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Titolo:
GENOMIC ORGANIZATION OF THE MOUSE AND HUMAN GENES FOR VASCULAR ENDOTHELIAL GROWTH-FACTOR-B (VEGF-B) AND CHARACTERIZATION OF A 2ND SPLICE ISOFORM
Autore:
OLOFSSON B; PAJUSOLA K; VONEULER G; CHILOV D; ALITALO K; ERIKSSON U;
Indirizzi:
LUDWIG INST CANC RES,STOCKHOLM BRANCH,BOX 240 S-17177 STOCKHOLM SWEDEN LUDWIG INST CANC RES,STOCKHOLM BRANCH S-17177 STOCKHOLM SWEDEN MOL CANC BIOL LAB HELSINKI 00014 FINLAND HAARTMAN INST HELSINKI 00014 FINLAND
Titolo Testata:
The Journal of biological chemistry
fascicolo: 32, volume: 271, anno: 1996,
pagine: 19310 - 19317
SICI:
0021-9258(1996)271:32<19310:GOOTMA>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
TYROSINE KINASE; PDGF RECEPTOR; CDNA CLONING; EXPRESSION; PLACENTA; PROTEIN; ANGIOGENESIS; BINDING; DIFFERENTIATION; VASCULOGENESIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
35
Recensione:
Indirizzi per estratti:
Citazione:
B. Olofsson et al., "GENOMIC ORGANIZATION OF THE MOUSE AND HUMAN GENES FOR VASCULAR ENDOTHELIAL GROWTH-FACTOR-B (VEGF-B) AND CHARACTERIZATION OF A 2ND SPLICE ISOFORM", The Journal of biological chemistry, 271(32), 1996, pp. 19310-19317

Abstract

A second isoform and the genomic structures of mouse and human vascular endothelial growth factor B are described. Both genes consist of seven coding exons and span about 4 kilobases of DNA. The two identifiedisoforms of vascular endothelial growth factor B are generated by alternative splicing where different, splice acceptor sites in exon 6 introduce a frameshift and a partial use of different but overlapping reading frames, Consequently, the COOK-terminal domains in the two isoforms show no resemblance, Mouse and human cDNA clones for the novel isoform of vascular endothelial growth factor B encoded a secreted proteinof 186 amino acid residues. Expression in transfected cells generateda protein of 25 kDa which upon secretion was modified by O-linked glycosylation and displayed a molecular mass of 32 kDa under reducing conditions. The protein was expressed as a disulfide-linked homodimer, and heterodimers were generated when coexpressed with vascular endothelial growth factor. The entirely different COOH-terminal domains in the two isoforms of vascular endothelial growth factor B imply that some functional properties of the two proteins are distinct.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 15/07/20 alle ore 20:17:46