Molecular And Cellular Biology Of Intermediate Filaments

Steinert, Peter M.

doi:10.1146/annurev.biochem.57.1.593

Cited by 211 publications

(242 citation statements)

References 130 publications

Supporting

Mentioning

236

Contrasting

Unclassified

Order By: Relevance

“…This result is consistent with the colocalization of vimentin and cytokeratin in many cultured cells (Steinert and Roop, 1988;Lazarides, 1980). These results, taken together, demonstrate that antibodies against MDM1 recognize the intermediate filament network in a variety of animal ceils.…”

Section: Antibodies To the Mdmi Protein Recognize The Intermediate L~supporting

confidence: 88%

“…Third, structural predictions suggest that the MDM1 protein contains a high a-helical content, a property shared by many filamentous proteins. Finally, the MDM1 protein demonstrates solubility properties similar to those described for intermediate filament proteins (Steinert and Roop, 1988;Lazarides, 1980). In particular, MDM1 remained largely in the insoluble fraction upon extraction of disrupted yeast ceils with the detergent Triton X-100 (S. McConnell, unpublished observations).…”

Section: Tion Gene Disruption Experiments Demonstrated That Mdm1mentioning

confidence: 77%

See 1 more Smart Citation

Nuclear and mitochondrial inheritance in yeast depends on novel cytoplasmic structures defined by the MDM1 protein

McConnell¹

1992

Trends in Cell Biology

View full text Add to dashboard Cite

Section: Antibodies To the Mdmi Protein Recognize The Intermediate L~supporting

confidence: 88%

Section: Tion Gene Disruption Experiments Demonstrated That Mdm1mentioning

confidence: 77%

Nuclear and mitochondrial inheritance in yeast depends on novel cytoplasmic structures defined by the MDM1 protein

McConnell¹

1992

Trends in Cell Biology

View full text Add to dashboard Cite

“…Vimentin is a cytoskeletal, intermediate filament protein very abundant during development, which can be found in immature glial cells, including radial glia (Bignami et al, 1982;Dahl et al, 1981), and in highly undifferentiated neuronal precursors (Cochard and Paulin, 1984). In adult animals, although mainly replaced by other intermediate filament proteins such as GFAP in glial cells and neurofilament triplet protein in neurons (see Steinert and Roop, 1988;Gorham et al, 1991), vimentin persists in many cell populations which are enriched in carnosine-related dipeptides, namely cerebellar Bergmann glia, ependymal cells, tanycytes, a sub-population of astrocytes in large myelinated bundles (Shaw et al, 1981;Pixley and De Vellis, 1984), radial glia-like cells in the supraoptic nucleus (Bonfanti et al, 1993), astrocytes of the glial tubes , and olfactory receptor neurons Gorham et al, 1991). This transition from a precursor type of intermediate filament proteins (vimentin), to more specialized ones, has also been described to occur in skeletal muscle cells (Granger and Lazarides, 1979).…”

Section: Discussionmentioning

confidence: 99%

Carnosine-related dipeptides in the mammalian brain

Bonfanti

Peretto

Marchis

et al. 1999

Progress in Neurobiology

188

107

View full text Add to dashboard Cite

-Carnosine and structurally related dipeptides are a group of histidine-containing molecules widely distributed in vertebrate organisms and particularly abundant in muscle and nervous tissue. Although many theories have been proposed, the biological function(s) of these compounds in the nervous system remains enigmatic. The purpose of this article is to review the distribution of carnosine-related dipeptides in the mammalian brain, with particular reference to some cell populations wherein these molecules have been demonstrated to occur very recently. The high expression of carnosine in the mammalian olfactory receptor neurons led to infer that this dipeptide could play a role as a neurotransmitter/modulator in olfaction. This prediction, which has not yet been fully demonstrated, does not explain the localization of carnosine-related dipeptides in other cell types, such as glial and ependymal cells. A recent demonstration of high carnosine-like immunoreactivity in the subependymal layer of rodents, an area of the forebrain which shares with the olfactory neuroepithelium the occurrence of continuous neurogenesis during adulthood, supports the hypothesis that carnosine-related dipeptides could be implicated in some forms of structural plasticity. However, the particular distribution of these molecules in the subependymal layer, along with their expression in glial/ependymal cell populations, suggests that they are not directly linked to cell migration or cell renewal. In the absence of a unified theory about the role of carnosine-related dipeptides in the nervous system, some common features shared by different cell populations of the mammalian brain which contain these molecules are discussed.

show abstract

“…The rod is flanked by nonhelical head and tail segments that are variable in size and sequence. The helices contain heptad repeats of hydrophobic residues, producing a hydrophobic seal on the helical surface, thus enabling the coiled-coil heterodimerization of parallel aligned molecules of K14 and K5, or K10 and K1 (Steinert and Freedberg, 1991;Cheng et al, 1992).…”

Section: Discussionmentioning

confidence: 99%

A keratin K10 gene mutation in a Japanese patient with epidermolytic hyperkeratosis

et al. 1997

View full text Add to dashboard Cite

SummaryEpidermolytic hyperkeratosis (EHK), or bullous congenital ichthyosiform erythroderma, is characterized by generalized erythroderma, ichthyosiform skin and blistering, and is caused by an aberration of the keratin intermediate filaments° In this study, we examined keratin K10 and 1 gene mutations in a Japanese EHK patient who had severe ichthyosiform erythroderma at birth and developed subsequent blistering. The patient had a G to A transition at codon 156 of the keratin K10 gene, which resulted in an arginine (Arg)--~histidine (His) substitution in the helix initiation peptide of the highly-conserved IA domain in keratin K10. This .is the first mutation report of a Japanese patient with EHK, although the position and mode of the mutation identified here did not differ from those in reported Western cases.

show abstract

Molecular And Cellular Biology Of Intermediate Filaments

Abstract: Axons of many Arthropoda do not contain ncurofilamcnts (33), d Protein detectt,d by use of the "universal" IF antibody (34), the epitope of which is presumably a canonical feature of the rod domain.

Cited by 211 publications

References 130 publications

Nuclear and mitochondrial inheritance in yeast depends on novel cytoplasmic structures defined by the MDM1 protein

Nuclear and mitochondrial inheritance in yeast depends on novel cytoplasmic structures defined by the MDM1 protein

Carnosine-related dipeptides in the mammalian brain

A keratin K10 gene mutation in a Japanese patient with epidermolytic hyperkeratosis

Contact Info

Product

Resources

About