scholarly journals Keratin Filament

2020 ◽  
Author(s):  
Keyword(s):  
Keratin Filament

scholarly journals Keratins determine network stress responsiveness in reconstituted actin-keratin filament systems

Soft Matter ◽  
2021 ◽  
Author(s):  
Iman Elbalasy ◽  
Paul Mollenkopf ◽  
Cary Tutmarc ◽  
Harald Herrmann ◽  
Jörg Schnauß
Keyword(s):  
Cell Mechanics ◽  
Major Determinant ◽  
Stress Responsiveness ◽  
Keratin Filament

The cytoskeleton is a major determinant of cell mechanics, and alterations in the central mechanical aspects of cells are observed during many pathological situations. Therefore, it is essential to investigate...

scholarly journals Keratin Filament Suspensions Show Unique Micromechanical Properties

1999 ◽  
Vol 274 (27) ◽  
pp. 19145-19151 ◽  
Author(s):  
Linglei Ma ◽  
Jingyuan Xu ◽  
Pierre A. Coulombe ◽  
Denis Wirtz
Keyword(s):  
Micromechanical Properties ◽  
Keratin Filament

scholarly journals Keratin 8 Phosphorylation by p38 Kinase Regulates Cellular Keratin Filament Reorganization

2002 ◽  
Vol 277 (13) ◽  
pp. 10775-10782 ◽  
Author(s):  
Nam-On Ku ◽  
Salman Azhar ◽  
M. Bishr Omary
Keyword(s):  
P38 Kinase ◽  
Keratin Filament ◽  
Keratin 8

scholarly journals Epiplakin Is Dispensable for Skin Barrier Function and for Integrity of Keratin Network Cytoarchitecture in Simple and Stratified Epithelia

2006 ◽  
Vol 26 (2) ◽  
pp. 559-568 ◽  
Author(s):  
Daniel Spazierer ◽  
Peter Fuchs ◽  
Siegfried Reipert ◽  
Irmgard Fischer ◽  
Matthias Schmuth ◽  
...  
Keyword(s):  
Actin Filaments ◽  
Primary Cultures ◽  
Embryonic Stem ◽  
Skin Barrier ◽  
Skin Barrier Function ◽  
Wild Type ◽  
Primary Hepatocytes ◽  
Specific Expression ◽  
Keratin Filament ◽  
Deficient Mice

ABSTRACT Epiplakin, a giant epithelial protein of >700 kDa, belongs to the plakin family of cytolinker proteins. It represents an atypical family member, however, as it consists entirely of plakin repeat domains but lacks any of the other domains commonly shared by plakins. Hence, its putative function as a cytolinker protein remains to be shown. To investigate epiplakin's biological role, we generated epiplakin-deficient mice by gene targeting in embryonic stem cells. Epiplakin-deficient mice were viable and fertile, without developing any discernible phenotype. Ultrastructurally, their epidermis revealed no differences compared to wild-type littermates, and cornified envelopes isolated from skin showed no alterations in shape or stability. Furthermore, neither embryonal formation nor later function of the epithelial barrier was affected. In primary cultures of epiplakin-deficient keratinocytes, the organization of actin filaments, microtubules, and keratin networks was found to be normal. Similarly, no alterations in keratin network organization were observed in simple epithelia of small intestine and liver or in primary hepatocytes. We conclude that, despite epiplakin's abundant and highly specific expression in stratified and simple epithelia, its absence in mice does not lead to severe skin dysfunctions, nor has it detectable consequences for keratin filament organization and cytoarchitecture of cells.

scholarly journals Posttranslational regulation of keratins: degradation of mouse and human keratins 18 and 8.

1989 ◽  
Vol 9 (4) ◽  
pp. 1553-1565 ◽  
Author(s):  
D A Kulesh ◽  
G Ceceña ◽  
Y M Darmon ◽  
M Vasseur ◽  
R G Oshima
Keyword(s):  
Cell Types ◽  
Immunofluorescent Staining ◽  
Type I ◽  
Type Ii ◽  
Tail Domain ◽  
Proteolytic System ◽  
L Cells ◽  
Adult Mice ◽  
3T3 Fibroblasts ◽  
Keratin Filament

Human keratin 18 (K18) and keratin 8 (K8) and their mouse homologs, Endo B and Endo A, respectively, are expressed in adult mice primarily in a variety of simple epithelial cell types in which they are normally found in equal amounts within the intermediate filament cytoskeleton. Expression of K18 alone in mouse L cells or NIH 3T3 fibroblasts from either the gene or a cDNA expression vector results in K18 protein which is degraded relatively rapidly without the formation of filaments. A K8 cDNA containing all coding sequences was isolated and expressed in mouse fibroblasts either singly or in combination with K18. Immunoprecipitation of stably transfected L cells revealed that when K8 was expressed alone, it was degraded in a fashion similar to that seen previously for K18. However, expression of K8 in fibroblasts that also expressed K18 resulted in stabilization of both K18 and K8. Immunofluorescent staining revealed typical keratin filament organization in such cells. Thus, expression of a type I and a type II keratin was found to be both necessary and sufficient for formation of keratin filaments within fibroblasts. To determine whether a similar proteolytic system responsible for the degradation of K18 in fibroblasts also exists in simple epithelial cells which normally express a type I and a type II keratin, a mutant, truncated K18 protein missing the carboxy-terminal tail domain and a conserved region of the central, alpha-helical rod domain was expressed in mouse parietal endodermal cells. This resulted in destabilization of endogenous Endo A and Endo B and inhibition of the formation of typical keratin filament structures. Therefore, cells that normally express keratins contain a proteolytic system similar to that found in experimentally manipulated fibroblasts which degrades keratin proteins not found in their normal polymerized state.

scholarly journals Cytoskeleton in motion: the dynamics of keratin intermediate filaments in epithelia

2011 ◽  
Vol 194 (5) ◽  
pp. 669-678 ◽  
Author(s):  
Reinhard Windoffer ◽  
Michael Beil ◽  
Thomas M. Magin ◽  
Rudolf E. Leube
Keyword(s):  
Intermediate Filaments ◽  
Molecular Mechanisms ◽  
Protein Biosynthesis ◽  
Epithelial Tissue ◽  
Multistep Process ◽  
Keratin Filament ◽  
Cell Type Specific ◽  
Cytoskeletal Networks ◽  
Microtubule Networks ◽  
Keratin Intermediate Filaments

Epithelia are exposed to multiple forms of stress. Keratin intermediate filaments are abundant in epithelia and form cytoskeletal networks that contribute to cell type–specific functions, such as adhesion, migration, and metabolism. A perpetual keratin filament turnover cycle supports these functions. This multistep process keeps the cytoskeleton in motion, facilitating rapid and protein biosynthesis–independent network remodeling while maintaining an intact network. The current challenge is to unravel the molecular mechanisms underlying the regulation of the keratin cycle in relation to actin and microtubule networks and in the context of epithelial tissue function.

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