Meng Jun

Email Address
obgmj@nus.edu.sg


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ANATOMY
dept

Publication Search Results

Now showing 1 - 2 of 2
  • Publication
    Hydrogen sulfide promotes nitric oxide production in corpus cavernosum by enhancing expression of endothelial nitric oxide synthase
    (2013-05) Meng, J.; Adaikan, P.G.; Srilatha, B.; OBSTETRICS & GYNAECOLOGY
    Recently, hydrogen sulfide (H 2 S) has been identified as a potential therapy for ED. However, a thorough understanding of its molecular mechanisms of action would be essential to develop H 2 S as a new therapy for ED. In this study, the effect of H 2 S on nitric oxide (NO) production, especially through the expression of constitutive nitric oxide synthase (NOS) isoforms - endothelial NOS (eNOS) and neuronal NOS (nNOS) in rat corpus cavernosum (CC) were explored. Real-time PCR studies subsequent to in vitro treatment of sodium hydrosulfide hydrate (NaHS), a stable H 2 S donor, showed increases in eNOS but not nNOS mRNA. Western blot studies confirmed that the exogenously applied NaHS increased eNOS but not nNOS protein expression in the rat CC. Furthermore, NaHS did not alter the expressed amounts of Caveolin-1 (CAV-1), a dominant inhibitory interaction partner of eNOS, in these tissues. Not surprisingly, NaHS also enhanced the NO production in eNOS-associated membrane fraction of rat CC. Taken together, we ascertain that H 2 S could exert its proerectile effects by augmenting NO pathway. It appears that H 2 S would be particularly useful in improving the clinical outcome of ED patients, whose erectile impairment is due to an inherent attenuation of the endothelial NO formation in the cavernosum. © 2012 Macmillan Publishers Limited All rights reserved.
  • Publication
    Cloning and molecular characterization of BmHYA1, a novel hyaluronidase from the venom of Chinese red scorpion Buthus martensi Karsch
    (2010) Feng, L.; Gao, R.; Meng, J.; Gopalakrishnakone, P.; INTERACTIVE & DIGITAL MEDIA INSTITUTE; ANATOMY; BIOLOGICAL SCIENCES; OBSTETRICS & GYNAECOLOGY
    In this communication, the full protein sequence of a novel venom hyaluronidase BmHYA1 was reported. It is the first full hyaluronidase amino acid sequence from scorpion venom. It was deduced from nucleotide sequence by 3' Rapid Amplification of cDNA Ends (RACE) PCR cloning, followed by alignment with the N-terminal amino acid sequence, which was obtained by Edman degradation. BmHYA1 has 385 amino acid residues containing five potential N-glycosylation sites. The phylogenetic analysis indicates early divergence and independent evolution of BmHYA1 from other hyaluronidases. © 2010 Elsevier Ltd.