Evidence map›Paper›PMID 38704122›Full record

ArticleJournal of thrombosis and haemostasis : JTH2024

Nanobody activator improves sensitivity of the von Willebrand factor activity assay to multimer size.

Qian Liang, Ernest T Parker, Gabrielle Dean, Matthew S Karpen, Yujia Wu, Xuefeng Wang, Jorge Di Paola, Cheryl L Maier, Shannon L Meeks, Pete Lollar and 2 more

Abstract read
In one paragraph

Article in Journal of thrombosis and haemostasis : JTH, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors.

Qian LiangDepartment of Laboratory Medicine, Ruijin Hospital, Shanghai Jiaotong University School of Medicine, Shanghai, China; Aflac Cancer and Blood Disorders Center, Children's Healthcare of Atlanta, Department of Pediatrics, Emory University School of Medicine, Atlanta, Georgia, USA.
Ernest T ParkerAflac Cancer and Blood Disorders Center, Children's Healthcare of Atlanta, Department of Pediatrics, Emory University School of Medicine, Atlanta, Georgia, USA.
Gabrielle DeanAflac Cancer and Blood Disorders Center, Children's Healthcare of Atlanta, Department of Pediatrics, Emory University School of Medicine, Atlanta, Georgia, USA.
Matthew S KarpenAflac Cancer and Blood Disorders Center, Children's Healthcare of Atlanta, Department of Pediatrics, Emory University School of Medicine, Atlanta, Georgia, USA.
Yujia WuDepartment of Statistics, School of Statistics and Center of Statistical Research, Southwestern University of Finance and Economics, Chengdu, China.
Xuefeng WangDepartment of Laboratory Medicine, Ruijin Hospital, Shanghai Jiaotong University School of Medicine, Shanghai, China.
Jorge Di PaolaDepartment of Pediatrics, Washington University School of Medicine, St. Louis, Missouri, USA.
Cheryl L MaierDepartment of Pathology and Laboratory Medicine, Emory University School of Medicine, Atlanta, Georgia, USA.
Shannon L MeeksAflac Cancer and Blood Disorders Center, Children's Healthcare of Atlanta, Department of Pediatrics, Emory University School of Medicine, Atlanta, Georgia, USA.
Pete LollarAflac Cancer and Blood Disorders Center, Children's Healthcare of Atlanta, Department of Pediatrics, Emory University School of Medicine, Atlanta, Georgia, USA.
Robert F SidonioAflac Cancer and Blood Disorders Center, Children's Healthcare of Atlanta, Department of Pediatrics, Emory University School of Medicine, Atlanta, Georgia, USA.
Renhao LiAflac Cancer and Blood Disorders Center, Children's Healthcare of Atlanta, Department of Pediatrics, Emory University School of Medicine, Atlanta, Georgia, USA. Electronic address: renhao.li@emory.edu.

Funding

Conformational activation of von Willebrand factorR01HL143794 · NHLBI · EMORY UNIVERSITY · PI LI, RENHAO · 2018 to 2021
$2.7M
GPIb-IX and VWF in thrombosis and thrombocytopeniaR35HL166654 · NHLBI · EMORY UNIVERSITY · PI LI, RENHAO · 2023 to 2023
$1.1M
NHLBI NIH HHS R01 HL143794NHLBI NIH HHS R35 HL166654
6 · The paper itself

Abstract

backgroundThe activity of von Willebrand factor (VWF) in facilitating platelet adhesion and aggregation correlates with its multimer size. Traditional ristocetin-dependent functional assays lack sensitivity to multimer sizes. Recently, nanobodies targeting the autoinhibitory module and activating VWF were identified.

objectivesTo develop an assay that can differentiate the platelet-binding activity of VWF multimers.

methodsA novel enzyme-linked immunosorbent assay (nanobody-triggered glycoprotein Ib binding assay [VWF:GPIbNab]) utilizing a VWF-activating nanobody was developed. Recombinant VWF, plasma-derived VWF (pdVWF), and selected gel-filtrated fractions of pdVWF were evaluated for VWF antigen and activity levels. A linear regression model was developed to estimate the specific activity of VWF multimers.

resultsOf the 3 activating nanobodies tested, 6C11 with the lowest activation effect exhibited the highest sensitivity for high-molecular-weight multimers (HMWMs) of VWF. VWF:GPIbNab utilizing 6C11 (VWF:GPIbNab

conclusionThe VWF:GPIbNab

Indexed as

Enzyme-Linked Immunosorbent AssayProtein MultimerizationSingle-Domain Antibodiesvon Willebrand FactorBlood PlateletsHumansLinear ModelsMolecular WeightPlatelet AdhesivenessPlatelet AggregationPlatelet Glycoprotein GPIb-IX ComplexProtein BindingRecombinant ProteinsPlatelet Glycoprotein GPIb-IX ComplexRecombinant ProteinsSingle-Domain Antibodiesvon Willebrand Factornanobodyplateletristocetinsensitivityvon Willebrand factor

Identifiers

PMID38704122
PMCPMC11214880

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.