cDNA cloning and functional expression of jerdostatin, a novel RTS-disintegrin from Trimeresurus jerdonii and a specific antagonist of the alpha(1)beta(1) integrin
文献类型：期刊论文
| 作者 | Sanz L1; Chen RQ2; Marcinkiewicz C3; Monleon D4; Celda B4; Xiong YL2; Perez-Paya E5; Calvete JJ[*]1; Perez A2; Hilario R1 |
| 刊名 | JOURNAL OF BIOLOGICAL CHEMISTRY
 |
| 出版日期 | 2006 |
| 卷号 | 280期号:49页码:40714-40722 |
| 英文摘要 | Jerdostatin represents a novel RTS-containing short disintegrin cloned by reverse transcriptase-PCR from the venom gland mRNA of the Chinese Jerdons pit viper Trimeresurus jerdonii. The jerdostatins precursor cDNA contained a 333-bp open reading frame encoding a signal peptide, a pre-peptide, and a 43-amino acid disintegrin domain, whose amino acid sequence displayed 80% identity with that of the KTS-disintegrins obtustatin and viperistatin. The jerdostatin cDNA structure represents the first complete open reading frame of a short disintegrin and points to the emergence of jerdostatin from a short-coding gene. The different residues between jerdostatin and obtustatin/viperistatin are segregated within the integrin-recognition loop and the C-terminal tail. Native jerdostatin (r-jerdostatin-R21) and a R21K mutant (r-jerdostatin-K21) were produced in Escherichia coli. In each case, two conformers were isolated. One-dimensional (1)HNMRshowed that conformers 1 and 2 of r-jerdostatin-R21 represent, respectively, well folded and unfolded proteins. The two conformers of the wild-type and the R21K mutant inhibited the adhesion of alpha(1)-K562 cells to collagen IV with IC50 values of 180 and 703 nM, respectively. The IC50 values of conformers 2 of r-jerdostatin-R21 and r-jerdostatin-K21 were, respectively, 5.95 and 12.5 mu M. Neither r-jerdostatin-R21 nor r-jerdostatin-K21 showed inhibitory activity toward other integrins, including alpha(IIb)beta(3), alpha(v)beta(3), alpha(2)beta(1), alpha(5)beta(1), alpha(4)beta(1), alpha(6)beta(1), and alpha(9)beta(1) up to a concentration of 24 mu M. Although the RTS motif appears to be more potent than KTS inhibiting the alpha(1)beta(1) integrin, r-jerdostatin-R21 is less active than the KTS-disintegrins, strongly suggesting that substitutions outside the integrin- binding motif and/or C-terminal proteolytic processing are responsible for the decreased inhibitory activity. |
| 语种 | 英语 |
| 资助机构 | This work was supported in part by National Institutes of Health Grant RO1CA100145- 01A1 and American Heart Association Grant 0230163N (to C. M.), and Ministerio de Educacio ´nyCiencia,Madrid,Spain,GrantBFU2004–01432/BMC(toJ.J.C.).Thecosts of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact. ; This work was supported in part by National Institutes of Health Grant RO1CA100145- 01A1 and American Heart Association Grant 0230163N (to C. M.), and Ministerio de Educacio ´nyCiencia,Madrid,Spain,GrantBFU2004–01432/BMC(toJ.J.C.).Thecosts of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact. ; This work was supported in part by National Institutes of Health Grant RO1CA100145- 01A1 and American Heart Association Grant 0230163N (to C. M.), and Ministerio de Educacio ´nyCiencia,Madrid,Spain,GrantBFU2004–01432/BMC(toJ.J.C.).Thecosts of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact. ; This work was supported in part by National Institutes of Health Grant RO1CA100145- 01A1 and American Heart Association Grant 0230163N (to C. M.), and Ministerio de Educacio ´nyCiencia,Madrid,Spain,GrantBFU2004–01432/BMC(toJ.J.C.).Thecosts of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact. |
| 源URL | [http://159.226.149.26:8080/handle/152453/10591]  |
| 专题 | 昆明动物研究所_其他 |
| 通讯作者 | jcalvete@ibv.csic.es |
| 作者单位 | 1.Institutode Biomedicina de Valencia,C.S.I.C.,JaimeRoig11,46010Valencia,Spain 2.Department of Animal Toxinology,Kumming Institute of Zoology,TheChineseAcademyofSciences,Kumming650223,PeoplesRepublicofChina 3.College of Science and Technology,Center for Neurovirology and Cancer Biology,TempleUniversity,Philadelphia,Pennsylvania 19122 4.Departamento de QuımicaFısica,Universitatde Valencia,Dr.Moliner50,46100Valencia,Spain 5.Centrode Investigacion “PrincipeFelipe” and Consejo SuperiordeInvestigacionesCientı ´ficas,Avda.delSaler16,46013 Valencia, Spain |
| 推荐引用方式 GB/T 7714 | Sanz L,Chen RQ,Marcinkiewicz C,et al. cDNA cloning and functional expression of jerdostatin, a novel RTS-disintegrin from Trimeresurus jerdonii and a specific antagonist of the alpha(1)beta(1) integrin[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2006,280(49):40714-40722. |
| APA | Sanz L.,Chen RQ.,Marcinkiewicz C.,Monleon D.,Celda B.,...&jcalvete@ibv.csic.es.(2006).cDNA cloning and functional expression of jerdostatin, a novel RTS-disintegrin from Trimeresurus jerdonii and a specific antagonist of the alpha(1)beta(1) integrin.JOURNAL OF BIOLOGICAL CHEMISTRY,280(49),40714-40722. |
| MLA | Sanz L,et al."cDNA cloning and functional expression of jerdostatin, a novel RTS-disintegrin from Trimeresurus jerdonii and a specific antagonist of the alpha(1)beta(1) integrin".JOURNAL OF BIOLOGICAL CHEMISTRY 280.49(2006):40714-40722. |
入库方式： OAI收割
来源：昆明动物研究所
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