caa a22 4500 445845236 CHVBK 20180317145356.0 cr unu---uuuuu 170323e20110301xx s 000 0 eng 10.1007/s10709-011-9549-1 doi (NATIONALLICENCE)springer-10.1007/s10709-011-9549-1 Vertebrate endothelial lipase: comparative studies of an ancient gene and protein in vertebrate evolution [Elektronische Daten] [Roger Holmes, John VandeBerg, Laura Cox] Endothelial lipase (gene: LIPG; enzyme: EL) is one of three members of the triglyceride lipase family that contributes to lipoprotein degradation within the circulation system and plays a major role in HDL metabolism in the body. In this study, in silico methods were used to predict the amino acid sequences, secondary and tertiary structures, and gene locations for LIPG genes and encoded proteins using data from several vertebrate genome projects. LIPG is located on human chromosome 18 and is distinct from other human ‘neutral lipase' genes, hepatic lipase (gene: LIPC; enzyme: HL) and lipoprotein lipase (gene: LPL; enzyme: LPL) examined. Vertebrate LIPG genes usually contained 10 coding exons located on the positive strand for most primates, as well as for horse, bovine, opossum, platypus and frog genomes. The rat LIPG gene however contained only 9 coding exons apparently due to the presence of a ‘stop' codon' within exon 9. Vertebrate EL protein subunits shared 58-97% sequence identity as compared with 38-45% sequence identities with human HL and LPL. Four previously reported human EL N-glycosylation sites were predominantly conserved among the 10 potential N-glycosylation sites observed for the vertebrate EL sequences examined. Sequence alignments and identities for key EL amino acid residues were observed as well as conservation of predicted secondary and tertiary structures with those previously reported for horse pancreatic lipase (PL) (Bourne et al. 1994). Several potential sites for regulating LIPG gene expression were observed including CpG islands near the LIPG gene promoter and a predicted microRNA binding site near the 3'-untranslated region. Promoter regions containing functional polymorphisms that regulate HDL cholesterol in baboons were conserved among primates but not retained between primates and rodents. Phylogenetic analyses examined the relationships and potential evolutionary origins of the vertebrate LIPG gene subfamily with other neutral triglyceride lipase gene families, LIPC and LPL. It is apparent that the triglyceride lipase ancestral gene for the vertebrate LIPG gene predated the appearance of fish during vertebrate evolution >500millionyearsago. Springer Science+Business Media B.V., 2011 Vertebrates nationallicence Amino acid sequence nationallicence Endothelial lipase nationallicence Evolution nationallicence Gene duplication nationallicence Holmes Roger Department of Genetics, Southwest Foundation for Biomedical Research, San Antonio, TX, USA aut VandeBerg John Department of Genetics, Southwest Foundation for Biomedical Research, San Antonio, TX, USA aut Cox Laura Department of Genetics, Southwest Foundation for Biomedical Research, San Antonio, TX, USA aut Genetica Springer Netherlands 139/3(2011-03-01), 291-304 0016-6707 139:3<291 2011 139 10709 https://doi.org/10.1007/s10709-011-9549-1 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10709-011-9549-1 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Holmes Roger Department of Genetics, Southwest Foundation for Biomedical Research, San Antonio, TX, USA aut NATIONALLICENCE 700 1- VandeBerg John Department of Genetics, Southwest Foundation for Biomedical Research, San Antonio, TX, USA aut NATIONALLICENCE 700 1- Cox Laura Department of Genetics, Southwest Foundation for Biomedical Research, San Antonio, TX, USA aut NATIONALLICENCE 773 0- Genetica Springer Netherlands 139/3(2011-03-01), 291-304 0016-6707 139:3<291 2011 139 10709 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer