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Titolo:
A NOVEL SYNAPTOBREVIN VAMP HOMOLOGOUS PROTEIN (VAMP5) IS INCREASED DURING IN-VITRO MYOGENESIS AND PRESENT IN THE PLASMA-MEMBRANE/
Autore:
ZENG Q; SUBRAMANIAM VN; WONG SH; TANG BL; PARTON RG; REA S; JAMES DE; HONG WJ;
Indirizzi:
NATL UNIV SINGAPORE,INST MOL & CELL BIOL SINGAPORE 117609 SINGAPORE NATL UNIV SINGAPORE,INST MOL & CELL BIOL SINGAPORE 117609 SINGAPORE UNIV QUEENSLAND,DEPT PHYSIOL & PHARMACOL,CTR CELLULAR & MOL BIOL ST LUCIA QLD 4072 AUSTRALIA UNIV QUEENSLAND,CTR MICROSCOPY & MICROANAL ST LUCIA QLD 4072 AUSTRALIA
Titolo Testata:
Molecular biology of the cell
fascicolo: 9, volume: 9, anno: 1998,
pagine: 2423 - 2437
SICI:
1059-1524(1998)9:9<2423:ANSVHP>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
SKELETAL-MUSCLE CELLS; ENDOPLASMIC-RETICULUM; MYOBLAST FUSION; GOLGI-APPARATUS; TERMINAL DIFFERENTIATION; RETINOBLASTOMA PROTEIN; VESICULAR TRANSPORT; SYNAPTIC VESICLES; SYNTAXIN FAMILY; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
66
Recensione:
Indirizzi per estratti:
Citazione:
Q. Zeng et al., "A NOVEL SYNAPTOBREVIN VAMP HOMOLOGOUS PROTEIN (VAMP5) IS INCREASED DURING IN-VITRO MYOGENESIS AND PRESENT IN THE PLASMA-MEMBRANE/", Molecular biology of the cell, 9(9), 1998, pp. 2423-2437

Abstract

cDNA clones encoding a novel protein (VAMP5) homologous to synaptobrevins/VAMPs are detected during database searches. The predicted 102-amino acid VAMP5 harbors a 23-residue hydrophobic region near the carboxyl terminus and exhibits an overall amino acid identity of 33% with synaptobrevin/VAMP1 and 2 and cellubrevin. Northern blot analysis reveals that the mRNA for VAMP5 is preferentially expressed in the skeletal muscle and heart, whereas significantly lower levels are detected in several other tissues but not in the brain. During in vitro differentiation (myogenesis) of C2C12 myoblasts into myotubes, the mRNA level forVAMP5 is increased similar to 8- to 10-fold. Immunoblot analysis using antibodies specific for VAMP5 shows that the protein levels are alsoelevated similar to 6-fold during in vitro myogenesis of C2C12 cells. Indirect immunofluorescence microscopy and immunoelectron microscopy reveal that VAMP5 is associated with the plasma membrane as well as intracellular perinuclear and peripheral vesicular structures of myotubes. Epitope-tagged versions of VAMP5 are similarly targeted to the plasma membrane.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/09/20 alle ore 22:57:19