Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase
Patent
1997-07-07
1999-10-26
Prouty, Rebecca E.
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Hydrolase
536 232, C12N 920, C12N 1555
Patent
active
059726776
ABSTRACT:
Novel mammalian phospholipase (PLA.sub.2) nucleotide sequences and low molecular weight (about 14KD) amino acid sequences encoded thereby are disclosed. More particularly, a cloned human HPLA.sub.2 cDNA expressing HPLA.sub.2 -10 and its cloned rat RPLA.sub.2 cDNA counterpart, expressing RPLA.sub.2 -10, which are characterized as PLA.sub.2 Type IV, are disclosed. A second type of PLA.sub.2 cDNA, characterized as PLA.sub.2 Type III and exemplified by a rat PLA.sub.2 cDNA encoding RPLA.sub.2 -8 and a partial human PLA.sub.2 nucleotide sequence encoding HPLA.sub.2 -8, is disclosed. Expression of the cDNAs encode the two new types of PLA.sub.2 enzymes which have phospholipase activity. The novel PLA.sub.2 s do not include disulfide bridges between cysteine amino acids 11 and 77 or elapid loops. However, the novel PLA.sub.2 s may include amino acid COOH-terminal extensions which can vary in length. Seventeen of the eighteen absolutely conserved amino acids in all active 14KD PLA.sub.2 s are believed to be conserved in RPLA.sub.2 -8 and HPLA.sub.2 -8, whereas all eighteen are believed to be conserved in RPLA.sub.2 -10 and HPLA.sub.2 -10. Because the encoded sequences of RPLA.sub.2 -8 and HPLA.sub.2 -8 include only 16 cysteine amino acids, they have been designated as Type III. RPLA.sub.2 -10 and HPLA.sub.2 -10 are designated as Type IV since their encoded sequences include only 12 cysteine amino acids.
REFERENCES:
patent: 5019508 (1991-05-01), Johnson et al.
Westermann, et al., "Inhibition of expression of SV40 virus large T-antigen by antisense oligodeoxyribonucleotides," Biomed. Biochim. Acta 48 (1989) 1, 85-93.
Seilhamer, et al., "Novel Gene Exon Homologous to Pancreatic Phospholipase A.sub.2 : Sequence and Chromosomal Mapping of Both Human Genes," Journal of Cellular Biochemistry 39:327-337 (1989).
Macejak, et al., "Internal initiation of translation mediated by the 5'leader of a cellular mRNA," Nature. vol. 353, Sep. 5, 1991, 90-94.
Young, et al., "Utilization of an Epstein-Barr virus replicon as a eukaryotic expression vector," Gene, 62 (Feb. 1988) 171-185.
Bekkers, et al, "The use of genetic engineering to obtain efficient production of porcine pancreatic phospholipase A.sub.2 by Saccharomyces cerevisiae, " Biochimica et Biophisica Acta, 1089 (1991) 345-351.
Deng, et al, "A novel expression vector for high-level synthesis and secretion of foreign proteins in Escherichia coli: overproduction of bovine pancreatic phospholipase A.sub.2," Gene 93 (1990) 229-234.
J.J. Seilhamer et al. "Novel Gene Exon Homologous to . . . " J. Cell. Biochem. 39:327-337 (1989).
R.L. Heinrikson "Dissection and Sequence Analysis . . . " Meth. in Enzymology 197:201-214 (1991).
Davidson, et al., Evolutionary Relationships and Implications for the Regulation of Phospholipase A.sub.2 from Snake Venom to Human Secreted Forms, J. Mol. Evol (1990) 31:228-238.
Seilhamer Jeffrey J.
Tischfield Jay A.
Incyte Pharmaceuticals Inc.
Prouty Rebecca E.
Tischfield J.
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