tailieunhanh - Báo cáo khoa học: Murine serum nucleases – contrasting effects of plasmin and heparin on the activities of DNase1 and DNase1-like 3 (DNase1l3)

DNase1 is regarded as the major serum nuclease; however, a systematic investigation into the presence of additional serum nuclease activities is lacking. We have demonstrated directly that serum contains DNase1-like 3 (DNase1l3) in addition to DNase1 by an improved denaturing SDS-PAGE zymography method and anti-murine DNase1l3 immunoblotting. | ỊFEBS Journal Murine serum nucleases - contrasting effects of plasmin and heparin on the activities of DNasel and DNase1-like 3 DNase1l3 Markus Napirei Sebastian Ludwig Jamal Mezrhab Thomas Klockl and Hans G. Mannherz Abteilung fur Anatomie und Embryologie Medizinische Fakultat Ruhr-Universitat Bochum Germany Keywords DNase1 DNase1l3 plasminogen system serum systemic lupus erythematosus Correspondence M. Napirei Abteilung fur Anatomie und Embryologie Medizinische FakulteSt Ruhr-Universitat Bochum UniversitatsstraBe 150 D-44801 Bochum Germany Fax 49 2343214474 Tel 49 2343223164 E-mail Received 8 November 2008 revised 27 November 2008 accepted 10 December 2008 doi DNasel is regarded as the major serum nuclease however a systematic investigation into the presence of additional serum nuclease activities is lacking. We have demonstrated directly that serum contains DNase1-like 3 DNase1l3 in addition to DNase1 by an improved denaturing SDS-PAGE zymography method and anti-murine DNase1l3 immunoblotting. Using DNA degradation assays we compared the activities of recombinant murine DNase1 and DNase1l3 rmDNase1 rmDNase1l3 with the serum of wild-type and DNasel knockout mice. Serum and rmDNase1 degrade chromatin effectively only in cooperation with serine proteases such as plasmin or thrombin which remove DNA-bound proteins. This can be mimicked by the addition of heparin which displaces histones from chromatin. In contrast serum and rmDNase1l3 degrade chromatin without proteolytic help and are directly inhibited by heparin and proteolysis by plasmin. In previous studies serum DNase1l3 escaped detection because of its sensitivity to proteolysis by plasmin after activation of the plasminogen system in the DNA degradation assays. In contrast DNase1 is resistant to plasmin probably as a result of its di-N-glycosylation which is lacking in DNase1l3. Our data demonstrate that secreted rmDNase1 and murine parotid DNase1 are .

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