scholarly journals Identification and developmental expression of a novel low molecular weight neuronal intermediate filament protein expressed in Xenopus laevis

1992 ◽  
Vol 12 (8) ◽  
pp. 3010-3024 ◽  
Author(s):  
LR Charnas ◽  
BG Szaro ◽  
H Gainer
Keyword(s):  
Molecular Weight ◽  
Xenopus Laevis ◽  
Intermediate Filament ◽  
Developmental Expression ◽  
Low Molecular Weight ◽  
Intermediate Filament Protein ◽  
Filament Protein

scholarly journals A High Molecular Weight Intermediate Filament-associated Protein in BHK-21 Cells Is Nestin, a Type VI Intermediate Filament Protein

1999 ◽  
Vol 274 (14) ◽  
pp. 9881-9890 ◽  
Author(s):  
Peter M. Steinert ◽  
Ying-Hao Chou ◽  
Veena Prahlad ◽  
David A. D. Parry ◽  
Lyuben N. Marekov ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Intermediate Filament ◽  
Intermediate Filament Protein ◽  
Filament Protein

scholarly journals A nontetrameric species is the major soluble form of keratin in Xenopus oocytes and rabbit reticulocyte lysates.

1996 ◽  
Vol 132 (1) ◽  
pp. 153-165 ◽  
Author(s):  
J B Bachant ◽  
M W Klymkowsky
Keyword(s):  
Molecular Weight ◽  
Intermediate Filament ◽  
Apparent Molecular Weight ◽  
Soluble Form ◽  
Intermediate Filament Protein ◽  
Type I ◽  
Type Ii ◽  
Cell Biol ◽  
Reticulocyte Lysates ◽  
Filament Protein

Inside the interphase cell, approximately 5% of the total intermediate filament protein exists in a soluble form. Past studies using velocity gradient sedimentation (VGS) indicate that soluble intermediate filament protein exists as an approximately 7 S tetrameric species. While studying intermediate filament assembly dynamics in the Xenopus oocyte, we used both VGS and size-exclusion chromatography (SEC) to analyze the soluble form of keratin. Previous studies (Coulombe, P. A., and E. Fuchs. 1990. J. Cell Biol. 111:153) report that tetrameric keratins migrate on SEC with an apparent molecular weight of approximately 150,000; the major soluble form of keratin in the oocyte, in contrast, migrates with an apparent molecular weight of approximately 750,000. During oocyte maturation, the keratin system disassembles into a soluble form (Klymkowsky, M. W., L. A. Maynell, and C. Nislow. 1991. J. Cell Biol. 114:787) and the amount of the 750-kD keratin complex increases dramatically. Immunoprecipitation analysis of soluble keratin from matured oocytes revealed the presence of type I and type II keratins, but no other stoichiometrically associated polypeptides, suggesting that the 750-kD keratin complex is composed solely of keratin. To further study the formation of the 750-kD keratin complex, we used rabbit reticulocyte lysates (RRL). The 750-kD keratin complex was formed in RRLs contranslating type I and type II Xenopus keratins, but not when lysates translated type I or type II keratin RNAs alone. The 750-kD keratin complex could be formed posttranslationally in an ATP-independent manner when type I and type II keratin translation reactions were mixed. Under conditions of prolonged incubation, such as occur during VGS analysis, the 750-kD keratin complex disassembled into a 7 S (by VGS), 150-kD (by SEC) form. In urea denaturation studies, the 7 S/150-kD form could be further disassembled into an 80-kD species that consists of cofractionating dimeric and monomeric keratin. Based on these results, the 750-kD species appears to be a supratetrameric complex of keratins and is the major, soluble form of keratin in both prophase and M-phase oocytes, and RRL reactions.

scholarly journals Phosphorylation of the peripherin 58-kDa neuronal intermediate filament protein

1989 ◽  
Vol 264 (8) ◽  
pp. 4619-4627
Author(s):  
J M Aletta ◽  
M L Shelanski ◽  
L A Greene
Keyword(s):  
Intermediate Filament ◽  
Intermediate Filament Protein ◽  
Filament Protein
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