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dc.contributor.authorHolmes, Roger S
dc.contributor.authorCox, Laura A
dc.date.accessioned2017-05-03T13:52:13Z
dc.date.available2017-05-03T13:52:13Z
dc.date.issued2012
dc.date.modified2013-06-21T03:48:26Z
dc.identifier.issn2190-572X
dc.identifier.doi10.1007/s13205-012-0087-z
dc.identifier.urihttp://hdl.handle.net/10072/51807
dc.description.abstractLipase H (LIPH) is a membrane-bound phospholipase generating 2-acyl lysophosphatidic acid (LPA) in the body. LPA is a lipid mediator required for maintaining homeostasis of diverse biological functions and in activating cell surface receptors such as P2Y5, which plays an essential role in hair growth. Bioinformatic methods were used to predict the amino acid sequences, secondary and tertiary structures, and gene locations for LIPH genes and encoded proteins using data from several vertebrate genome projects. Vertebrate LIPH genes contained ten coding exons transcribed on either the positive or negative DNA strands. Evidence is presented for duplicated LIPH genes for the chicken and zebra fish genomes. Vertebrate LIPH protein subunits shared 56-97 % sequence identities and exhibited sequence alignments and identities for key LIPH amino acid residues as well as extensive conservation of predicted secondary and tertiary structures with those previously reported for horse pancreatic lipase (LIPP), with 'N-signal peptide', 'lipase,' and 'plat' structural domains. Comparative studies of vertebrate LIPH sequences with other phospholipase A1-like lipases (LIPI and PS-PLA1), as well as vascular and pancreatic lipases, confirmed predictions for LIPH N-terminal signal peptides (residues 1-18); a conserved vertebrate LIPH N-glycosylation site (66NVT for human LIPH); active site 'triad' residues (Ser 154; Asp 178; His 248); disulfide bond residues (233-246; 270-281; 284-292; 427-446), and a 'short' 12 residue 'active site lid', which is comparable to other phospholipases examined. Phylogenetic analyses demonstrated the relationships and potential evolutionary origins of the vertebrate LIPH family of genes related to, but distinct from other phospholipase A1-like genes (LIPI and PS-PLA1), and from vascular lipase and pancreatic lipase gene families.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.format.extent1364719 bytes
dc.format.mimetypeapplication/pdf
dc.languageEnglish
dc.language.isoeng
dc.publisherSpringer
dc.publisher.placeGermany
dc.relation.ispartofstudentpublicationN
dc.relation.ispartofpagefrom263
dc.relation.ispartofpageto275
dc.relation.ispartofissue4
dc.relation.ispartofjournal3 Biotech
dc.relation.ispartofvolume2
dc.rights.retentionY
dc.subject.fieldofresearchBiochemistry and cell biology
dc.subject.fieldofresearchGenomics
dc.subject.fieldofresearchcode3101
dc.subject.fieldofresearchcode310509
dc.titleComparative structures and evolution of vertebrate lipase H (LIPH) genes and proteins: a relative of the phospholipase A1 gene families
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.rights.copyright© The Author(s) 2012. This is a SpringerOpen Access license agreement which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
gro.date.issued2012
gro.hasfulltextFull Text
gro.griffith.authorHolmes, Roger S.


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