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F Gros

Publications and source records attributed to F Gros.

275 records · Page 16Linked to original sources

Regulation of peripherin in mouse neuroblastoma and rat PC 12 pheochromocytoma cell lines.

Peripherin (Formerly the Y protein) is found in the peripheral nervous system. This Triton-insoluble protein is characterized by its isoelectric point (5.6), its apparent molecular weight (56,000 daltons) and its peptide map. Peripherin was also observed in a mouse neuroblastoma cell line, NIE 115, where its expression appeared regulated by the presence of an inducer of morphological differentiation. In order to analyze more precisely this control, the presence of peripherin was investigated in several neuroblastoma cell lines which exhibit different morphological patterns of differentiation and in the rat pheochromocytoma PC 12 cell line. Differentiation of these cells was induced with 1-methylcyclohexane carboxylic acid (CCA) and nerve growth factor (NGF), respectively. Peripherin was found in these different cell lines. Moreover, the cellular amount of peripherin appraised by [35S]-methionine incorporation was significatively increased in differentiated cells. In contrast, other cytoskeletal components did not undergo a similar raise. The level at which the control of the peripherin content takes place was studied in a cell-free translation system. Poly(A)-rich RNAs extracted from growing or differentiated NIE 115 cells directed the synthesis of similar amounts of peripherin in a reticulocyte lysate. In contrast, polysomes prepared from differentiated cells and the corresponding polysomal RNA programmed in vitro the synthesis of twice more peripherin than polysomes or polysomal RNA from growth-phase cells. Since peripherin synthesis is enhanced 5 times in living cells, it seems probable that the cellular amount of peripherin is controlled partly at the translational level and partly at the turn-over level.

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Peripherin, a new member of the intermediate filament protein family.

Peripherin, a Triton-insoluble protein, whose distribution was found to be restricted to neurons in the rodent and human peripheral nervous system, was characterized by its electrophoretic features (isoelectric point: 5.6; molecular weight: 56,000 daltons) and by its peptidic map after limited proteolysis. Comparative peptide analysis of the 70,000-dalton subunit of neurofilaments (70K NFP), vimentin and peripherin, was performed by two different methods; limited proteolysis with Staphylococcus aureus V8 protease yields a different peptidic map for each protein; treatment with N-chlorosuccinimide, which cleaves preferentially at tryptophan residues, yields only two peptides from each protein: the size of the two fragments indicates that these proteins possess a single tryptophan residue located in the central part of the molecule. A rabbit antiserum raised against mouse peripherin decorated an intracellular filamentous network in mouse neuroblastoma NIE 115 cell line. The IgG fraction of the antiserum recognizes peripherin and the smallest subunit of the neurofilament triplet (70K NFP)--but not vimentin--whereas a monoclonal anti-70K NFP recognizes only the 70K NFP. Moreover, peripherin displays the common antigenic determinant shared by all intermediate filament proteins. Hence, we propose that peripherin represents a new member of the intermediate filament protein family, and might belong to the neurofilament class.

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