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Titolo:
THE AMINO-TERMINAL SEQUENCE OF PROOPIOMELANOCORTIN DIRECTS INTRACELLULAR TARGETING TO THE REGULATED SECRETORY PATHWAY
Autore:
TAM WWH; ANDREASSON KI; LOH YP;
Indirizzi:
NICHHD,DEV NEUROBIOL LAB,CELLULAR NEUROBIOL SECT,BLDG 49,ROOM 5A38 BETHESDA MD 20892 NICHHD,DEV NEUROBIOL LAB,CELLULAR NEUROBIOL SECT BETHESDA MD 20892 HOWARD HUGHES MED INST BETHESDA MD 00000
Titolo Testata:
European journal of cell biology
fascicolo: 2, volume: 62, anno: 1993,
pagine: 294 - 306
SICI:
0171-9335(1993)62:2<294:TASOPD>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
ANTERIOR-PITUITARY CELLS; ADRENOCORTICOTROPIN SECRETION; ARGININE VASOPRESSIN; INTERMEDIATE LOBE; MESSENGER-RNA; GOLGI-COMPLEX; TUMOR-CELLS; ATT20 CELLS; TRANSPORT; PROTEINS;
Keywords:
INTRACELLULAR TRANSPORT; ATT-20 CELLS; PROHORMONE; SECRETORY GRANULES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
39
Recensione:
Indirizzi per estratti:
Citazione:
W.W.H. Tam et al., "THE AMINO-TERMINAL SEQUENCE OF PROOPIOMELANOCORTIN DIRECTS INTRACELLULAR TARGETING TO THE REGULATED SECRETORY PATHWAY", European journal of cell biology, 62(2), 1993, pp. 294-306

Abstract

The molecular signal which targets the pro-opiomelanocortin (POMC) prohormone into the regulated secretory pathway was investigated. DNA sequences encoding the first 10, 26, 50, and 101 N-terminal amino acids of mouse POMC were fused in frame to the chloramphenicol acetyltransferase (CAT) gene and expressed in AtT-20 cells. Immunofluorescence microscopy using antibody directed against CAT indicated that fusion proteins carrying 26, 50 and 101 amino acids of N-POMC were directed to secretory granules. This finding was confirmed by secretion studies in which 1 mu M forskolin stimulated the release of fusion proteins carrying 26 and 101 amino acids of N-POMC, whereas no regulated secretion wasobserved with the shortest fusion protein. Subcellular fractionation studies also indicated the presence of the fusion proteins with 26 and101 amino acids of N-POMC in secretory granules. These results provide evidence that the signal directing POMC to secretory granules is contained within the N-terminus of the prohormone, with the first 26 amino acids being sufficient for targeting. Binding studies showed that N-P0MC(1-76) bound to secretory granule membranes specifically on the luminal side and in a pH-sensitive manner. Only N-POMC(1-76) bound optimally to secretory granule membranes at pH 5 to 6.5, but not the ACTH(1-39) (mid), corticotropin-like intermediate lobe peptide (CLIP) and beta lipotropin (C-terminal) domains of POMC. Such binding may be involved in the mechanism of sorting POMC to the regulated secretory pathway.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 22:45:50