Origin of the Beta Cells of the Islets of Langerhans is Further Questioned by the Expression of Neuronal Intermediate Filament Proteins, Peripherin and NF-L, in the Rat Insulinoma RIN5F Cell Line

1991 ◽  
Vol 13 (6) ◽  
pp. 424-432 ◽  
Author(s):  
Michel Escurat ◽  
Karima Djabali ◽  
Claude Huc ◽  
Françoise Landon ◽  
Chantal Bécourt ◽  
...  
Keyword(s):  
Cell Line ◽  
Beta Cells ◽  
Islets Of Langerhans ◽  
Intermediate Filament ◽  
Intermediate Filament Proteins ◽  
Neuronal Intermediate Filament Proteins ◽  
Rat Insulinoma

scholarly journals Tissue type-specific expression of intermediate filament proteins in a cultured epithelial cell line from bovine mammary gland

1983 ◽  
Vol 96 (1) ◽  
pp. 37-50 ◽  
Author(s):  
E Schmid ◽  
DL Schiller ◽  
C Grund ◽  
J Stadler ◽  
WW Franke
Keyword(s):  
Mammary Gland ◽  
Epithelial Cell ◽  
Cell Line ◽  
Cell Lines ◽  
Intermediate Filament ◽  
Striking Difference ◽  
Intermediate Filament Proteins ◽  
Cell Clones ◽  
Vimentin Filaments

Different clonal cell lines have been isolated from cultures of mammary gland epithelium of lactating cow's udder and have been grown in culture media containing high concentrations of hydrocortisone, insulin, and prolactin. These cell (BMGE+H), which grow in monolayers of typical epithelial appearance, are not tightly packed, but leave intercellular spaces spanned by desmosomal bridges. The cells contain extended arrays of cytokeratin fibrils, arranged in bundles attached to desmosomes. Gel electophoresis show that they synthesize cytokeratins similar, if not identical, to those found in bovine epidermis and udder, including two large (mol wt 58,500 and 59,000) and basic (pH range: 7-8) and two small (mol wt 45,500 and 50,000) and acidic (pH 5.32 and 5.36) components that also occur in phosphorylated forms. Two further cytokeratins of mol wts 44,000 (approximately pH 5.7) and 53,000 (pH 6.3) are detected as minor cytokeratins in some cell clones. BMGE+H cells do not produce vimentin filaments as determined by immunofluorescence microscopy and gel electrophoresis. By contrast, BMGE-H cells, which have emerged from the same original culture but have been grown without hormones added, are not only morphologically different, but also contain vimentin filaments and a different set of cytokeratins, the most striking difference being the absence of the two acidic cytokeratins of mol wt 50,000 and 45,500. Cells of the BMGE+H line are characterized by an unusual epithelial morphology and represent the first example of a nonmalignant permanent cell line in vitro that produces cytokeratin but not vimentin filaments. The results show that (a) tissue-specific patterns of intermediate filament expression can be maintained in permanent epithelial cell lines in culture, at least under certain growth conditions; (b) loss of expression of relatively large, basic cytokeratins is not an inevitable consequence of growth of epithelial cells in vitro. Our results further show that, during culturing, different cell clones with different cytoskeletal composition can emerge from the same cell population and suggest that the presence of certain hormones may have an influence on the expression of intermediate filament proteins.

scholarly journals Quantitative phosphoproteomic analysis of neuronal intermediate filament proteins (NF‐M/H) in Alzheimer's disease by iTRAQ

2010 ◽  
Vol 24 (11) ◽  
pp. 4396-4407 ◽  
Author(s):  
Parvathi Rudrabhatla ◽  
Philip Grant ◽  
Howard Jaffe ◽  
Michael J. Strong ◽  
Harish C. Pant
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Intermediate Filament ◽  
Intermediate Filament Proteins ◽  
Neuronal Intermediate Filament Proteins

scholarly journals Characterisation of neurofilament protein NF70 mRNA from the gastropod Helix aspersa reveals that neuronal and non-neuronal intermediate filament proteins of cerebral ganglia arise from separate lamin-related genes

1995 ◽  
Vol 108 (11) ◽  
pp. 3581-3590 ◽  
Author(s):  
J. Adjaye ◽  
U. Plessmann ◽  
K. Weber ◽  
H. Dodemont
Keyword(s):  
Sequence Analysis ◽  
Intermediate Filament ◽  
Cerebral Ganglion ◽  
Helix Aspersa ◽  
Neurofilament Protein ◽  
Intermediate Filament Proteins ◽  
Nuclear Lamins ◽  
Untranslated Sequence ◽  
Cerebral Ganglia ◽  
Neuronal Intermediate Filament Proteins

The neuronal cytoplasmic intermediate filament (IF) protein HeNF70 of the gastropod Helix aspersa is identified by sequence analysis of the corresponding 4,600 bp cDNA isolated from a cerebral ganglion cDNA library. HeNF70 shares 60% sequence identity with the neuronal LoNF70 protein of the cephalopod Loligo pealei and only 36% identity with the Helix non-neuronal IF-A protein. All three molluscan IF proteins display the lamin-type extended coil 1b subdomain harbouring six additional heptads and all have long C-terminal sequences with substantial homology to the tail domains of nuclear lamins. The lamin-like tail domains of the two neurofilament proteins share a unique motif comprising 13 residues, which is absent from Helix IF-A and all other known non-neuronal IF proteins. HeNF70 is encoded by a 9.5 kb RNA transcript. The very long 7.2 kb 3′-untranslated sequence contains a unique 26 nucleotide repeat extending over 0.5 kb in its 5′-region. The HeNF70 mRNA is expressed at low abundancy in cerebral ganglia but not in any of the 13 non-neuronal tissues tested. In contrast, all tissues express at fairly high levels the same 4.6 and 4.2 kb mRNAs encoding the Helix non-neuronal IF-A/B proteins. Blot hybridisation studies on genomic DNA and ganglion mRNA with subprobes from the cloned HeNF70 cDNA, as well as sequence analysis of an RT-PCR generated partial cDNA encoding a putative HeNF60 protein, indicate at least two different neuronal IF genes in Helix.

Analysis of the roles of the head domains of type IV rat neuronal intermediate filament proteins in filament assembly using domain-swapped chimeric proteins

1999 ◽  
Vol 112 (13) ◽  
pp. 2233-2240
Author(s):  
G.Y. Ching ◽  
R.K. Liem
Keyword(s):  
Intermediate Filament ◽  
Self Assembly ◽  
Chimeric Proteins ◽  
Filament Formation ◽  
Intermediate Filament Proteins ◽  
L Protein ◽  
Type Iv ◽  
Filament Assembly ◽  
Head Domain ◽  
Neuronal Intermediate Filament Proteins

Type IV neuronal intermediate filament proteins consist of alpha-internexin, which can self-assemble into filaments and the neurofilament triplet proteins, which are obligate heteropolymers, at least in rodents. These IF proteins therefore provide good systems for elucidating the mechanism of intermediate filament assembly. To analyze the roles of the head domains of these proteins in contributing to their differential assembly properties, we generated chimeric proteins by swapping the head domains between rat alpha-internexin and either rat NF-L or NF-M and examined their assembly properties in transfected cells that lack their own cytoplasmic intermediate filament network. Lalphaalpha and Malphaalpha, the chimeric proteins generated by replacing the head domain of alpha-internexin with those of NF-L and NF-M, respectively, were unable to self-assemble into filaments. In contrast, alphaLL, a chimeric NF-L protein generated by replacing the head domain of NF-L with that of alpha-internexin, was able to self-assemble into filaments, whereas MLL, a chimeric NF-L protein containing the NF-M head domain, was unable to do so. These results demonstrate that the alpha-internexin head domain is essential for alpha-internexin's ability to self-assemble. While coassembly of Lalphaalpha with NF-M and coassembly of Malphaalpha with NF-L resulted in formation of filaments, coassembly of Lalphaalpha with NF-L and coassembly of Malphaalpha with NF-M yielded punctate patterns. These coassembly results show that heteropolymeric filament formation requires that one partner has the NF-L head domain and the other partner has the NF-M head domain. Thus, the head domains of rat NF-L and NF-M play important roles in determining the obligate heteropolymeric nature of filament formation. The data obtained from these self-assembly and coassembly studies provide some new insights into the mechanism of intermediate filament assembly.

scholarly journals Absence of the Mid-sized Neurofilament Subunit Decreases Axonal Calibers, Levels of Light Neurofilament (NF-L), and Neurofilament Content

1998 ◽  
Vol 141 (3) ◽  
pp. 727-739 ◽  
Author(s):  
Gregory A. Elder ◽  
Victor L. Friedrich ◽  
Paolo Bosco ◽  
Chulho Kang ◽  
Andrei Gourov ◽  
...  
Keyword(s):  
Nervous System ◽  
Intermediate Filament ◽  
Small Diameter ◽  
Behavioral Phenotype ◽  
Structural Defects ◽  
Null Mutation ◽  
Myelinated Axons ◽  
Intermediate Filament Proteins ◽  
Axonal Diameter ◽  
Neuronal Intermediate Filament Proteins

Neurofilaments (NFs) are prominent components of large myelinated axons and probably the most abundant of neuronal intermediate filament proteins. Here we show that mice with a null mutation in the mid-sized NF (NF-M) subunit have dramatically decreased levels of light NF (NF-L) and increased levels of heavy NF (NF-H). The calibers of both large and small diameter axons in the central and peripheral nervous systems are diminished. Axons of mutant animals contain fewer neurofilaments and increased numbers of microtubules. Yet the mice lack any overt behavioral phenotype or gross structural defects in the nervous system. These studies suggest that the NF-M subunit is a major regulator of the level of NF-L and that its presence is required to achieve maximal axonal diameter in all size classes of myelinated axons.

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