COEXPRESSION OF ALPHA-SARCOMERIC ACTIN, ALPHA-SMOOTH MUSCLE ACTIN AND DESMIN DURING MYOGENESIS IN RAT AND MOUSE EMBRYOS .1. SKELETAL-MUSCLE

被引:125
作者
BABAI, F
MUSEVIAGHDAM, J
SCHURCH, W
ROYAL, A
GABBIANI, G
机构
[1] INST CANC MONTREAL,MONTREAL,QUEBEC,CANADA
[2] UNIV GENEVA,DEPT PATHOL,CH-1211 GENEVA 4,SWITZERLAND
关键词
D O I
10.1111/j.1432-0436.1990.tb00546.x
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Expression of vimentin, desmin, α-sarcomeric and α-smooth muscle actins in embryonic tissues of rat and mice was examined using an immunohistochemical approach. The results showed a similarity in the expression of desmin and α-actin isoforms (α-sr and α-sm) in skeletal muscle cells during murine feto-embryonic development. In the two species, coexpression of α-sr and α-sm actins has been observed in cardiomyoblasts, myotomal myoblasts and myotubes. The intensity of α-sm actin expression decreased during the terminal steps of myogenesis and disappeared completely in mature cardiomyocytes and myofibres. Desmin was expressed in all prefusion myoblasts (type 1 and 2 myoblasts), myotubes, and in myofibres. The appearance of desmin in myoblasts of somites preceded by a few hours the expression of the α-actins (α-sr and α-sm). Our study on vimentin expression, limited to rat embryos, revealed that somite premyoblasts expressed only vimentin, type 1 myoblasts expressed vimentin and desmin, and type 2 myoblasts (rhabdomyoblasts) expressed desmin and α-actins (α-sr and α-sm). Our study demonstrates the resemblance between feto-embryonic myogenesis and myogenic neoplastic differentiation: desmin appears before the α-actins in embryonic myoblasts, and can be considered as a marker of an initial step in myogenic differentiation, α-sm actin, considered as a striated muscle cell feto-embryonic actin, is expressed transiently in skeletal myoblasts and cardiomyoblasts during development and reappears during neoplastic transformation of skeletal muscle. © 1990, International Society of Differentiation. All rights reserved.
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页码:132 / 142
页数:11
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