h2-Calponin is regulated by mechanical tension and modifies the function of actin cytoskeleton
MM Hossain, JF Crish, RL Eckert, JJC Lin… - Journal of Biological …, 2005 - ASBMB
Calponin is an extensively studied actin-binding protein, but its function is not well
understood. Among three isoforms of calponin, h2-calponin is found in both smooth muscle …
understood. Among three isoforms of calponin, h2-calponin is found in both smooth muscle …
Developmentally regulated expression of calponin isoforms and the effect of h2-calponin on cell proliferation
MM Hossain, DY Hwang, QQ Huang… - American Journal of …, 2003 - journals.physiology.org
h2-Calponin is found in both smooth muscle and nonmuscle cells, and its function remains
to be established. Western blots with specific monoclonal antibodies detected significant …
to be established. Western blots with specific monoclonal antibodies detected significant …
[HTML][HTML] Diminished expression of h2-calponin in prostate cancer cells promotes cell proliferation, migration and the dependence of cell adhesion on substrate …
MM Hossain, X Wang, RC Bergan, JP Jin - FEBS open bio, 2014 - Elsevier
Calponin is an actin filament-associated protein and its h2 isoform inhibits cell motility. Here
we report significant expression of h2-calponin in prostate epithelial cells, which is …
we report significant expression of h2-calponin in prostate epithelial cells, which is …
The single CH domain of calponin is neither sufficient nor necessary for F-actin binding
M Gimona, R Mital - Journal of cell science, 1998 - journals.biologists.com
Calponins have been implicated in the regulation of actomyosin interactions in smooth
muscle cells, cytoskeletal organisation in nonmuscle cells, and the control of neurite …
muscle cells, cytoskeletal organisation in nonmuscle cells, and the control of neurite …
Expression and purification of the h1 and h2 isoforms of calponin
JP Jin, D Wu, J Gao, R Nigam, S Kwong - Protein expression and …, 2003 - Elsevier
Three homologous calponin isoforms, named h1, h2, and acidic calponins, have been found
in birds and mammals. Based primarily on studies of chicken gizzard smooth muscle (h1) …
in birds and mammals. Based primarily on studies of chicken gizzard smooth muscle (h1) …
Calponin in non-muscle cells
KC Wu, JP Jin - Cell biochemistry and biophysics, 2008 - Springer
Calponin is an actin filament-associated regulatory protein expressed in smooth muscle and
non-muscle cells. Calponin is an inhibitor of the actin-activated myosin ATPase. Three …
non-muscle cells. Calponin is an inhibitor of the actin-activated myosin ATPase. Three …
[HTML][HTML] Structural comparisons of calponin homology domains: implications for actin binding
S Bañuelos, M Saraste, KD Carugo - Structure, 1998 - cell.com
Background: The actin-binding site of several cytoskeletal proteins is comprised of two
calponin homology (CH) domains in a tandem arrangement. As a single copy, the CH …
calponin homology (CH) domains in a tandem arrangement. As a single copy, the CH …
The presence of h2-calponin in human keratinocyte
Y Fukui, H Masuda, M Takagi, K Takahashi… - Journal of …, 1997 - Elsevier
Calponin (h1 isoform) was characterized as a smooth muscle specific, actin-, tropomyosin-,
calmodulin-binding protein and described as a factor which inhibits contraction. H2 …
calmodulin-binding protein and described as a factor which inhibits contraction. H2 …
Physical characterization of calponin: a circular dichroism, analytical ultracentrifuge, and electron microscopy study
WF Stafford, K Mabuchi, K Takahashi, T Tao - Journal of Biological …, 1995 - ASBMB
Calponin is a thin filament-associated smooth muscle protein that has been suggested to
play a role in the regulation of smooth muscle contraction. We have used circular dichroism …
play a role in the regulation of smooth muscle contraction. We have used circular dichroism …
[PDF][PDF] Calponin interaction with α-actinin-actin: evidence for a structural role for calponin
B Leinweber, JX Tang, WF Stafford, JM Chalovich - Biophysical journal, 1999 - cell.com
The purpose of this study was to address the paradox of calponin localization with α-actinin
and filamin, two proteins with tandem calponin homology (CH) domains, by determining the …
and filamin, two proteins with tandem calponin homology (CH) domains, by determining the …