Abstract
Mammalian-secreted phospholipases A2 (sPLA2) form a diverse family of at least nine enzymes that hydrolyze phospholipids to release free fatty acids and lysophospholipids. We report here the cloning and characterization of human group IIF sPLA2 (hGIIF sPLA2). The full-length cDNA codes for a signal peptide of 20 amino acid followed by a mature protein of 148 amino acids containing all of the structural features of catalytically active group II sPLA2s. hGIIF sPLA2 gene is located on chromosome 1 and lies within a sPLA2 gene cluster of about 300 kbp that also contains the genes for group IIA, IIC, IID, IIE, and V sPLA2s. In adult tissues, hGIIF is highly expressed in placenta, testis, thymus, liver, and kidney. Finally, recombinant expression of hGIIF sPLA2 in Escherichia coli shows that the enzyme is Ca2+-dependent, maximally active at pH 7–8, and hydrolyzes phosphatidylglycerol versus phosphatidylcholine with a 15-fold preference.
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