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J Virol, August 1998, p. 6574-6580, Vol. 72, No. 8
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Apoptosis Induction by the Binding of the Carboxyl
Terminus of Human Immunodeficiency Virus Type 1 gp160 to
Calmodulin
Hiroki
Ishikawa,1
Masafumi
Sasaki,2
Satoshi
Noda,1 and
Yasuhiro
Koga1,*
Department of Infectious Diseases, Tokai
University School of Medicine, Isehara, Kanagawa
259-1193,1 and
Department of Virology,
Medical Institute of Bioregulation, Kyushu University, Fukuoka
812-8582,2 Japan
Received 18 November 1997/Accepted 25 April 1998
The role of calmodulin (CaM) in apoptosis induced by gp160 of human
immunodeficiency virus type 1 was investigated with cells undergoing
single-cell killing. These cells were found to express, under the
control of an inducible promoter, wild-type gp160 or mutant gp160
devoid of various lengths of the carboxyl terminus. Immunoprecipitation
accompanied by immunoblotting revealed binding of CaM to wild-type
gp160 but not to mutant gp160 bearing a carboxyl terminus with a
deletion spanning more than five amino acid residues. A significant
coenzyme activity was detected in the CaM bound to gp160 even in the
presence of a Ca2+ chelater, EGTA. The cells forming this
gp160-CaM complex exhibited an elevated intracellular Ca2+
level followed by DNA fragmentation, which is a hallmark of apoptosis, and finally cell killing, while the cells not forming this complex did
not show any significant elevation in Ca2+ level or DNA
fragmentation. These results thus indicated that CaM plays a key role
in gp160-induced apoptosis.
*
Corresponding author. Mailing address: Department of
Infectious Diseases, Tokai University School of Medicine, Isehara,
Kanagawa 259-1193, Japan. Phone: 463-93-1121, ext. 2591. Fax:
463-94-2976.
J Virol, August 1998, p. 6574-6580, Vol. 72, No. 8
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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