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J. Biol. Chem., Vol. 276, Issue 51, 48398-48403, December 21, 2001
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From the The actin-bound ADP was separated from
cytoplasmic nucleotides by treatment of intact arterial smooth muscle
with 50% ethanol. In 32P-labeled smooth muscle the
actin-bound ADP and phosphate readily exchanged with the cytoplasmic
[
Exchange of the Actin-bound Nucleotide in Intact Arterial Smooth
Muscle*
§,
Department of Biochemistry and Molecular
Biology, and
Department of Physiology and Biophysics, University
of Illinois College of Medicine, Chicago, Illinois 60612, the
¶ Section of Cardiology, Rush Medical College, Department of
Medicine, Chicago, Illinois 60612
,
-32P]ATP; the specific radioactivity of
actin-bound ADP was equal to that of the
-phosphate of cytoplasmic
ATP and the specific radioactivity of actin-bound phosphate was equal
to that of the
-phosphate of cytoplasmic ATP. In contrast, the
exchange of the actin-bound ADP in skeletal muscle was very slow. The
presence of cytoplasmic ATP was required for the exchange of the
actin-bound ADP and phosphate; if ATP synthesis was inhibited the
exchange was also inhibited. The extent of exchange was reduced in
muscles contracted by histamine or K+, as compared with
resting muscles. The exchange was also shown in other mammalian smooth
muscles, uterus, urinary bladder, and stomach. The data indicate a
dynamic state of actin in smooth muscle. The data also suggest that
polymerization-depolymerization of actin is part of the
contraction-relaxation cycle of smooth muscle.
*
This work was supported by the Edgar Folk Jr. Foundation for
Senior Physiologists.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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