CALDESMON CONTENT OF MAMMALIAN SMOOTH MUSCLES

被引:37
作者
HAEBERLE, JR [1 ]
HATHAWAY, DR [1 ]
SMITH, CL [1 ]
机构
[1] INDIANA UNIV, SCH MED, DEPT MED, KRANNERT INST CARDIOL, INDIANAPOLIS, IN 46202 USA
关键词
D O I
10.1007/BF01738431
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
In the present study we have used a quantitative immunoblotting method to measure the caldesmon content of a variety of smooth muscles with distinctly different contractile phenotypes. Two tonic vascular smooth muscles and several phasic smooth muscles were examined. The caldesmon, actin and myosin contents of each muscle type were measured. Smooth muscle from large arteries (i.e. bovine aorta and porcine carotid artery) had the lowest caldesmon content and phasic muscles (e.g. rat uterus and guinea pig taenia coli) had the highest. The molar ratio of monomeric caldesmon to monomeric actin was 1:205 for the aorta and carotid artery versus 1:22-28 for the taenia coli and uterus. The molar ratio of caldesmon to monomeric myosin heavy chain was 1:9 for the aorta and carotid versus 1:2 for the uterus and taenia coli. The caldesmon contents of canine trachealis and rabbit ileum were intermediate between these extremes. Evidence was found for the presence of both tissue- and species-specific caldesmon isoforms. The relatively high caldesmon content in rat uterus and guinea pig taenia coli suggests the possibility that the contractile phenotype associated with phasic smooth muscles may be dependent on the presence of caldesmon.
引用
收藏
页码:81 / 89
页数:9
相关论文
共 26 条
[1]  
ADAM LP, 1989, J BIOL CHEM, V264, P7698
[2]  
BRYAN J, 1989, J BIOL CHEM, V264, P13873
[3]   SALT DEPENDENT DIMERIZATION OF CALDESMON [J].
CROSS, RA ;
CROSS, KE ;
SMALL, JV .
FEBS LETTERS, 1987, 219 (02) :306-310
[4]   THE INFLUENCE OF CALDESMON ON ATPASE ACTIVITY OF THE SKELETAL-MUSCLE ACTOMYOSIN AND BUNDLING OF ACTIN-FILAMENTS [J].
DABROWSKA, R ;
GOCH, A ;
GALAZKIEWICZ, B ;
OSINSKA, H .
BIOCHIMICA ET BIOPHYSICA ACTA, 1985, 842 (01) :70-75
[5]   CALDESMON IS AN ELONGATED, FLEXIBLE MOLECULE LOCALIZED IN THE ACTOMYOSIN DOMAINS OF SMOOTH-MUSCLE [J].
FURST, DO ;
CROSS, RA ;
DEMEY, J ;
SMALL, JV .
EMBO JOURNAL, 1986, 5 (02) :251-257
[6]  
GRACEFFA P, 1988, J BIOL CHEM, V263, P14196
[7]   REGULATION OF ISOMETRIC FORCE AND ISOTONIC SHORTENING VELOCITY BY PHOSPHORYLATION OF THE 20,000 DALTON MYOSIN LIGHT CHAIN OF RAT UTERINE SMOOTH-MUSCLE [J].
HAEBERLE, JR ;
HOTT, JW ;
HATHAWAY, DR .
PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY, 1985, 403 (02) :215-219
[8]   COMPLEXES BETWEEN 15 KDA CALDESMON FRAGMENT AND ACTIN INVESTIGATED BY IMMUNOELECTRON MICROSCOPY [J].
HARRICANE, MC ;
CAVADORE, C ;
AUDEMARD, E ;
MORNET, D .
FEBS LETTERS, 1990, 269 (01) :185-188
[9]  
HATHAWAY DR, 1985, AM J PHYSIOL, V249, pC345
[10]  
HEMRIC ME, 1988, J BIOL CHEM, V263, P1878