TY - JOUR
T1 - Expression of human cardiac actin in mouse L cells
T2 - A sarcomeric actin associates with a nonmuscle cytoskeleton
AU - Gunning, Peter
AU - Ponte, Phyllis
AU - Kedes, Larry
AU - Hickey, Robert J.
AU - Skoultchi, Arthur I.
N1 - Funding Information:
The authors thank Sheldon Penman for a seminal suggesticn and Chloe Bulinski for critical comments. Peter Evans in P&J Afto and Paul Zel in the Bronx provided expert technical assistance. Dcds Hosmer ccntrfbuted valuable editorial assistance. This work was supported in part by grants from the National Institutes of Health (GM17995 and HD17031). the Muscular Dystrophy Assocfatiin, and the Veterans Adminffatfon to L. K., and by a grant from the National lnstiiutes of Health (CA16368) to A. I. S. P. P. was a recipient of a postdoctoral fellowship from the Am&can Cancer Society and is currentfy a very special postdoctoral fellow of the National lnstiies of Health. A. I. S. is a recipient of an Irma T. Hkschl Career Scientist Award.
PY - 1984/3
Y1 - 1984/3
N2 - A cloned human cardiac actin gene, introduced into mouse Ltk- cells, is expressed in several thymidine kinase (tk)-positive cotransfectants. The clones not only produce authentic polyadenylated human cardiac actin mRNA but also synthesize human cardiac actin protein. The cardiac actin protein, normally found only in myofibrils, is stably accumulated at a high level, about one-third that of the endogenous mouse β-actin. Furthermore, this sarcomeric protein partitions between the Triton X-100 insoluble and soluble phases to the same extent as the endogenous β-actin. This suggests that a sarcomeric actin can participate in the formation of Triton X-100-insoluble cytoskeletal structures.
AB - A cloned human cardiac actin gene, introduced into mouse Ltk- cells, is expressed in several thymidine kinase (tk)-positive cotransfectants. The clones not only produce authentic polyadenylated human cardiac actin mRNA but also synthesize human cardiac actin protein. The cardiac actin protein, normally found only in myofibrils, is stably accumulated at a high level, about one-third that of the endogenous mouse β-actin. Furthermore, this sarcomeric protein partitions between the Triton X-100 insoluble and soluble phases to the same extent as the endogenous β-actin. This suggests that a sarcomeric actin can participate in the formation of Triton X-100-insoluble cytoskeletal structures.
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U2 - 10.1016/0092-8674(84)90351-9
DO - 10.1016/0092-8674(84)90351-9
M3 - Article
C2 - 6538118
AN - SCOPUS:0021282350
VL - 36
SP - 709
EP - 715
JO - Cell
JF - Cell
SN - 0092-8674
IS - 3
ER -