receptor contrasts with the lack of effect of the corresponding alteration to insulin [FB24G]. Phe-B24 is not thought to be involved directly in the binding of insulin to the insulin receptor and the C-terminus of the B-chain of insulin is suggested to be displaced on binding. We suggest that for IGF-1, the C-terminus of the B chain cannot be displaced because of the presence of the C-domain and the large reduction in the binding affinities of [F23G]IGF-1 suggest that the Phe-23 side chain may be directly involved in binding of IGF-1 to the type I IGF and insulin receptors.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/03/20 alle ore 13:40:20