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Titolo:
IDENTIFICATION AND CHARACTERIZATION OF A NOVEL HUMAN NEUTROPHIL PROTEIN RELATED TO THE S100 FAMILY
Autore:
GUIGNARD F; MAUEL J; MARKERT M;
Indirizzi:
CHU VAUDOIS,CENT LAB CLIN CHEM CH-1011 LAUSANNE SWITZERLAND CHU VAUDOIS,CENT LAB CLIN CHEM CH-1011 LAUSANNE SWITZERLAND INST BIOCHEM EPALINGES SWITZERLAND
Titolo Testata:
Biochemical journal
, volume: 309, anno: 1995,
parte:, 2
pagine: 395 - 401
SICI:
0264-6021(1995)309:<395:IACOAN>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
CALCIUM-BINDING PROTEINS; PLASMA-MEMBRANE; MOLECULAR-CLONING; NADPH OXIDASE; DIFFERENTIATION; EXPRESSION; COMPLEX; ELECTROPHORESIS; MACROPHAGES; ACTIVATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
40
Recensione:
Indirizzi per estratti:
Citazione:
F. Guignard et al., "IDENTIFICATION AND CHARACTERIZATION OF A NOVEL HUMAN NEUTROPHIL PROTEIN RELATED TO THE S100 FAMILY", Biochemical journal, 309, 1995, pp. 395-401

Abstract

A rabbit polyclonal antibody raised against myeloid-related protein 8(MRP-8), a protein of the S100 family, recognized another S100 protein (MRP-14) as well as a protein of 6.5 kDa (p6) in the cytosol of resting neutrophils. p6 was found to be a novel member of the S100 family. It consisted of two isoforms with pi values of 6.2 (the minor form, p6a) and 6.3 (the major form, p6b) and constituted 5% of the total cytosolic proteins. Both isoforms were also demonstrated in the cytosol ofmonocytes, but not in lymphocytes, as previously shown for MRP-8 and MRP-14. Only the major isoform bound radioactive Ca2+, as also observed for MRP-8, whereas the different variants of MRP-14 were all labelled. On neutrophil activation with opsonized zymosan, a stimulant known to require extracellular Ca2+, 58% of p6a and 42% of p6b was translocated to the membrane. With phorbol 12-myristate 13-acetate, a Ca2+-independent stimulant, no translocation was detected. This translocation pattern was similar to that observed with MRP-8 and MRP-14. In addition, p6, MRP-8 and MRP-14 were specifically associated with the cytoskeletal fraction of the membrane. The Ca2+-dependent translocation of the novel S100 protein in parallel with MRP-8 and MRP-14 suggests a role for these proteins in regulating the Ca2+ signal to the membrane cytoskeleton and thus in regulating neutrophil activation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/07/20 alle ore 12:29:08