| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 259, Issue 20, 12873-12880, 10, 1984
A Bretscher
A method for the rapid purification of caldesmon, an F-actin binding
protein of smooth muscle, has been developed. Caldesmon remains native
after heating at 90 degrees C, a property that provides the basis for the
purification in high yield of both caldesmon and tropomyosin, another
heat-stable protein of smooth muscle. Caldesmon purified by this procedure
is a highly asymmetric protein with a sedimentation coefficient of
approximately 2.7 S and a Stokes radius of about 91 A. The protein exists
as two polypeptide chains of Mr = 135,000 and 140,000, with each Mr
polypeptide being resolvable into several isoelectric species. Estimates
based on densitometry of stained gels suggest that caldesmon is more
abundant in smooth muscle than filamin or alpha-actinin. Purified caldesmon
bound to F-actin in the pH range 6- 8. Binding was unaffected by Ca2+ or
Mg2+ at up to millimolar levels. Binding was saturable, with a polypeptide
molar ratio of about one caldesmon to six actins at saturation. F-actin
binding was not inhibited by saturating levels of tropomyosin. Caldesmon
dramatically increased the viscosity of F-actin. Light microscopy and
electron microscopy of negatively stained material revealed that caldesmon
induced the formation of massive F-actin bundles which contained up to
hundreds of filaments. Electron microscopy of sectioned caldesmon-
saturated F-actin mixtures revealed large bundles which appeared to include
linear arrays of regularly spaced actin filaments cut transversely,
exhibiting a center to center spacing of 15 nm. Possible structural
implications based on the existence of these structures is presented.
Smooth muscle caldesmon. Rapid purification and F-actin cross-linking properties
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  K. Takiguchi and F. Matsumura Role of the Basic C-Terminal Half of Caldesmon in Its Regulation of F-Actin: Comparison between Caldesmon and Calponin J. Biochem., December 1, 2005; 138(6): 805 - 813. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Y. Yamakita, F. Oosawa, S. Yamashiro, and F. Matsumura Caldesmon Inhibits Arp2/3-mediated Actin Nucleation J. Biol. Chem., May 9, 2003; 278(20): 17937 - 17944. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Yamashiro, H. Chern, Y. Yamakita, and F. Matsumura Mutant Caldesmon Lacking cdc2 Phosphorylation Sites Delays M-Phase Entry and Inhibits Cytokinesis Mol. Biol. Cell, January 1, 2001; 12(1): 239 - 250. [Abstract] [Full Text]
|
|
|
|
|
|
D. B. Foster, L.-H. Shen, J. Kelly, P. Thibault, J. E. Van Eyk, and A. S. Mak Phosphorylation of Caldesmon by p21-activated Kinase. IMPLICATIONS FOR THE Ca2+ SENSITIVITY OF SMOOTH MUSCLE CONTRACTION J. Biol. Chem., January 21, 2000; 275(3): 1959 - 1965. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
G. D'Angelo, P. Graceffa, C.-L. A. Wang, J. Wrangle, and L. P. Adam Mammal-specific, ERK-dependent, Caldesmon Phosphorylation in Smooth Muscle. QUANTITATION USING NOVEL ANTI-PHOSPHOPEPTIDE ANTIBODIES J. Biol. Chem., October 15, 1999; 274(42): 30115 - 30121. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. Feng, M. Ito, Y. Kureishi, K. Ichikawa, M. Amano, N. Isaka, K. Okawa, A. Iwamatsu, K. Kaibuchi, D. J. Hartshorne, et al. Rho-associated Kinase of Chicken Gizzard Smooth Muscle J. Biol. Chem., February 5, 1999; 274(6): 3744 - 3752. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
R. Ishikawa, S. Yamashiro, K. Kohama, and F. Matsumura Regulation of Actin Binding and Actin Bundling Activities of Fascin by Caldesmon Coupled with Tropomyosin J. Biol. Chem., October 9, 1998; 273(41): 26991 - 26997. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. E. Van Eyk, D. K. Arrell, D. B. Foster, J. D. Strauss, T. Y. K. Heinonen, E. Furmaniak-Kazmierczak, G. P. Cote, and A. S. Mak Different Molecular Mechanisms for Rho Family GTPase-dependent, Ca2+-independent Contraction of Smooth Muscle J. Biol. Chem., September 4, 1998; 273(36): 23433 - 23439. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
E. A. Czurylo, N. Kulikova, and R. Dabrowska Does Calponin Interact with Caldesmon? J. Biol. Chem., December 19, 1997; 272(51): 32067 - 32070. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. B. Menice, J. Hulvershorn, L. P. Adam, C.-L. A. Wang, and K. G. Morgan Calponin and Mitogen-activated Protein Kinase Signaling in Differentiated Vascular Smooth Muscle J. Biol. Chem., October 3, 1997; 272(40): 25157 - 25161. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Zhuang, K. Mabuchi, and C.-L. A. Wang Heat Treatment Could Affect the Biochemical Properties of Caldesmon J. Biol. Chem., November 22, 1996; 271(47): 30242 - 30248. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
P. Graceffa and P. Graceffa Cross-linking and Fluorescence Study of the COOH- and NH(2)-terminal Domains of Intact Caldesmon Bound to Actin J. Biol. Chem., December 15, 1995; 270(50): 30187 - 30193. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Zhuang, E. Wang, and C.-L. A. Wang Identification of the Functionally Relevant Calmodulin Binding Site in Smooth Muscle Caldesmon J. Biol. Chem., August 25, 1995; 270(34): 19964 - 19968. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. M. Chalovich, Y.-d. Chen, R. Dudek, and H. Luo Kinetics of Binding of Caldesmon to Actin J. Biol. Chem., April 28, 1995; 270(17): 9911 - 9916. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
E. Katayama, G. Scott-Woo, and M. Ikebe Effect of Caldesmon on the Assembly of Smooth Muscle Myosin J. Biol. Chem., February 24, 1995; 270(8): 3919 - 3925. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Yamashiro, Y. Yamakita, K.-s. Yoshida, K. Takiguchi, and F. Matsumura Characterization of the COOH Terminus of Non-muscle Caldesmon Mutants Lacking Mitosis-specific Phosphorylation Sites J. Biol. Chem., February 24, 1995; 270(8): 4023 - 4030. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 L. P. Adam, M. T. Franklin, G. J. Raff, and D. R. Hathaway Activation of Mitogen-Activated Protein Kinase in Porcine Carotid Arteries Circ. Res., February 1, 1995; 76(2): 183 - 190. [Abstract] [Full Text]
|
|
|
|
 |
|
 J Tanaka, T Watanabe, N Nakamura, and K Sobue Morphological and biochemical analyses of contractile proteins (actin, myosin, caldesmon and tropomyosin) in normal and transformed cells J. Cell Sci., January 2, 1993; 104(2): 595 - 606. [Abstract] [PDF]
|
|
|
|
|
|
X. Luo, S. W. Crawley, P. A. Steimle, T. T. Egelhoff, and G. P. Cote Specific Phosphorylation of Threonine by the Dictyostelium Myosin II Heavy Chain Kinase Family J. Biol. Chem., May 18, 2001; 276(21): 17836 - 17843. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
