TISSUE-SPECIFICITY OF ARTHROPOD TROPOMYOSIN

被引:7
作者
MIYAZAKI, JI
YAHATA, K
MAKIOKA, T
HIRABAYASHI, T
机构
[1] Institute of Biological Sciences, University of Tsukuba, Ibaraki
来源
JOURNAL OF EXPERIMENTAL ZOOLOGY | 1993年 / 267卷 / 05期
关键词
D O I
10.1002/jez.1402670505
中图分类号
Q95 [动物学];
学科分类号
071002 ;
摘要
In order to elucidate whether tropomyosin isoforms have different tissue-specific functions, we examined tissue specificity of tropomyosin by two-dimensional gel electrophoresis and immunoreplica tests using three arthropod species. These arthropods showed molecular heterogeneity and tissue specificity of tropomyosin in muscle and nonmuscle tissues. The beetle (Insecta) and centipede (Chilopoda) had three different isoforms. The scorpion (Arachnida) had six isoforms, two of which were nonmuscle-specific. In addition to these isoforms, all the species contained nonmuscle-specific isoforms of high electrophoretic mobilities and another isoform with a high electrophoretic mobility was found in the beetle heart and intestine. We summarized the results including the data from our previous studies on the horseshoe crab (Merostomata) and five crustaceans (Crustacea) and found that most isoforms were not shared by every tissue but detected in some particular tissues. In that sense, they were tissue specific, but each of them was not restricted to a single tissue. However, crustacean cardiac isoforms were contained exclusively in the hearts, and some of the nonmuscle isoforms were not found in other tissues; thus they were tissue specific in the strict sense. Considering our results and those on vertebrate tropomyosin together, we suggest that the existence of different isoforms alone does not imply straightforwardly different functions among the isoforms and that only strictly tissue-specific isoforms can be assumed to have functions peculiar to their tissues. (C) 1993 Wiley-Liss, Inc.
引用
收藏
页码:501 / 509
页数:9
相关论文
共 32 条
[1]  
Basi G.S., Boardman M., Storti R.V., Alternative splicing of a Drosophila tropomyosin gene generates muscle tropomyosin isoforms with different carboxy‐terminal ends, Mol. Cell. Biol., 4, pp. 2828-2836, (1984)
[2]  
Bronson D.D., Schachat F.H., Heterogeneity of contractile proteins, J. Biol. Chem., 257, pp. 3937-3944, (1982)
[3]  
Broschat K.O., Burgess D.R., Low Mr tropomyosin isoforms from chicken brain and intestinal epithelium have distinct actin‐binding properties, J. Biol. Chem., 261, pp. 13350-13359, (1986)
[4]  
Costello W.J., Govind C.K., Contractile proteins of fast and slow fibers during differentiation of lobster claw muscle, Dev. Biol., 104, pp. 434-440, (1984)
[5]  
Franke W.W., Heid H.W., Grund C., Winter S., Freudenstein C., Schmid E., Jarasch E.-D., Keenan T.W., Antibodies to the major insoluble milk fat globule membrane‐associated protein: Specific location in apical regions of lactating epithelial cells, J. Cell Biol., 89, pp. 485-494, (1981)
[6]  
Giometti C.S., Anderson N.L., Tropomyosin heterogeneity in human cells, J. Biol. Chem., 259, pp. 14113-14120, (1984)
[7]  
Hanke P.D., Storti R.V., The Drosophila melanogaster tropomyosin II gene produces multiple proteins by use of alternative tissue‐specific promoters and alternative splicing, Mol. Cell. Biol., 8, pp. 3591-3602, (1988)
[8]  
Heaslip R.J., Chacko S., Effects of Ca<sup>2+</sup> and Mg<sup>2+</sup> on the actomyosin adenosine‐5′‐triphosphatase of stably phos‐phorylated gizzard myosin, Biochemistry, 24, pp. 2731-2736, (1985)
[9]  
Hirabayashi T., Tamura R., Mitsui I., Watanabe Y., Investigation of actin in Tetrahymena cells. A comparison with skeletal muscle actin by a devised two‐dimensional gel electrophoresis method, J. Biochem., 93, pp. 461-468, (1983)
[10]  
Hirai S., Hirabayashi T., Developmental change of protein constituents in chicken gizzards, Dev. Biol., 97, pp. 483-493, (1983)