The Distribution Of Porcine TGH Gene And Its Primary Analysis By Bioinformatics

Lipolysis is an important process determining fuel metabolism.Adipose tissure lipolysis is the catabolic process leading to thebreakdown of triglycerdes stored in fat cell and the release of fatty acids and glycerol.The lipolytic catabolism of stored fat in adipose tissure supplies tissues with fatty acids as metabolites and energy substrates during times of food deprivation.Hormone sensitive lipase (HSL) is the first intracellular lipase to be cloned for Triacylglycerol hydrolysis ,which was once considered as the only limited enzyme in lipolysis. The characterization of hormone-sensitive lipase is not uniquely responsible for the hydrolysis of triccylgycerols and diacylglycerols of stored fat. Triacylglycerol hydrolase(TGH) is another key lipase of lipolysis in 2004. TGH has already been considered playing a certain role in lipolysis, now there is no report with TGH lipolysis function in mammal.The present study examined the distrution of pig TGH gene in different tissues with RT-PCR and Western-blot, analyzed the pathway of TGH by bioinformatics, which estabolished the base for bioinformatics research of TGH. The main results were summarized as following:1. Successfully cloned the pig TGH gene, and the GenBank accession number is EF525540. Homologous alignment analysis showed that the porcine TGH gene has 95%,85%and 86%homology to that of human, rat and mouse respectively.2. TGH expression is different in transcription and translation level. At seven tissues(heart, liver, kidney , epiploica adipose, subcutaneous adipose, spleen, lung) , there are all mRNA expression. Notable differences(P<0.5)is discoversd in epiploica adipose, subcutaneous adipose, liver and other tissues. There have signals in all tissues, excepting heart and kidney.3. The specific analysis of TGH in subcutaneous fat showed that TGH expression in subcutaneous fat of obese pig was lower than lean individuals on transcription and translation level, which was consistent with the results of deceased TGH expression in human and rodents.4. Bioinformatic analysis suggested that the difference of TGH and HSL function was caused by their different secondary structure. However, TGH and HSL existed the similar secretory structure, which were both guided by signal peptide.