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Titolo:
Molecular parameters of type IV alpha-internexin and type IV-type III alpha-internexin-vimentin copolymer intermediate filaments
Autore:
Steinert, PM; Marekov, LN; Parry, DAD;
Indirizzi:
NIAMS, Skin Biol Lab, NIH, Bethesda, MD 20892 USA NIAMS Bethesda MD USA 20892 S, Skin Biol Lab, NIH, Bethesda, MD 20892 USA Massey Univ, Inst Fundamental Sci, Palmerston North, New Zealand Massey Univ Palmerston North New Zealand Palmerston North, New Zealand
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 3, volume: 274, anno: 1999,
pagine: 1657 - 1666
SICI:
0021-9258(19990115)274:3<1657:MPOTIA>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
COILED-COIL MOLECULES; TRANSMISSION ELECTRON-MICROSCOPY; EPIDERMAL KERATIN FILAMENTS; NF-L; NEUROFILAMENT PROTEINS; END DOMAINS; INVITRO; PERIPHERIN; EXPRESSION; CELLS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
59
Recensione:
Indirizzi per estratti:
Indirizzo: Steinert, PM NIAMS, Skin Biol Lab, NIH, Bldg 6,Rm 425, Bethesda, MD 20892 USA NIAMS Bldg 6,Rm 425 Bethesda MD USA 20892 hesda, MD 20892 USA
Citazione:
P.M. Steinert et al., "Molecular parameters of type IV alpha-internexin and type IV-type III alpha-internexin-vimentin copolymer intermediate filaments", J BIOL CHEM, 274(3), 1999, pp. 1657-1666

Abstract

During neuronal development, a dynamic replacement mechanism occurs in which the type VI nestin and type III vimentin intermediate filament proteins are replaced by a series of type IV proteins beginning with alpha-internexin. We have explored molecular details of how the type III to type IV replacement process may occur. First, we have demonstrated by cross linking experiments that bacterially expressed forms of alpha-internexin and vimentin form heterodimer molecules in vitro that assemble into copolymer intermediatefilaments. We show using a urea disassembly assay that alpha-internexin molecules are likely to be more stable than those of vimentin. Second, by analyses of the induced cross-links, we have determined the axial lengths of alpha-internexin homodimer and alpha-internexin-vimentin heterodimer molecules and their modes of alignments in filaments. We report that these dimensions are the same as those reported earlier for vimentin homopolymer molecules and, by implication are also the same for the other neuronal type IV proteins. These data suggest that during neuronal development, alpha-internexin molecules are readily assimilated onto the pre-existing vimentin cytoskeletal intermediate filament network because the axial lengths and axial alignments of their molecules are the same. Furthermore, the dynamic replacement process may be driven by a positive equilibrium due to the increased stability of the alpha-internexin network.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/04/20 alle ore 06:30:07