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      cDNA Cloning and Expression Pattern of Homolog of Alpha Subunit of Platelet-Activating Factor Acetylhydrolase Ib from the Chinese Oak Silkworm, Antheraea pernyi

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          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 (ORE) 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.

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          The neighbour-joining method: a new method for constructing phylogenetic trees

          N Saitou, M Nei, J Saitou … (1987)
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            Platelet-activating factor acetylhydrolases.

            Grant McIntyre, Louis Zimmerman, Stephen Prescott … (1997)
            Article 0 comments Cited 39 times – based on 0 reviews     Review now
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              Plasma platelet-activating factor acetylhydrolase is a secreted phospholipase A2 with a catalytic triad.

              Thaddeus J. Unger, William Gray, H L Trong … (1995)
              Platelet-activating factor (PAF) is a potent pro-inflammatory autacoid with diverse physiological and pathological actions. These actions are modulated by PAF acetylhydrolase, which hydrolyzes the sn-2 ester bond to yield the biologically inactive lyso-PAF. In contrast to most secreted phospholipase A2s, plasma PAF acetylhydrolase is calcium-dependent and contains a GXSXG motif that is characteristic of the neutral lipases and serine esterases. In this study we tested whether the serine in this motif is part of the active site of plasma PAF acetylhydrolase and, if so, what the other components of the active site are. Using site-directed mutagenesis, we demonstrated that Ser-273 (of the GXSXG motif), Asp-296, and His-351 are essential for catalysis. These residues were conserved in PAF acetylhydrolase sequences isolated from bovine, dog, mouse, and chicken. The linear orientation and spacing of these catalytic residues are consistent with the alpha/beta hydrolase conformation of other lipases and esterases. In support of this model, analysis of systematic truncations of PAF acetylhydrolase revealed that deletions beyond 54 amino acids from the NH2 terminus and 21 from the COOH terminus resulted in a loss of enzyme activity. These observations demonstrate that although plasma PAF acetylhydrolase is a phospholipase A2 it has structural properties characteristic of the neutral lipases and esterases.
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                Author and article information

                Journal
                Journal ID (nlm-ta): J Insect Sci
                Journal ID (iso-abbrev): J. Insect Sci
                Journal ID (publisher-id): insc
                Title: Journal of Insect Science
                Publisher: University of Wisconsin Library
                ISSN (Electronic): 1536-2442
                Publication date Collection: 2011
                Publication date (Electronic): 8 November 2011
                Volume: 11
                Electronic Location Identifier: 148
                Affiliations
                [1]Department of Sericulture, School of Life Sciences, Shenyang Agricultural University, Shenyang 110866, China
                Author notes
                [*] [ * ]Corresponding authors

                Editor: Todd Shelly was Editor of this paper.

                Article
                DOI: 10.1673/031.011.14801
                PMC ID: 3281379
                PubMed ID: 22224584
                SO-VID: e465b802-09b2-4959-bf5b-032331f439ab
                Copyright © © 2011
                License:

                This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 4 September 2010
                Date accepted : 30 November 2010
                Page count
                Pages: 8
                Categories
                Subject: Article

                ScienceOpen disciplines: Entomology
                Data availability:
                ScienceOpen disciplines: Entomology

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