Yan-Ping Zhang

Changshu Institute of Technology, Chiu-ch’üan, Gansu Sheng, China

Are you Yan-Ping Zhang?

Claim your profile

Publications (2)1.99 Total impact

  • Source
    [show abstract] [hide abstract]
    ABSTRACT: Myostatin is a member of the TGF-beta superfamily and acts as a negative regulator of skeletal muscle growth. The characterization of the myostatin gene and its expression in Trachidermus fasciatus was reported in the current study. A full-length of 2 568 bp myostatin cDNA sequence in T. fasciats was cloned by 5' and 3' RACE, which included a 1 131 bp complete ORF encoding a 376 amino acid peptide, a 106 bp long 5'-UTR and a 1331 bp long 3'UTR. As other MSTN, the putative peptide contains a 22 amino acids long signal peptide, a conserved RARR proteolytic processing site, and 10 conserved cysteine residues in the C terminal of the protein. The Trachidermus fasciatus MSTN has high homology with Umbrina cirrosa, Morone saxatilis, Morone americana, Morone chrysops myostatin while has low homology with mammalian and birds myostatin. The phylogenetic analysis showed that the T. fasciatus myostatin had the closest relationship with U. cirrosa. In the four examined tissues, the myostatin gene was highly expressed in muscle and intestine and weakly expressed in brain and liver. These results suggested that the fish myostatin gene might not only play roles in muscle development but also contribute to other biological functions.
    Zoological Research 08/2010; 31(4):387-94.
  • [show abstract] [hide abstract]
    ABSTRACT: A novel disintegrin, stejnin, was purified from the Trimeresurus stejnegeri venom by gel filtration and reverse phase high performance liquid chromatography. The molecular weight of stejnin was determined to be 7428 Da by MALD-TOF MS analysis. The cDNA encoding the precursor of stejnin was cloned from the venom gland. From the deduced amino acid sequence, stejnin is composed of 71 amino acid residues contains the tripeptide sequence Arg-Gly-Asp (RGD), a well-known characteristic of the disintegrin family. Stejnin strongly inhibited ADP- and ristomycin-induced human platelet aggregation with IC50 of 45 and 50 nM, respectively. Stejnin also possessed potent inhibited cell proliferation of ECV304 cells.
    Protein and Peptide Letters 02/2007; 14(5):437-41. · 1.99 Impact Factor