ArticleBlood2020
Protease activity in single-chain prekallikrein.
Article in Blood, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
22 citing papers in PubMed, 38 citations in OpenAlex.
- Prekallikrein: the catalytic crossroads of inflammation and thrombosis.Current opinion in hematology · 2026Review
- A novel polypeptide from stony coral Goniopora columna inhibits thrombosis by interfering with the contact-kinin pathway.Archives of toxicology · 2025Article
- Aqueous carbonic anhydrase-1 overexpression and its association with cytokine profiles and macular structural changes in retinal vein occlusion-associated macular edema.Scientific reports · 2025Article
- Combining Metabolomics and Proteomics to Reveal Key Serum Compounds Related to Canine Intervertebral Disc Herniation.Metabolites · 2025Article
- A model of zymogen factor XII: insights into protease activation.Blood advances · 2025Article
- Antithrombotic coating with sheltered positive charges prevents contact activation by controlling factor XII-biointerface binding.Nature materials · 2025Article
- Identification and characterization of factor XI autoantibodies in 2 patients with systemic lupus erythematosus: insights into mechanisms of acquired factor XI deficiency.Research and practice in thrombosis and haemostasis · 2025Article
- A mechanistic model of in vitro plasma activation to evaluate therapeutic kallikrein-kinin system inhibitors.PLoS computational biology · 2024Article
- Characterization and Hemocompatibility of α, β, and γ Cyclodextrin-Modified Magnetic Nano-Adsorbents.International journal of molecular sciences · 2024Article
- Factor XII Structure-Function Relationships.Seminars in thrombosis and hemostasis · 2024Review
- Bat-derived oligopeptide LE6 inhibits the contact-kinin pathway and harbors anti-thromboinflammation and stroke potential.Zoological research · 2024Article
- Plasma kallikrein supports FXII-independent thrombin generation in mouse whole blood.Blood advances · 2024Article
- Hemocompatibility of β-Cyclodextrin-Modified (Methacryloyloxy)ethyl Phosphorylcholine Coated Magnetic Nanoparticles.Biomolecules · 2023Article
- Combined oral contraceptives may activate the contact system in healthy women.Research and practice in thrombosis and haemostasis · 2023Article
- Mechanisms involved in hereditary angioedema with normal C1-inhibitor activity.Frontiers in physiology · 2023Review
- Oral FXIIa inhibitor KV998086 suppresses FXIIa and single chain FXII mediated kallikrein kinin system activation.Frontiers in pharmacology · 2023Article
- Novel interaction of properdin and coagulation factor XI: Crosstalk between complement and coagulation.Research and practice in thrombosis and haemostasis · 2022Article
- Proteolysis and Deficiency of α1-Proteinase Inhibitor in SARS-CoV-2 Infection.Biochemistry (Moscow) Supplement. Series B, Biomedical chemistry · 2022Article
- Kallikrein augments the anticoagulant function of the protein C system in thrombin generation.Journal of thrombosis and haemostasis : JTH · 2022Article
- Proteolytic activity of contact factor zymogens.Journal of thrombosis and haemostasis : JTH · 2021Review
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
Abstract
Prekallikrein (PK) is the precursor of the trypsin-like plasma protease kallikrein (PKa), which cleaves kininogens to release bradykinin and converts the protease precursor factor XII (FXII) to the enzyme FXIIa. PK and FXII undergo reciprocal conversion to their active forms (PKa and FXIIa) by a process that is accelerated by a variety of biological and artificial surfaces. The surface-mediated process is referred to as contact activation. Previously, we showed that FXII expresses a low level of proteolytic activity (independently of FXIIa) that may initiate reciprocal activation with PK. The current study was undertaken to determine whether PK expresses similar activity. Recombinant PK that cannot be converted to PKa was prepared by replacing Arg371 with alanine at the activation cleavage site (PK-R371A, or single-chain PK). Despite being constrained to the single-chain precursor form, PK-R371A cleaves high-molecular-weight kininogen (HK) to release bradykinin with a catalytic efficiency ∼1500-fold lower than that of kallikrein cleavage of HK. In the presence of a surface, PK-R371A converts FXII to FXIIa with a specific activity ∼4 orders of magnitude lower than for PKa cleavage of FXII. These results support the notion that activity intrinsic to PK and FXII can initiate reciprocal activation of FXII and PK in solution or on a surface. The findings are consistent with the hypothesis that the putative zymogens of many trypsin-like proteases are actually active proteases, explaining their capacity to undergo processes such as autoactivation and to initiate enzyme cascades.
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Registered trials
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.