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J. Biol. Chem., Vol. 281, Issue 32, 22471-22484, August 11, 2006

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Suppression and Overexpression of Adenosylhomocysteine Hydrolase-like Protein 1 (AHCYL1) Influences Zebrafish Embryo Development

A POSSIBLE ROLE FOR AHCYL1 IN INOSITOL PHOSPHOLIPID SIGNALING^*

Benjamine J. Cooper, Brian Key, Adrian Carter, Nicola Z. Angel, Derek N. J. Hart^¶, and Masato Kato¹

From the Dendritic Cell Program, Mater Medical Research Institute, Brisbane, Queensland 4101, Australia and Discipline of Anatomy and Developmental Biology, School of Biomedical Sciences, University of Queensland, Brisbane, Queensland 4172, Australia, and the ^¶School of Medicine, University of Queensland, Herston, Queensland 4006, Australia

Adenosylhomocysteine hydrolase-like protein 1 (AHCYL1) is a novel intracellular protein with 50% protein identity to adenosylhomocysteine hydrolase (AHCY), an important enzyme for metabolizing S-adenosyl-L-homocysteine, the by-product of S-adenosyl-L-homomethionine-dependent methylation. AHCYL1 binds to the inositol 1,4,5-trisphosphate receptor, suggesting that AHCYL1 is involved in intracellular calcium release. We identified two zebrafish AHCYL1 orthologs (zAHCYL1A and -B) by bioinformatics and reverse transcription-PCR. Unlike the ubiquitously present AHCY genes, AHCYL1 genes were only detected in segmented animals, and AHCYL1 proteins were highly conserved among species. Phylogenic analysis suggested that the AHCYL1 gene diverged early from AHCY and evolved independently. Quantitative reverse transcription-PCR showed that zAHCYL1A and -B mRNA expression was regulated differently from the other AHCY-like protein zAHCYL2 and zAHCY during zebrafish embryogenesis. Injection of morpholino antisense oligonucleotides against zAHCYL1A and -B into zebrafish embryos inhibited zAHCYL1A and -B mRNA translation specifically and induced ventralized morphologies. Conversely, human and zebrafish AHCYL1A mRNA injection into zebrafish embryos induced dorsalized morphologies that were similar to those obtained by depleting intracellular calcium with thapsigargin. Human AHCY mRNA injection showed little effect on the embryos. These data suggest that AHCYL1 has a different function from AHCY and plays an important role in embryogenesis by modulating inositol 1,4,5-trisphosphate receptor function for the intracellular calcium release.

Received for publication, March 17, 2006 , and in revised form, June 2, 2006.

Note Added in Proof—Devogelaere et al. (28) showed recently that AHCYL1 binds directly to IP₃R and inhibits IP₃ binding and IP₃-induced Ca²⁺ release.

^* This work was supported by research grants from Pfizer and Mater Medical Research Institute. 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) AY611473 [GenBank] (zAHCYL1A), AY611474 [GenBank] (zAHCYL1B), BK005364 [GenBank] (fugu fish AHCYL1), BK005417 [GenBank] (hAHCYL1B), and BK005418 [GenBank] (hAHCYL1C).

¹ To whom correspondence should be addressed: Mater Medical ResearchInstitute, Aubigny Pl., South Brisbane, Queensland 4101, Australia. Tel.: 61-7-3840-2555; Fax: 61-7-3840-2550; E-mail: mkato{at}mmri.mater.org.au.

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