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dc.contributor.authorChen, J. G.zh_CN
dc.contributor.authorXu, X. N.zh_CN
dc.contributor.authorUnderhfll, C. B.zh_CN
dc.contributor.authorYang, S. M.zh_CN
dc.contributor.authorWang, L. P.zh_CN
dc.contributor.authorChen, Y. X.zh_CN
dc.contributor.authorHong, S. G.zh_CN
dc.contributor.authorCreswell, K.zh_CN
dc.contributor.authorZhang, L. R.zh_CN
dc.contributor.author陈奕欣zh_CN
dc.date.accessioned2013-12-12T02:24:31Z
dc.date.available2013-12-12T02:24:31Z
dc.date.issued2005-06-01zh_CN
dc.identifier.citationCancer Research, 2005,65(11):4614-4622zh_CN
dc.identifier.issn0008-5472zh_CN
dc.identifier.otherISI:000229407800020zh_CN
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/65599
dc.description.abstractTachyplesin is a small, cationic peptide that possesses antitumor properties. However, little is known about its action mechanism. We used phage display to identify a protein that interacted with tachyplesin and isolated a sequence corresponding to the collagen-like domain of C1q, a key component in the complement pathway. Their interaction was subsequently confirmed by both ELISA and affinity precipitation. Tachyplesin seemed to activate the classic complement cascade because it triggered several downstream events, including the cleavage and deposition of C4 and C3 and the formation of C5b-9. When TSU tumor cells were treated with tachyplesin in the presence of serum, activated C4b and C3b could be detected on tumor cells by flow cytometry, Western blotting, and confocal microscopy. However, this effect was blocked when the tumor cells were treated with hyaluronidase or a large excess of hyaluronan, indicating that hyaluronan or related glycosaminoglycans were involved in this process. Treatment of cells with tachyplesin and serum increased in membrane permeability as indicated by the ability of FITC-dextran to enter the cytoplasm. Finally, the combination of tachyplesin and human serum markedly inhibited the proliferation and caused death of TSU cells, and these effects were attenuated if the serum was heat-inactivated or if hyaluronidase was added. Taken together, these observations suggest that tachyplesin binds to both hyaluronan on the cell surface and C1q in the serum and activates the classic complement cascade, which damages the integrity of the membranes of the tumor cells resulting in their death.zh_CN
dc.language.isoen_USzh_CN
dc.source.urihttp://dx.doi.org/10.1158/0008-5472.CAN-04-2253zh_CN
dc.subjectKLEBSIELLA-PNEUMONIAEzh_CN
dc.subjectHYALURONAN SYNTHASE-3zh_CN
dc.subjectANTIBIOTIC PEPTIDEzh_CN
dc.subjectIMMUNE-COMPLEXESzh_CN
dc.subjectPROSTATE-CANCERzh_CN
dc.subjectC1Qzh_CN
dc.subjectMEMBRANEzh_CN
dc.subjectGROWTHzh_CN
dc.subjectDEFENSINSzh_CN
dc.subjectBINDINGzh_CN
dc.titleTachyplesin activates the classic complement pathway to kill tumor cellszh_CN
dc.typeArticlezh_CN


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