Expression of stress fibers in bullfrog mesothelial cells in response to tension

Sugimoto, Kenkichi; Fujii, Sachiko; Yamashita, Kazuo

doi:10.1016/0014-4827(91)90271-u

Cited by 14 publications

(11 citation statements)

References 36 publications

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“…We also examined the effect of mechanical stretch on the actin cytoskeleton: all cells examined only showed typical epithelial patterns of actin distribution and there was no fragmentation of actin during the cyclical stretch. The formation of actin stress fibres in response to stretch has been previously reported (Shirinsky et al, 1989) and is particularly evident in response to unilateral stretching (Shirinsky et al, 1989;Sugimoto et al, 1991;Takemasa et al, 1998). Radial stretching was used here, which may not lead to the formation of actin stress fibres and may explain the absence of stress fibres in our experiments.…”

Section: Keratin Fragmentation Is Induced By Mechanical Stretch In Ebsupporting

confidence: 58%

Mechanical stress induces profound remodelling of keratin filaments and cell junctions inepidermolysis bullosa simplexkeratinocytes

Reverter

Andrews

James

et al. 2004

Journal of Cell Science

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IntroductionAs the flexible outer covering of the body, the properties of skin must accommodate continuous stretching forces. The skin must be strong enough to endure physical trauma yet be flexible enough to allow a large range of movement. A large contribution to the physical resilience of epidermal skin cells comes from the keratin intermediate filaments that they express, as was shown with the discoveries that the inherited skin fragility disorder epidermolysis bullosa simplex (EBS) is caused by mutations in keratin genes (Bonifas et al., 1991;Coulombe et al., 1991;Lane et al., 1992). In EBS, the basal layer cells of the epidermis exhibit fragility under mild physical trauma, resulting in blistering; in severe cases, electron microscopy characteristically reveals electron-dense keratin aggregates in basal keratinocytes of patients (AntonLamprecht and Schnyder, 1982).Keratins belong to the superfamily of intermediate filament proteins. Heterodimeric filaments of type I and type II keratins are expressed in a tissue-and cell-specific manner in epithelial cells (reviewed by Fuchs and Weber, 1994). Stratified epithelia such as the epidermis express K5/K14 in the basal layer of cells and K1/K10 in the suprabasal layers. The keratins form a cytoplasmic network of filaments that are connected to the plasma membrane at complex cell-cell junctions (desmosomes) and cell-substrate junctions (hemidesmosomes). Tissue integrity in the epidermis is maintained by a complex cytoskeleton interaction between the keratin filaments and desmosomes and hemidesmosomes. Keratins are linked into desmosomes through desmoplakin and into hemidesmosomes via plectin; desmosomes are connected from cell to cell by the transmembrane cadherins (desmogleins and desmocollins), and hemidesmosomes are connected to the extracellular matrix substrate by integrins (usually α 6 β 4 ) and BP180. Other proteins found in these zones include plakoglobin within the plaques of both junctions, plakophilin in desmosomes and BP230 in hemidesmosomes. The exact nature of interactions between all these components is not yet clear (for reviews see Borradori and Sonnenberg, 1996;Jones et al., 1998).The mutations that cause the severe (Dowling-Meara) type of EBS are mostly found in the highly conserved ends of the α-helical rod domains of keratins K5 or K14. These regions are particularly important in filament assembly (Herrmann and Aebi, 1998). There is a particularly mutagenic codon at residue 125 of K14, in the helix initiation motif, leading to the substitution of the arginine residue at this position (Coulombe et al., 1991); mutations at this residue account for approximately 70% of Dowling-Meara EBS cases (Porter and Lane, 2003). Morphological effects of most keratin mutations are hardly detectable in unstressed cultured keratinocytes but spontaneous keratin aggregates are characteristically seen in cells containing a K14-R125 mutation; this is in keeping with the theory that the helix initiation motif is crucial in normal filament assembly (Herrmann and Aebi...

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Section: Keratin Fragmentation Is Induced By Mechanical Stretch In Ebsupporting

confidence: 58%

Mechanical stress induces profound remodelling of keratin filaments and cell junctions inepidermolysis bullosa simplexkeratinocytes

Reverter

Andrews

James

et al. 2004

Journal of Cell Science

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“…Previous in vitro experiments showed that cyclic stretching applied to cells in culture causes the cells to become oriented perpendicular to the direction of stretching [10, 21, 22] consistent with in vivo results [23]. On the other hand, in cells exposed to unidirectional tension, the stress fibers become organized along the axis of tension [24]. …”

Section: Introductionsupporting

confidence: 70%

“…The mechanism underlying the organization of stress fibers that run perpendicular to the direction of blood flow is unclear, but it is likely that these “perpendicular” stress fibers respond to stretching force generated by blood pressure applied to the endothelial cells. In mesothelial cells subjected to single-direction stretching, stress fibers were aligned in the direction of stretch [24]. On the other hand, cells subjected to cyclic stretching became aligned perpendicular to the direction of stretching force [23].…”

Section: Discussionmentioning

confidence: 99%

Distribution of Cytoskeletal Components in Endothelial Cells in the Guinea Pig Renal Artery

Katoh

Noda

2012

International Journal of Cell Biology

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The cytoskeletal components of endothelial cells in the renal artery were examined by analysis of en face preparations under confocal laser scanning microscopy. Renal arterial endothelial cells were shown to be elongated along the direction of blood flow, while stress fibers ran perpendicular to the flow in the basal portion. Focal adhesions were observed along the stress fibers in dot-like configurations. On the other hand, stress fibers in the apical portion of cells ran along the direction of flow. The localizations of stress fibers and focal adhesions in endothelial cells in the renal artery differed from those of unperturbed aortic and venous endothelial cells. Tyrosine-phosphorylated proteins were mainly detected at the sites of cell-to-cell apposition, but not in focal adhesions. Pulsatile pressure and fluid shear stress applied over endothelial cells in the renal artery induce stress fiber organization and localization of focal adhesions. These observations suggest that the morphological alignment of endothelial cells along the direction of blood flow and the organization of cytoskeletal components are independently regulated.

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“…70,71 These actin-myosin fibers are linked to discrete points on the inner plasma membrane called focal adhesions, where dynamic protein complexes that contribute to cell adhesion to the extracellular matrix are localized. 72 Formation of stress fibers and focal adhesion complexes by MLC phosphorylation was one of the first functions identified for ROCK.…”

Section: Rock Functionsmentioning

confidence: 99%

Rho-associated coiled-coil containing kinases (ROCK)

2014

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In humans, ROCK1 and ROCK2 both contain 33 exons and are located on chromosome 18 (18q11.1) and 2 (2p24) respectively. The ROCK1 open reading frame encodes 1354 amino acids, whereas ROCK2 encodes 1388 amino acids. ROCK2 also has a reported splice variant, preferentially expressed in skeletal muscle, which results in the inclusion of 57 additional amino acids. 7 The two ROCK homologs shares 64% identity in their primary amino acid sequences, with the highest homology (92%) within the kinase domains and the coiled-coil domains being the most diverse (55%). 5 The kinase domains of ROCK are closely related to many homologous domains in this family, including dystrophia myotonica protein kinase (DMPK), myotonic dystrophy kinase related-Cdc42 related kinases (MRCK) α and β, and citron Rho-interacting kinase (CRIK) . To date, the crystal structures of the kinase domains from ROCK1, 8 ROCK2, 9 MRCKβ, 10 and DMPK 11 have been determined, which has highlighted the high degree of tertiary as well as primary similarity. N-terminal and carboxyl-terminal extensions of the ROCK kinase domains are essential for catalytic activity. 4,8,9 The ROCK kinase domains are located in the N-terminal region, which is followed by a central ~600 amino acid long amphipathic α-helix forming a coiledcoil region (Fig. 1).12 At the carboxyl-terminal region, there is a split pleckstrin homology (PH) domain, which is bisected by an internal cysteine-rich zinc finger-like motif domain (CRD). The two separate PH portions assemble together to form a typical PH domain that is attached by two short linkers to a separate CRD. 13The canonical Rho binding domain (RBD) forms a parallel coiled coil dimer, as revealed by crystal structure determinations, and binds exclusively to the switch I and switch II regions of GTP-bound active RhoA and RhoC.14,15 Two additional Rhointeracting domains were identified that can tightly interact with RhoA, which may cooperatively contribute to binding. 16 Crystal structure studies revealed that ROCK has two dimerization domains: the ~70 residue N-terminal dimerization region 8,9 and the coiled-coil helical regions.12 Charged residues in the coiled-coil might function as a hinge that allows the N-terminal kinase domains to interact with C-terminal inhibitory regions. Structural determination of full-length ROCK protein crystals will ultimately reveal how the various domains interact and the mechanism of auto-inhibition. Regulation of ROCK ActivityAlthough ROCK1 and ROCK2 have highly related functional domains and significant amino acid identity, they are regulated both by common means as well as mechanisms unique to ROCK1 or ROCK2.

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Expression of stress fibers in bullfrog mesothelial cells in response to tension

Cited by 14 publications

References 36 publications

Mechanical stress induces profound remodelling of keratin filaments and cell junctions inepidermolysis bullosa simplexkeratinocytes

Mechanical stress induces profound remodelling of keratin filaments and cell junctions inepidermolysis bullosa simplexkeratinocytes

Distribution of Cytoskeletal Components in Endothelial Cells in the Guinea Pig Renal Artery

Rho-associated coiled-coil containing kinases (ROCK)

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