J. Biochem, 1982, Vol. 92, No. 5 1457-1468
© 1982 Japanese Biochemical Society
research-article |
Molecular Properties and Functions In Vitro of Chicken Smooth-Muscle
-Actinin in Comparison with Those of Striated-Muscle
-Actinins1
Institute of Basic Medical Sciences, The University of Tsukuba Sakura-mura, Niihari-gun, Ibaraki 305
-Actinin purified from chicken gizzard smooth muscle was characterized in comparison with
-actinins from chicken striated muscles, or fast-skeletal muscle, slow-skeletal muscle, and cardiac muscle. The gizzard
-actinin molecule consisted of two apparently identical subunits with a molecular weight of 100,000 on SDS-polyacrylamide gel electrophoresis, as do striated-muscle
-actinins. Its isoelectric points in the presence of urea were similar to the striated-muscle counterparts. Despite these similarities, distinctive amino acid sequences between smooth-muscle
-actinin and striated-muscle
-actinins were revealed by peptide mapping using limited proteolysis in SDS. Gizzard
-actinin was immunologically distinguished from striated-muscle
-actinins.
Gizzard
-actinin formed bundles of gizzard F-actin as well as of skeletal-muscle F-actin, but could not form any cross-bridges between adjacent actin filaments under conditions where skeletal-muscle
-actinin could. Temperature-dependent competition between gizzard
-actinin and tropomyosin on binding to gizzard thin filaments was demonstrated by electron microscopic observations. Gizzard
-actinin promoted Mg2+-ATPase activity of reconstituted skeletal actomyosin, gizzard acto-skeletal myosin, and gizzard actomyosin. This promoting effect was depressed by the addition of gizzard tropomyosin. These findings imply that, despite structural differences between gizzard and striated-muscle
-actinin molecules, they function similarly in vitro, and that gizzard
-actinin can interact not only with smooth-muscle actin (
- and ß-actin) but also with skeletal-muscle actin (
-actin).
1This study was supported in part by Grants-in-Aid from the Ministry of Education, Science and Culture of Japan.
![]()
CiteULike
Connotea
Del.icio.us What's this?
This article has been cited by other articles:
![]() |
T. Abe, K. Takano, A. Suzuki, Y. Shimada, M. Inagaki, N. Sato, T. Obinata, and T. Endo Myocyte differentiation generates nuclear invaginations traversed by myofibrils associating with sarcomeric protein mRNAs J. Cell Sci., December 15, 2004; 117(26): 6523 - 6534. [Abstract] [Full Text] [PDF] |
||||
![]() |
P. Pomies, T. Macalma, and M. C. Beckerle Purification and Characterization of an alpha -Actinin-binding PDZ-LIM Protein That Is Up-regulated during Muscle Differentiation J. Biol. Chem., October 8, 1999; 274(41): 29242 - 29250. [Abstract] [Full Text] [PDF] |
||||
![]() |
T. Ohtsuka, H. Nakanishi, W. Ikeda, A. Satoh, Y. Momose, H. Nishioka, and Y. Takai Nexilin: A Novel Actin Filament-binding Protein Localized at Cell-Matrix Adherens Junction J. Cell Biol., November 30, 1998; 143(5): 1227 - 1238. [Abstract] [Full Text] [PDF] |
||||
![]() |
H. Nakanishi, H. Obaishi, A. Satoh, M. Wada, K. Mandai, K. Satoh, H. Nishioka, Y. Matsuura, A. Mizoguchi, and Y. Takai Neurabin: A Novel Neural Tissue-specific Actin Filament-binding Protein Involved in Neurite Formation J. Cell Biol., November 17, 1997; 139(4): 951 - 961. [Abstract] [Full Text] [PDF] |
||||
![]() |
I. N. Rybakova and J. M. Ervasti Dystrophin-Glycoprotein Complex Is Monomeric and Stabilizes Actin Filaments in Vitro through a Lateral Association J. Biol. Chem., November 7, 1997; 272(45): 28771 - 28778. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. E. Hungerford, J. P. Hoeffler, C. W. Bowers, L. M. Dahm, R. Falchetto, J. Shabanowitz, D. F. Hunt, and C. D. Little Identification of a Novel Marker for Primordial Smooth Muscle and Its Differential Expression Pattern in Contractile vs Noncontractile Cells J. Cell Biol., May 19, 1997; 137(4): 925 - 937. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. Kato, T. Sasaki, T. Ohya, H. Nakanishi, H. Nishioka, M. Imamura, and Y. Takai Physical and Functional Interaction of Rabphilin-3A with alpha -Actinin J. Biol. Chem., December 13, 1996; 271(50): 31775 - 31778. [Abstract] [Full Text] [PDF] |
||||
![]() |
T. Endo, K. Matsumoto, T. Hama, Y. Ohtsuka, G. Katsura, and T. Obinata Distinct Troponin T Genes Are Expressed in Embryonic/Larval Tail Striated Muscle and Adult Body Wall Smooth Muscle of Ascidian J. Biol. Chem., November 1, 1996; 271(44): 27855 - 27862. [Abstract] [Full Text] [PDF] |
||||
![]() |
R. Parekh and J. Bag Inhibition of Myogenesis in Mouse C2 Cells by Double-stranded Phosphorothioate Oligodeoxynucleotides containing mef-1 Sequence J. Biol. Chem., July 19, 1996; 271(29): 17372 - 17376. [Abstract] [Full Text] [PDF] |
||||
![]() |
U. Gluck and A. Ben-Ze'ev Modulation of alpha-actinin levels affects cell motility and confers tumorigenicity on 3T3 cells J. Cell Sci., July 1, 1994; 107(7): 1773 - 1782. [Abstract] [PDF] |
||||
![]() |
M. W. Kelley, X. M. Xu, M. A. Wagner, M. E. Warchol, and J. T. Corwin The developing organ of Corti contains retinoic acid and forms supernumerary hair cells in response to exogenous retinoic acid in culture Development, December 1, 1993; 119(4): 1041 - 1053. [Abstract] [PDF] |
||||



