title: Cloning, characterization, expression and comparative analysis of pig Golgi membrane sphingomyelin synthase 1.
abstract: Pig sphingomyelin synthase 1 (SMS1) cDNA was cloned, characterized and compared to the human ortholog. Porcine protein consists of 413 amino acids and displays a 97% sequence identity with human protein. A phylogenic tree of proteins reveals that porcine SMS1 is more closely related to bovine and rodent proteins than to human. Analysis of protein mass was higher than the theoretical prediction based on amino acid sequence suggesting a kind of posttranslational modification. Quantitative representation of tissue distribution obtained by real-time RT-PCR showed that it was widely expressed although important variations in levels were obtained among organs. Thus, the cardiovascular system, especially the heart, showed the highest value of all the tissues studied. Regional differences of expression were observed in the central nervous system and intestinal tract. Analysis of the hepatic mRNA and protein expressions of SMS1 following turpentine treatment revealed a progressive decrease in the former paralleled by a decrease in the protein concentration. These findings indicate the variation in expression in the different tissues might suggest a different requirement of Golgi sphingomyelin for the specific function in each organ and a regulation of the enzyme in response to turpentine-induced hepatic injury.
authors.affiliation: Departamento de Bioquímica y Biología Molecular y Celular, Facultad de Veterinaria, Universidad de Zaragoza, Miguel Servet 177, E-50013 Zaragoza, Spain.
authors.forename: Natalia
authors.initials: N
authors.lastname: Guillén
authors.forename: María A
authors.initials: MA
authors.lastname: Navarro
authors.forename: Joaquín C
authors.initials: JC
authors.lastname: Surra
authors.forename: Carmen
authors.initials: C
authors.lastname: Arnal
authors.forename: Marta
authors.initials: M
authors.lastname: Fernández-Juan
authors.forename: Jose Alvaro
authors.initials: JA
authors.lastname: Cebrián-Pérez
authors.forename: Jesús
authors.initials: J
authors.lastname: Osada
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D015152:Blotting, Northern; D002490:Central Nervous System / Q000201:enzymology / Q000378:metabolism; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000737:chemistry / Q000235:genetics; D005260:Female; D020869:Gene Expression Profiling; D006056:Golgi Apparatus / Q000201:enzymology*; D007249:Inflammation / Q000201:enzymology / Q000235:genetics / Q000662:veterinary; D007413:Intestinal Mucosa / Q000378:metabolism; D007422:Intestines / Q000201:enzymology; D007668:Kidney / Q000201:enzymology / Q000378:metabolism; D008099:Liver / Q000201:enzymology / Q000378:metabolism; D008297:Male; D008969:Molecular Sequence Data; D009206:Myocardium / Q000201:enzymology / Q000378:metabolism; D010802:Phylogeny; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D020133:Reverse Transcriptase Polymerase Chain Reaction; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D013552:Swine / Q000235:genetics*; D013553:Swine Diseases / Q000201:enzymology / Q000235:genetics; D017855:Transferases (Other Substituted Phosphate Groups) / Q000235:genetics* / Q000378:metabolism
chemical_list: D018076:DNA, Complementary; D012333:RNA, Messenger; D017855:Transferases (Other Substituted Phosphate Groups); C070186:phosphatidylcholine-ceramide phosphocholine transferase