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Titolo:
Cloning a novel metallophosphoesterase gene from a kidney cDNA library of hypertensive rat
Autore:
Chern, TH; Chiang, FT; Hsu, KL; Lo, HM; Tseng, CD; Tseng, YZ;
Indirizzi:
Natl Yang Ming Univ, Sch Med, Inst Clin Med, Taipei 112, Taiwan Natl Yang Ming Univ Taipei Taiwan 112 Inst Clin Med, Taipei 112, Taiwan Natl Taiwan Univ, Coll Med, Dept Med, Taipei, Taiwan Natl Taiwan Univ Taipei Taiwan Univ, Coll Med, Dept Med, Taipei, Taiwan
Titolo Testata:
JOURNAL OF THE FORMOSAN MEDICAL ASSOCIATION
fascicolo: 1, volume: 99, anno: 2000,
pagine: 49 - 53
SICI:
0929-6646(200001)99:1<49:CANMGF>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
PURPLE ACID-PHOSPHATASES; ZN2+-GLYCEROPHOSPHOCHOLINE CHOLINEPHOSPHODIESTERASE; MOTIF; BRAIN; SITE;
Keywords:
cDNA library; spontaneously hypertensive rat; kidney; metallophosphoesterase; modified; equalized kidney cDNA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Citazioni:
19
Recensione:
Indirizzi per estratti:
Indirizzo: Tseng, YZ Natl Taiwan Univ Hosp, Dept Internal Med, 7 Chung Shan S Rd, Taipei 100, Taiwan Natl Taiwan Univ Hosp 7 Chung Shan S Rd Taipei Taiwan 100 aiwan
Citazione:
T.H. Chern et al., "Cloning a novel metallophosphoesterase gene from a kidney cDNA library of hypertensive rat", J FORMOS ME, 99(1), 2000, pp. 49-53

Abstract

Background and purpose: Genetic and environmental factors may contribute to the pathogenesis of essential hypertension. To facilitate genetic studiesof hypertension and renal disorders, we sought to clone novel genes from amodified, equalized kidney (MEK) cDNA library of a spontaneously hypertensive rat (SHR). Methods: A kidney cDNA library of an SHR was synthesized using the modified equalization method. Inserts of 350 random clones were amplified by polymerase chain reaction (PCR) and sequenced, of which 246 were presumably unknown after being compared against a nonredundant database in the GenBank. The cDNA ends of clone 383 were obtained by rapid amplification of cDNA ends,sequenced, and then analyzed with Translate, Prosite, Profile, SignalP, and TMpred programs. Results: The full-length cDNA was 938 bp, and translated into a 182-amino acid protein. The deduced protein had a metallophosphoesterase domain, a signal peptide at its amino end, a protein kinase C phosphorylation site, anda transmembrane domain. Northern blot analysis revealed that this gene wasexpressed in the heart, brain, spleen, lungs, liver, skeletal muscles, kidneys and testes of Sprague-Dawley rats. A putative protein of Arabidopsis thaliana shares 62% homology with protein 38S, but the two proteins differ in terms of function and structure. Conclusions: Our results support that protein 38S is a novel membrane metallophosphoesterase, although its function in the kidneys remains to be elucidated. This study also demonstrates the feasibility of using PCR to clone novel genes from our MEK cDNA library.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/08/20 alle ore 02:19:04