Functional impact of cholesterol sequestration on actin cytoskeleton in normal and transformed fibroblasts

2013 ◽  
Vol 37 (6) ◽  
pp. 617-623 ◽  
Author(s):  
Vladislav I. Chubinskiy-Nadezhdin ◽  
Tatiana N. Efremova ◽  
Sofia Y. Khaitlina ◽  
Elena A. Morachevskaya
Keyword(s):  
Actin Cytoskeleton ◽  
Functional Impact ◽  
Transformed Fibroblasts

Regulation of actin organisation by TGF-beta in H-ras-transformed fibroblasts

1999 ◽  
Vol 112 (8) ◽  
pp. 1169-1179 ◽  
Author(s):  
A. Moustakas ◽  
C. Stournaras
Keyword(s):  
Growth Factor ◽  
Actin Cytoskeleton ◽  
Transforming Growth Factor Beta ◽  
Transforming Growth Factor ◽  
Focal Adhesions ◽  
Small Gtpase ◽  
Morphological Alteration ◽  
Direct Role ◽  
Transformed Fibroblasts ◽  
Growth Factor Beta

The actin cytoskeleton undergoes architectural changes during the processes of cell transformation and tumourigenesis. Transforming growth factors beta arrest cell cycle progression, regulate differentiation and modulate the onset of oncogenesis and tumourigenesis. Here, we investigated the direct role of transforming growth factor beta-1 in altering the transformed phenotype and regulating the actin organisation of oncogenic fibroblasts that constitutively or inducibly express the H-ras oncogene. Following transforming growth factor beta-1 treatment, these transformed fibroblasts undergo a dramatic morphological alteration that includes a discrete reorganisation of their actin cytoskeleton and focal adhesions. Quantitative biochemical analysis demonstrated that transforming growth factor beta-1 potently induced polymerisation of globular to filamentous actin, thus corroborating the morphological analysis. The effect of transforming growth factor beta-1 on the cytoskeleton correlates with the ability of this cytokine to suppress anchorage-independent growth of the transformed fibroblasts. Furthermore, transforming growth factor beta-1 upregulates considerably the levels of the RhoB small GTPase and less the RhoA levels. Finally, The beta GTPase inhibitor, C3 exotransferase, blocks the ability of TGF-beta1 to induce cytoskeletal reorganisation. These findings indicate that transforming growth factor beta can regulate cell morphology and growth in a concerted manner possibly via mechanisms that control the actin cytoskeleton.

Simvastatin induced actin cytoskeleton disassembly in normal and transformed fibroblasts without affecting lipid raft integrity

2017 ◽  
Vol 41 (9) ◽  
pp. 1020-1029 ◽  
Author(s):  
Vladislav I. Chubinskiy-Nadezhdin ◽  
Yuri A. Negulyaev ◽  
Elena A. Morachevskaya
Keyword(s):  
Actin Cytoskeleton ◽  
Lipid Raft ◽  
Transformed Fibroblasts

A role for the actin cytoskeleton in the hormonal and growth-factor-mediated activation of protein kinase B

2001 ◽  
Vol 353 (3) ◽  
pp. 735
Author(s):  
K. PEYROLLIER ◽  
E. HAJDUCH ◽  
A. GRAY ◽  
G. J. LITHERLAND ◽  
A. R. PRESCOTT ◽  
...  
Keyword(s):  
Growth Factor ◽  
Protein Kinase ◽  
Actin Cytoskeleton ◽  
Protein Kinase B

Spatial control of actin-based motility through plasmalemmal PtdIns(4,5)P2-rich raft assemblies.

2005 ◽  
Vol 72 ◽  
pp. 119-127 ◽  
Author(s):  
Tamara Golub ◽  
Caroni Pico
Keyword(s):  
Protein Kinase ◽  
Cell Surface ◽  
Actin Cytoskeleton ◽  
Lipid Rafts ◽  
Patch Clustering ◽  
Pkc Protein Kinase C ◽  
Membrane Bound ◽  
And Function ◽  
Cytoskeleton Dynamics ◽  
Syndrome Protein

The interactions of cells with their environment involve regulated actin-based motility at defined positions along the cell surface. Sphingolipid- and cholesterol-dependent microdomains (rafts) order proteins at biological membranes, and have been implicated in most signalling processes at the cell surface. Many membrane-bound components that regulate actin cytoskeleton dynamics and cell-surface motility associate with PtdIns(4,5)P2-rich lipid rafts. Although raft integrity is not required for substrate-directed cell spreading, or to initiate signalling for motility, it is a prerequisite for sustained and organized motility. Plasmalemmal rafts redistribute rapidly in response to signals, triggering motility. This process involves the removal of rafts from sites that are not interacting with the substrate, apparently through endocytosis, and a local accumulation at sites of integrin-mediated substrate interactions. PtdIns(4,5)P2-rich lipid rafts can assemble into patches in a process depending on PtdIns(4,5)P2, Cdc42 (cell-division control 42), N-WASP (neural Wiskott-Aldrich syndrome protein) and actin cytoskeleton dynamics. The raft patches are sites of signal-induced actin assembly, and their accumulation locally promotes sustained motility. The patches capture microtubules, which promote patch clustering through PKA (protein kinase A), to steer motility. Raft accumulation at the cell surface, and its coupling to motility are influenced greatly by the expression of intrinsic raft-associated components that associate with the cytosolic leaflet of lipid rafts. Among them, GAP43 (growth-associated protein 43)-like proteins interact with PtdIns(4,5)P2 in a Ca2+/calmodulin and PKC (protein kinase C)-regulated manner, and function as intrinsic determinants of motility and anatomical plasticity. Plasmalemmal PtdIns(4,5)P2-rich raft assemblies thus provide powerful organizational principles for tight spatial and temporal control of signalling in motility.

Clathrin Hub Expression Dissociates the Actin-Binding Protein Hip1R from Coated Pits and Disrupts Their Alignment with the Actin Cytoskeleton

Traffic ◽  
2001 ◽  
Vol 2 (11) ◽  
pp. 851-858 ◽  
Author(s):  
Elizabeth M. Bennett ◽  
Chih-Ying Chen ◽  
Asa E. Y. Engqvist-Goldstein ◽  
David G. Drubin ◽  
Frances M. Brodsky
Keyword(s):  
Actin Cytoskeleton ◽  
Binding Protein ◽  
Actin Binding ◽  
Coated Pits ◽  
Actin Binding Protein

Sleep Functional Impact Scale

2011 ◽  
Author(s):  
Christopher Bell ◽  
Lori D. McLeod ◽  
Lauren M. Nelson ◽  
Sheri E. Fehnel ◽  
Laurie J. Zografos ◽  
...  
Keyword(s):  
Functional Impact ◽  
Impact Scale

Recombinant expression, purification and functional impact of CTGF/CCN2 and NOV/CCN3 on liver fibrogenesis

2011 ◽  
Vol 49 (01) ◽  
Author(s):  
W Bohr ◽  
S Lux ◽  
E Borkham-Kamphorst ◽  
E Van de Leur ◽  
M Kupper ◽  
...  
Keyword(s):  
Recombinant Expression ◽  
Functional Impact ◽  
Liver Fibrogenesis

Functional impact of FKBP51 on cellular pathways

2011 ◽  
Vol 44 (06) ◽  
Author(s):  
NC Gassen ◽  
Y Han ◽  
G Wochnik ◽  
F Holsboer ◽  
T Rein
Keyword(s):  
Functional Impact ◽  
Cellular Pathways
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