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Titolo:
S100: a multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles
Autore:
Donato, R;
Indirizzi:
Univ Perugia, Sect Anat, Dept Expt & Biochem Sci, I-06122 Perugia, Italy Univ Perugia Perugia Italy I-06122 & Biochem Sci, I-06122 Perugia, Italy
Titolo Testata:
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY
fascicolo: 7, volume: 33, anno: 2001,
pagine: 637 - 668
SICI:
1357-2725(200107)33:7<637:SAMFOC>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACTIN-CAPPING PROTEIN; S100-BETA TRANSGENIC MICE; SMOOTH-MUSCLE CALDESMON; PHOTORECEPTOR GUANYLATE-CYCLASE; SARCOPLASMIC-RETICULUM VESICLES; GLIAL-NEURONAL INTERACTIONS; FIBRILLARY ACIDIC PROTEIN; MESSENGER-RNA EXPRESSION; CELL-SURFACE RECEPTOR; YEAST 2-HYBRID SYSTEM;
Keywords:
S100; calcium; structure; target proteins; receptor; signaling;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
279
Recensione:
Indirizzi per estratti:
Indirizzo: Donato, R Univ Perugia, Sect Anat, Dept Expt & Biochem Sci, Via Giochetto,CP 81 Succ3, I-06122 Perugia, Italy Univ Perugia Via Giochetto,CP 81 Succ 3Perugia Italy I-06122 y
Citazione:
R. Donato, "S100: a multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles", INT J BIO C, 33(7), 2001, pp. 637-668

Abstract

S100 is a multigenic family of non-ubiquitous Ca2+-modulated proteins of the EF-hand type expressed in vertebrates exclusively and implicated in intracellular and extracellular regulatory activities. Within cells, most of S100 members exist in the form of antiparallely packed homodimers (in some cases heterodimers), capable of functionally crossbridging two homologous or heterologous target proteins in a Ca2+-dependent (and, in some instances, Ca2+-independent) manner. S100 oligomers can also form, under the non-reducing conditions found in the extracellular space and/or within cells upon changes in the cell redox status. Within cells, S100 proteins have been implicated in the regulation of protein phosphorylation, some enzyme activities, the dynamics of cytoskeleton components, transcription factors, Ca2+ homeostasis, and cell proliferation and differentiation. Certain S100 members arereleased into the extracellular space by an unknown mechanism. Extracellular S100 proteins stimulate neuronal survival and/or differentiation and astrocyte proliferation, cause neuronal death via apoptosis, and stimulate (insome cases) or inhibit (in other cases) the activity of inflammatory cells. A cell surface receptor, RAGE, has been identified on inflammatory cells and neurons for S100A12 and S100B, which transduces S100A12 and S100B effects. It is not known whether RAGE is a universal S100 receptor, S100 membersinteract with other cell surface receptors, or S100 protein interaction with other extracellular factors specifies the biological effects of a given S100 protein on a target cell. The variety of intracellular target proteinsof S100 proteins and, in some cases, of a single S100 protein, and the cell specificity of expression of certain S100 members suggest that these proteins might have a role in the fine regulation of effector proteins and/or specific steps of signaling pathways/cellular functions. Future analyses should discriminate between functionally relevant S100 interactions with target proteins and in vitro observations devoid of physiological importance. (C) 2001 Elsevier Science Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/04/20 alle ore 07:37:36