cDNA cloning and expression pattern of homolog of alpha subunit of platelet-activating factor acetylhydrolase Ib from the Chinese oak silkworm, Antheraea pernyi

Yu-Ping Li, Yan-Qun Liu*, Huan Wang, Run-Xi Xia, Sheng-Lin Shi, Xian Liu, Shi-Fu Wang*, Li Qin

Department of Sericulture, School of Life Sciences, Shenyang Agricultural University, Shenyang 110866, China

Abstract

Platelet-activating factor acetylhydrolase (PAF-AH) is an enzyme that catalyzes the hydrolysis of platelet-activating factor (PAF). A homolog of alpha subunit of PAF-AH(Ib) from Antheraea pernyi (Guérin-Méneville) (Lepidoptera: Saturniidae) (ApPAFAHIbα) was isolated and characterized. The obtained cDNA sequence was 1843 base pairs (bp) long with an open reading frame (ORF) of 678 bp encoding 225 amino acids. The predicted amino acid sequence shared several conserved features of PAF-AHs of other organisms, and revealed 88, 60, and 46% identity with the homologues of Bombyx mori, Drosophila melanogaster, and Homo sapiens, respectively. Phylogenetic analysis indicated that lepidopteran PAFAHIbαs including ApPAFAHIbα might be a new member of the PAF-AHs family of insects. Reverse transcriptase polymerase chain reaction (RT-PCR) analysis showed that the ApPAFAHIbα gene was transcribed at four developmental stages and expressed in all tissues tested.

Correspondence: liuyqlyp@yahoo.com.cn, syauwsf163@163.com, *Corresponding authors

Editor: Todd Shelly was Editor of this paper.

Received: 4 September 2010 | Accepted: 30 November 2010 | Published: 8 November 2011

ISSN: 1536-2442 | Volume 11, Number 148

Li Y-P, Liu Y-Q, Wang H, Xia R-X, Shi S-L, Liu X, Wang S-F, Qin L. 2011. cDNA cloning and expression pattern of homolog of alpha subunit of platelet-activating factor acetylhydrolase Ib from the Chinese oak silkworm, Antheraea pernyi. Journal of Insect Science 11:148 available online: insectscience.org/11.148


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