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Gender specific expression of myo ‐inositol‐3‐phosphate synthase in Drosophila melanogaster
Author(s) -
Batugedara Gayani D.,
Eldon Elizabeth D.,
Klig Lisa S.
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.564.1
Subject(s) - gene isoform , drosophila melanogaster , biology , alternative splicing , melanogaster , biochemistry , inositol , microbiology and biotechnology , gene , receptor
myo ‐Inositol, an essential metabolite, plays an important role in development, osmoregulation, and diseases such as Alzheimer's, autism, Down syndrome, bipolar disorder and spinal cord defects. myo ‐Inositol‐3‐phosphate synthase (MIPS) converts glucose‐6‐phosphate to myo ‐inositol‐3‐phosphate. In Drosophila melanogaster , MIPS has a computationally determined MW of 62kDa and is 59% identical (72% similar) to the human MIPS protein. Initial experiments revealed the molecular structure of the native MIPS protein in D. melanogaster to be a tetramer. MIPS RNA has been shown to be highly expressed in the fly head, hindgut, ovary and testis. Western blot analyses using crude lysates of male and female wild‐type whole flies, heads, gonads and carcasses revealed multiple isoforms of the D. melanogaster MIPS protein. Moreover, gender specific differential expression of the approximately 63kDa, 62kDa and 40kDa MIPS isoforms is apparent. Multiple isoforms of this protein have been demonstrated in other organisms, however this is the first demonstration of gender specific expression of the MIPS isoforms. These isoforms may be generated by alternate splicing of the MIPS transcript. In silico experiments demonstrate the existence of cDNAs that could encode some of the MIPS isoforms. These studies contribute to understanding the role of inositol synthesis in development and neurological disorders.