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10.1182/blood-2015-12-688747 http://scihub22266oqcxt.onion/10.1182/blood-2015-12-688747 C4937355!4937355 !27207796     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27207796 &cmd=llinks): Failed to open stream: HTTP request failed! 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Human neutrophil peptides inhibit cleavage of von Willebrand factor by ADAMTS13: a potential link of inflammation to TTP |pdf=|usr=}}{{27207796 }} gab.com Text Human neutrophil peptides inhibit cleavage of von Willebrand factor by ADAMTS13: a potential link of inflammation to TTP JO: Blood http://www.kidney.de/pget.php?&tw=1&pmid=27207796 #FOAvip Infection or inflammation may precede and trigger formation of microvascular thrombosis in patients with acquired thrombotic thrombocytopenic purpura (TTP). However, the mechanism underlying this clinical observation is not fully understood. Here, we show that human neutrophil peptides (HNPs) released from activated and degranulated neutrophils inhibit proteolytic cleavage of von Willebrand factor (VWF) by ADAMTS13 in a concentration-dependent manner. Half-maximal inhibitory concentrations of native HNPs toward ADAMTS13-mediated proteolysis of peptidyl VWF73 and multimeric VWF are 3.5 ?M and 45 ?M, respectively. Inhibitory activity of HNPs depends on the RRY motif that is shared by the spacer domain of ADAMTS13. Native HNPs bind to VWF73 (KD = 0.72 ?M), soluble VWF (KD = 0.58 ?M), and ultra-large VWF on endothelial cells. Enzyme-linked immunosorbent assay (ELISA) demonstrates markedly increased plasma HNPs1-3 in most patients with acquired autoimmune TTP at presentation (median, ?170 ng/mL; range, 58-3570; n = 19) compared with healthy controls (median, ?23 ng/mL; range, 6-44; n = 18) (P < .0001). Liquid chromatography plus tandem mass spectrometry (LC-MS/MS) reveals statistically significant increases of HNP1, HNP2, and HNP3 in patient samples (all P values <.001). There is a good correlation between measurement of HNPs1-3 by ELISA and by LC-MS/MS (Spearman ? = 0.7932, P < .0001). Together, these results demonstrate that HNPs1-3 may be potent inhibitors of ADAMTS13 activity, likely by binding to the central A2 domain of VWF and physically blocking ADAMTS13 binding. Our findings may provide a novel link between inflammation/infection and the onset of microvascular thrombosis in acquired TTP and potentially other immune thrombotic disorders. Twit Text FOAVip Human neutrophil peptides inhibit cleavage of von Willebrand factor by ADAMTS13: a potential link of inflammation to TTP ????Blood http://www.kidney.de/pget.php?&tw=1&pmid=27207796 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27207796 #FOAvip English Wikipedia <ref>{{Cite pmid|27207796 }}</ref> Human neutrophil peptides inhibit cleavage of von Willebrand factor by ADAMTS13: a potential link of inflammation to TTP #MMPMID27207796 Pillai VG ; Bao J ; Zander CB ; McDaniel JK ; Chetty PS ; Seeholzer SH ; Bdeir K ; Cines DB ; Zheng XL Blood 2016[Jul]; 128 (1 ): 110-9 PMID27207796 show ga Infection or inflammation may precede and trigger formation of microvascular thrombosis in patients with acquired thrombotic thrombocytopenic purpura (TTP). However, the mechanism underlying this clinical observation is not fully understood. Here, we show that human neutrophil peptides (HNPs) released from activated and degranulated neutrophils inhibit proteolytic cleavage of von Willebrand factor (VWF) by ADAMTS13 in a concentration-dependent manner. Half-maximal inhibitory concentrations of native HNPs toward ADAMTS13-mediated proteolysis of peptidyl VWF73 and multimeric VWF are 3.5 ?M and 45 ?M, respectively. Inhibitory activity of HNPs depends on the RRY motif that is shared by the spacer domain of ADAMTS13. Native HNPs bind to VWF73 (KD = 0.72 ?M), soluble VWF (KD = 0.58 ?M), and ultra-large VWF on endothelial cells. Enzyme-linked immunosorbent assay (ELISA) demonstrates markedly increased plasma HNPs1-3 in most patients with acquired autoimmune TTP at presentation (median, ?170 ng/mL; range, 58-3570; n = 19) compared with healthy controls (median, ?23 ng/mL; range, 6-44; n = 18) (P < .0001). Liquid chromatography plus tandem mass spectrometry (LC-MS/MS) reveals statistically significant increases of HNP1, HNP2, and HNP3 in patient samples (all P values <.001). There is a good correlation between measurement of HNPs1-3 by ELISA and by LC-MS/MS (Spearman ? = 0.7932, P < .0001). Together, these results demonstrate that HNPs1-3 may be potent inhibitors of ADAMTS13 activity, likely by binding to the central A2 domain of VWF and physically blocking ADAMTS13 binding. Our findings may provide a novel link between inflammation/infection and the onset of microvascular thrombosis in acquired TTP and potentially other immune thrombotic disorders. |*Proteolysis [MESH] |ADAMTS13 Protein/*metabolism [MESH] |Amino Acid Motifs [MESH] |Defensins/*metabolism [MESH] |Female [MESH] |Humans [MESH] |Inflammation/metabolism/pathology [MESH] |Male [MESH] |Neutrophils/*metabolism/pathology [MESH] |Purpura, Thrombotic Thrombocytopenic/*metabolism/pathology [MESH]Human neutrophil peptides inhibit cleavage of von Willebrand factor by(epmc).pdf DeepDyve Pubget Overpricing