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J. Biol. Chem., Vol. 279, Issue 27, 28000-28008, July 2, 2004

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The Insect Hemolymph Protein HP19 Mediates the Nongenomic Effect of Ecdysteroids on Acid Phosphatase Activity^*

Abul Arif, Palaniappan Vasanthi, Immo Alex Hansen¶||, Klaus Scheller¶, and Aparna Dutta-Gupta**

From the Department of Animal Sciences, School of Life Sciences, University of Hyderabad, Hyderabad, 500 046, India, ^¶Department of Cell and Developmental Biology, Biocentre of the University, D-97074, Wuerzburg, Germany, and ^||Department of Entomology, University of California, Riverside California 92521

The activity of acid phosphatase (ACP) in insect fat bodies is stimulated by the steroid hormone 20-hydoxyecdysone (20E) in vivo. However, in fat bodies kept in culture, a factor from the hemolymph is required to enhance the ACP activity. We identified the factor as a protein with a molecular mass of 19 kDa (HP19) from the hemolymph of a lepidopteran insect, the rice moth, Corcyra cephalonica. Western analysis of hemolymph proteins with denaturing and non-denaturing PAGE using antibodies raised against HP19 suggest that this protein exists as a monomer. It is synthesized by the hind gut-associated lobular fat body of the larvae and is released into the hemolymph. The stimulatory effect of HP19 on the ACP activity is developmentally regulated and exhibits its maximal effect shortly before the onset of metamorphosis. We cloned the HP19 cDNA by immunoscreening a hind gut-associated lobular fat body cDNA expression library. Analysis of the amino acid sequence shows that HP19 belongs to the family of glutathione S-transferase (GST) like proteins. However, affinity-purified GST from Corcyra failed to show any mediation effect on 20E-stimulated ACP activity, and HP19 lacks GST enzymatic activity. Notably, HP19 mediates the hormone-stimulated ACP activity in intact fat body tissue and homogenates even in the presence of inhibitors of transcription and translation, suggesting a nongenomic mode of action. In addition, we show that HP19 inhibits the 20E-induced phosphorylation of the hexamerin receptor protein.

Received for publication, March 1, 2004 , and in revised form, April 23, 2004.

^* This work was supported by Council of Scientific and Industrial Research, Government of India Grant 37(1026)99/EMR-II and Department of Science and Tecnology, Government of India Grant P108/99 (to A. D.-G.) and Deutscher Akademischer Austausch Dienst (German Academic Exchange Service), Germany Grant 9835203 (to K. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AY369240.

Supported by a fellowship from UGC-India.

^** To whom correspondence should be addressed. Tel.: 91-40-23010-052; Fax: 91-40-23010-120; E-mail: apdgsl{at}uohyd.ernet.in.

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