ADAMTS‐13 plasma level determination uncovers antigen absence in acquired thrombotic thrombocytopenic purpura and ethnic differences

Feys, Hendrik B.; Liu, Fang; Dong, Ningzheng; Pareyn, Inge; Vauterin, Stefaan; Vandeputte, Nele; Noppe, Wim; Ruan, Changgeng; Deckmyn, Hans; Vanhoorelbeke, Karen

doi:10.1111/j.1538-7836.2006.01833.x

Cited by 83 publications

(90 citation statements)

References 39 publications

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“…Monoclonal antibody 20D2 was prepared essentially as described previously. 24 A sheep-anti-mouse-HRP-labeled antibody (in conjunction with 20A5 and 20D2) and a donkey antirabbit-HRP-labeled antibody (in conjunction with the rabbit antimetalloprotease antibody), both obtained from GE Healthcare (Bio-Sciences AB, Uppsala, Sweden), were used for chemiluminescence detection (Roche Applied Science, Almere, the Netherlands).…”

Section: Construction and Expression Of Recombinant Adamts13 And Trunmentioning

confidence: 99%

Residues Arg568 and Phe592 contribute to an antigenic surface for anti-ADAMTS13 antibodies in the spacer domain

Pos¹,

Sorvillo²,

Fijnheer³

et al. 2011

Haematologica

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The online version of this article has a Supplementary Appendix. BackgroundThe majority of patients diagnosed with thrombotic thrombocytopenic purpura have autoantibodies directed towards the spacer domain of ADAMTS13. Design and MethodsIn this study we explored the epitope specificity and immunoglobulin class and immunoglobulin G subclass distribution of anti-ADAMTS13 antibodies. The epitope specificity of antispacer domain antibodies was examined using plasma from 48 patients with acute acquired thrombotic thrombocytopenic purpura by means of immunoprecipitation of ADAMTS13 variants containing single or multiple alanine substitutions. Using similar methods, we also determined the presence of anti-TSP2-8 and CUB1-2 domain antibodies in this cohort of patients.

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Section: Construction and Expression Of Recombinant Adamts13 And Trunmentioning

confidence: 99%

Residues Arg568 and Phe592 contribute to an antigenic surface for anti-ADAMTS13 antibodies in the spacer domain

Pos¹,

Sorvillo²,

Fijnheer³

et al. 2011

Haematologica

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118

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“…The VWF-GpIb:BC of pooled standard plasma (see above) was arbitrarily given a ratio of 1.0. ADAMTS13 antigen was measured in Kortrijk using the ELISA described by Feys et al [7], with values expressed in percentage of a pooled plasma (see above) arbitrarily taken as 100%.…”

mentioning

confidence: 99%

Active platelet‐binding conformation of plasma von Willebrand factor in young women with acute myocardial infarction

Peyvandi

Hollestelle

Palla

et al. 2010

Journal of Thrombosis and Haemostasis

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, a monophasic clearance was observed (not shown) similar to FX/AP 176-194-N181A-N191A . However, its elimination was slower than for FX/AP 176-194-N181A-N191A but faster compared with wt-FX (Fig. 1C). Thus, In conclusion, the carboxy-terminal end of AP plays a crucial role in FX catabolism, both in recovery and half-life, mainly through N-glycosylation sites at positions 181 and 191. Further studies are needed to determine the cells and the receptors involved in this process. Finally, these findings could be useful in improving half-life or recovery of future therapeutic molecules based on FX, especially in blood disorders. Disclosure of Conflict of InterestsThe authors state that they have no conflict of interest.

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“…Hereditary TTP can be efficiently treated by simple fresh frozen plasma (FFP) infusion that rapidly reverses acute bouts of the disease, and, when given prophylactically at 2-3-week intervals, prevents relapses [24,25]. Acquired TTP with autoantibodymediated inhibition of ADAMTS-13 activity is best treated with plasma exchange and large volume FFP replacement, and immunosuppressive medication to suppress inhibitory autoantibodies is needed in addition [see 17].The paper by Feys and coworkers [26] makes an important contribution to the diagnostic armamentarium for ADAMTS-13 measurement. The authors report an ADAMTS-13 antigen Correspondence: B. La¨mmle,…”

mentioning

confidence: 99%

“…The paper by Feys and coworkers [26] makes an important contribution to the diagnostic armamentarium for ADAMTS-13 measurement. The authors report an ADAMTS-13 antigen sandwich ELISA, using a murine monoclonal antibody (2G3) as capturing antibody and a mixture of two different biotinylated monoclonal antibodies (8C10 and 13F7) as detecting antibodies.…”

mentioning

confidence: 99%

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A new tool to further explore the role of ADAMTS‐13 in health and disease

Lämmle

Hovinga

2006

Journal of Thrombosis and Haemostasis

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See also Feys HB, Liu F, Dong N, Pareyn I, Vauterin S, Vandeputte N, Noppe W, Ruan C, Deckmyn H, Vanhoorelbeke K. ADAMTS-13 plasma level determination uncovers antigen absence in acquired thrombotic thrombocytopenic purpura and ethnic differences. This issue, pp 955-62.In 1996, a hitherto unrecognized protease was isolated from human plasma [1,2] that cleaved multimeric von Willebrand factor (VWF) in vitro to cleavage fragments previously reported to be generated in vivo [3]. Shortly after its discovery this VWFcleaving protease activity was found to be severely deficient in many patients diagnosed with acute idiopathic thrombotic thrombocytopenic purpura (TTP) [4][5][6], most often because of inhibitory IgG autoantibodies in acute acquired TTP [5][6][7], but sometimes also in siblings with an obviously hereditary form of TTP without inhibiting autoantibodies [4,5], a condition previously denoted as Upshaw-Schulman syndrome [8,9].In 2001, the VWF-cleaving protease was purified from human plasma to homogeneity allowing partial amino acid sequencing [10][11][12] and identification of the enzyme as a member of the ADAMTS (a disintegrin-like and metalloprotease with thrombospondin type 1-motifs) family of metalloproteases, denoted as ADAMTS-13 [13]. Independently, genome-wide linkage analysis in pedigrees affected by hereditary TTP identified the same gene and several different ADAMTS-13 mutations were reported: double heterozygous or homozygous mutations were putatively responsible for severely deficient ADAMTS-13 activity in affected patients; heterozygous carriers of mutations were asymptomatic and showed about 50% of normal VWF-cleaving protease activity [14].Even though functionally active recombinant ADAMTS-13 has been expressed in transfected mammalian cells already in 2002 [15], and many diagnostic studies on VWF-cleaving protease activity and functionally inhibiting autoantibodies in patients with TTP, other thrombotic microangiopathies and other disorders have been reported [for review, see 16-18], assays of ADAMTS-13 activity in human plasma have been subject to ongoing controversy. Several ADAMTS-13 activity assays, based on the degradation of purified or recombinant multimeric VWF by patient plasma and analyzing its multimeric pattern [1,5] Two multicenter studies [20,21] on several of these activity assays have been performed and generally have shown acceptable agreement concerning the detection of severe ADAMTS-13 functional deficiency ( < 5% of normal plasma activity); however, there was less concordance of the results on plasma samples with mildly decreased or normal ADAMTS-13 activity. Moreover, some assays proved to be clearly unreliable for diagnostic purposes [21]. A recently developed functional assay using a truncated 73-amino acid VWF peptide encompassing the 1605 Y-1606 M cleavage site and labeled with a fluorescent and quencher group on both sites of the cleavage site, respectively, allows for rapid activity measurement of ADAMTS-13 by fluorescence resonance energy transfer and may greatly...

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ADAMTS‐13 plasma level determination uncovers antigen absence in acquired thrombotic thrombocytopenic purpura and ethnic differences

Abstract: Plasma level determination uncovers antigen absence in acquired thrombotic thrombocytopenic purpura and ethnic differences.

Cited by 83 publications

References 39 publications

Residues Arg568 and Phe592 contribute to an antigenic surface for anti-ADAMTS13 antibodies in the spacer domain

Residues Arg568 and Phe592 contribute to an antigenic surface for anti-ADAMTS13 antibodies in the spacer domain

Active platelet‐binding conformation of plasma von Willebrand factor in young women with acute myocardial infarction

A new tool to further explore the role of ADAMTS‐13 in health and disease

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