Premium
Identification of the DAG Lipase alpha‐1 and beta‐1 mRNA transcripts in Human Tissues.
Author(s) -
liang yanbin,
Li Chen,
guzman Victor,
Woodward David
Publication year - 2008
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.22.1_supplement.791.4
Subject(s) - lipase , diacylglycerol lipase , biology , alternative splicing , lipoprotein lipase , messenger rna , biochemistry , microbiology and biotechnology , gene , enzyme , diacylglycerol kinase , protein kinase c
Using human DAG lipase α and β specific RT‐PCR, we identified two alternatively spliced variants of human DAG lipase mRNAs, DAG lipase α–1 and β‐1, in human multiple tissues. The alternative splicing of DAG lipase α‐1 occurred at +206 (Gene bank: NM_006133 ), spliced out 212 bp (+206 to +418 bp) of the coding region, and encoded a 956 amino acid DAG lipase α‐1 protein. The N‐terminus of DAG lipase α–1 differed from that of DAG lipase α. The alternative splicing of DAG lipase β‐1 occurred at 360 (Gene bank: NM_139179 ), spliced out 552 bp (+360 to +912 bp) of the coding region, and encoded a 391 amino acid DAG lipase β‐1 protein with a 281 amino acid N‐terminal deletion. This study is the first to document alternative splicing of DAG lipase genes. We therefore studied DAG lipase α‐1 and DAG lipase β‐1 mRNA distribution in human tissues (heart, kidney, brain, lung, liver, spleen, and small intestine). DAG lipase α‐1 mRNA was highly expressed in heart, kidney, brain, liver, spleen, small intestine and smooth muscle, but not lung. DAG lipase β‐1 mRNA was highly expressed in kidney, brain, spleen, small intestine and smooth muscle, but not heart, liver, and lung. DAG lipase α‐1 and DAG lipase β‐1 were not found in rat and mouse tissues, indicating species specificity of the alternative splicing variants of DAG lipase mRNA expression. When recombinant DAG lipase α‐1 and DAG lipase β‐1 were expressed in HEK293/EBNA cells, DAG lipase α‐1 was present almost exclusively in membrane, whereas DAG lipase β‐1 was present in cytosolic fractions. The data suggest that the N‐terminus of DAG lipases may be important for this protein translocating to the cell membrane, and alternative splicing variants of DAG lipase α or β may play an unique role in the regulation of “on‐demand” 2‐AG production in human tissues.