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Journal articles on the topic 'Apc protein'

Author: Grafiati

Published: 10 March 2023

Last updated: 31 July 2025

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1

Brugge, Jeroen, Guido Tans, Jan Rosing, and Elisabetta Castoldi. "Protein S levels modulate the activated protein C resistance phenotype induced by elevated prothrombin levels." Thrombosis and Haemostasis 95, no. 02 (2006): 236–42. http://dx.doi.org/10.1160/th05-08-0582.

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SummaryElevated plasma prothrombin levels, due to the prothrombin 20210 G/A mutation or to acquired causes, area risk factor for venous thrombosis,partly because of prothrombin-mediated inhibition of the protein C anticoagulant pathway and consequent activated proteinC (APC) resistance. We determined the effect of plasma prothrombin concentration on the APC resistance phenotype and evaluated the role of protein S levels asa modulating variable. The effect of prothrombin and protein S levels on APC resistance was investigated in reconstituted plasma systems and in a population of healthy indivi

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Sen, Prosenjit, Sanghamitra Sahoo, Usha Pendurthi, and L. Vijaya Mohan Rao. "Zinc Binding to Protein C and Activated Protein C Modulates Their Interaction with Endothelial Cell Protein C Receptor." Blood 114, no. 22 (2009): 331. http://dx.doi.org/10.1182/blood.v114.22.331.331.

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Abstract Abstract 331 Introduction/background: Zinc is a multi-functional element that is essential for life and the second most abundant metal ion, after iron in eukaryotic organisms. Zinc deficiency has been associated with bleeding disorders and with defective platelet aggregation, suggesting it may play an important role in hemostasis. Zinc ions have been shown to enhance activation of the intrinsic pathway of coagulation but to down-regulate the extrinsic pathway of coagulation. All vitamin K-dependent coagulation proteins have calcium binding sites and may therefore to some extent, inter

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Preston, Roger JS, Shona Harmon, Fionnuala B. Ni Ainle, et al. "Dissociation of Activated Protein C Functions by Elimination of Protein S Cofactor Enhancement." Blood 112, no. 11 (2008): 21. http://dx.doi.org/10.1182/blood.v112.11.21.21.

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Abstract Activated protein C (APC) plays a critical anticoagulant role by inactivating factor Va (FVa) and factor VIIIa (FVIIIa) and thus down-regulating thrombin generation. In addition, APC bound to the endothelial cell protein C receptor (EPCR) can initiate PAR-1 mediated cytoprotective signalling. Although protein S constitutes a critical cofactor for APC anticoagulant function, the molecular basis through which protein S interacts with APC is not fully understood. In this study, we employed a site-directed mutagenesis strategy to characterise the effects of four single amino acid substitu

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Marx, Antje, Hans Weiler, Volker Liebe, et al. "Stabilization of monocyte chemoattractant protein-1-mRNA by activated protein C." Thrombosis and Haemostasis 89, no. 01 (2003): 149–60. http://dx.doi.org/10.1055/s-0037-1613554.

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SummaryThe activated protein C (APC) pathway has been suggested to be a common link between coagulation and inflammation. APC may function to restore hemostasis via modulation of cytokine expression. We investigated the effect of APC on the endothelial expression of monocyte chemoattractant protein-1 (MCP-1), a chemokine that is controlled by the activation of central proinflammatory transcription factors, such as nuclear factor-kappa B (NF-κ B).We found that human APC (2.5-10 μ g/ml) upregulated the amount of MCP-1-mRNA in human umbilical vein endothelial cells (HUVEC) and caused a time- and

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Stefanski, Casey D., Anne Arnason, Sara Maloney, et al. "APC Loss Prevents Doxorubicin-Induced Cell Death by Increasing Drug Efflux and a Chemoresistant Cell Population in Breast Cancer." International Journal of Molecular Sciences 24, no. 8 (2023): 7621. http://dx.doi.org/10.3390/ijms24087621.

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Chemoresistance is a major health concern affecting cancer patients. Resistance is multifactorial, with one mechanism being the increased expression of ABC transporters (such as MDR1 and MRP1), which are drug efflux transporters capable of preventing intracellular accumulation of drugs and cell death. Our lab showed that the loss of Adenomatous Polyposis Coli (APC) caused an intrinsic resistance to doxorubicin (DOX), potentially through an enhanced tumor-initiating cell (TIC) population and the increased activation of STAT3 mediating the expression of MDR1 in the absence of WNT being activated

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Maurissen, Lisbeth F. A., M. Christella L. G. D. Thomassen, Gerry A. F. Nicolaes, et al. "Re-evaluation of the role of the protein S-C4b binding protein complex in activated protein C-catalyzed factor Va-inactivation." Blood 111, no. 6 (2008): 3034–41. http://dx.doi.org/10.1182/blood-2007-06-089987.

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AbstractProtein S expresses cofactor activity for activated protein C (APC) by enhancing the APC-catalyzed proteolysis at R306 in factor Va. It is generally accepted that only free protein S is active and that complex formation with C4b-binding protein (C4BP) inhibits the APC-cofactor activity of protein S. However, the present study shows that protein S-C4BP expresses APC-cofactor activity and stimulates APC-catalyzed proteolysis at R306 more than 10-fold, but instead inhibits proteolysis at R506 by APC 3- to 4-fold. Free protein S stimulates APC-catalyzed cleavage at R306 approximately 20-fo

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Nishioka, Junji, Masaru Ido, Tatsuya Hayashi, and Koji Suzuki. "The Gla26 Residue of Protein C Is Required for the Binding of Protein C to Thrombomodulin and Endothelial Cell Protein C Receptor, but not to Protein S and Factor Va." Thrombosis and Haemostasis 75, no. 02 (1996): 275–82. http://dx.doi.org/10.1055/s-0038-1650260.

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SummaryA functionally defective protein C (PC)-Mie, detected in the plasma of a patient with hereditary thrombophilia, has Lys substituted for γ-carboxyglutamic acid (Gla)26 residue. The activation rate of PC-Mie by Protac or thrombin in the absence of Ca2+ and that by thrombin with native thrombomodulin (TM), recombinant soluble truncated TM or on cultured endothelial cells in the presence of Ca2+ were all apparently lower than that of normal PC. The anticoagulant activity of Protac-activated PC (APC)-Mie on the plasma clotting time and the rate of inactivation of factor Va by APC-Mie in the

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8

Pérez-Casal, Margarita, Colin Downey, Kenji Fukudome, Gernot Marx, and Cheng Hock Toh. "Activated protein C induces the release of microparticle-associated endothelial protein C receptor." Blood 105, no. 4 (2005): 1515–22. http://dx.doi.org/10.1182/blood-2004-05-1896.

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Abstract Activated protein C (APC) treatment is now used for patients with severe sepsis. We investigated its effect in vitro on primary, physiologically relevant cells and demonstrate a novel mechanism of endothelial protein C receptor (EPCR) release that is not inhibited by metalloproteinase inhibitors. Exposure of human umbilical vein endothelial cells or monocytes to APC (6.25-100 nM) results in the release of EPCR-containing microparticles, as demonstrated by confocal microscopy and characterized through flow cytometry, enzyme-linked immunosorbent assay quantitation of isolated microparti

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Brinkman, Herm Jan, Erica Sellink, Bas de Laat, and Koen Mertens. "Differential Anticoagulant Effects of Protein S on Vascular Cells and Platelets." Blood 112, no. 11 (2008): 2026. http://dx.doi.org/10.1182/blood.v112.11.2026.2026.

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Abstract Background: Protein S is a vitamin K-dependent plasma protein and involved in down-regulation of the coagulation process. Protein S serves as a cofactor of activated protein C (APC) in the proteolytic inactivation of activated factor V and VIII. Protein S is also able to exert its anticoagulant activity independent of APC, e.g. by supporting the anticoagulant activity of tissue factor pathway inhibitor (TFPI). The anticoagulant properties of protein S have been thoroughly characterized by in vitro methods. However, fewer studies focus on protein S function on vascular cells. These stu

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Preston, Roger JS, Jennifer A. Johnson, Fionnuala Ni Ainle, et al. "Platelet Factor 4 Mediates Activated Protein C Resistance by Impairment of Protein S Cofactor Enhancement." Blood 112, no. 11 (2008): 20. http://dx.doi.org/10.1182/blood.v112.11.20.20.

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Abstract Platelet factor 4 (PF4) is an abundant platelet α-granule chemokine released following platelet activation. PF4 interacts with thrombomodulin and the γ-carboxyglutamic acid (Gla) domain of protein C to significantly enhance activated protein C (APC) generation by the thrombin-thrombomodulin complex on the surface of endothelial cells. However, the protein C Gla domain not only mediates protein C activation in vivo, but also plays a critical role in modulating the diverse functional properties of APC once generated. The functional consequences of the interaction between the APC Gla dom

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de Fouw, N. J., Y. F. de Jong, F. Haverkate, and R. M. Bertina. "Activated Protein C Increases Fibrin Clot Lysis by Neutralization of Plasminogen Activator Inhibitor No Evidence for a Cofactor Role of Protein S." Thrombosis and Haemostasis 60, no. 02 (1988): 328–33. http://dx.doi.org/10.1055/s-0038-1647055.

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summaryThe effect of purified human activated protein G (APC) on fibrinolysis was studied using a clot iysis system consisting of purified glu-plasminogen, tissue-type plasminogen activator, plasminogen activator inhibitor (released from endothelial cells or blood platelets), fibrinogen, 125T-fibrinogen and thrombin. All proteins were of human origin.In this system APC could increase fibrinolysis in a dose dependent way, without affecting fibrin formation or fibrin crosslinking. However, this profibrinolytic effect of APC could only be observed when plasminogen activator inhibitor (PAI-l) was

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Jörgensen, Pia-Marie, Eva Brundell, Maria Starborg, and Christer Höög. "A Subunit of the Anaphase-Promoting Complex Is a Centromere-Associated Protein in Mammalian Cells." Molecular and Cellular Biology 18, no. 1 (1998): 468–76. http://dx.doi.org/10.1128/mcb.18.1.468.

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ABSTRACT Sister chromatids in early mitotic cells are held together mainly by interactions between centromeres. The separation of sister chromatids at the transition between the metaphase and the anaphase stages of mitosis depends on the anaphase-promoting complex (APC), a 20S ubiquitin-ligase complex that targets proteins for destruction. A subunit of the APC, called APC-α in Xenopus (and whose homologs are APC-1, Cut4, BIME, and Tsg24), has recently been identified and shown to be required for entry into anaphase. We now show that the mammalian APC-α homolog, Tsg24, is a centromere-associate

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Bolte, Melanie, Patrick Dieckhoff, Cindy Krause, Gerhard H. Braus, and Stefan Irniger. "Synergistic inhibition of APC/C by glucose and activated Ras proteins can be mediated by each of the Tpk1–3 proteins in Saccharomyces cerevisiae." Microbiology 149, no. 5 (2003): 1205–16. http://dx.doi.org/10.1099/mic.0.26062-0.

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Proteolysis triggered by the anaphase-promoting complex/cyclosome (APC/C) is essential for the progression through mitosis. APC/C is a highly conserved ubiquitin ligase whose activity is regulated during the cell cycle by various factors, including spindle checkpoint components and protein kinases. The cAMP-dependent protein kinase (PKA) was identified as negative regulator of APC/C in yeast and mammalian cells. In the yeast Saccharomyces cerevisiae, PKA activity is induced upon glucose addition or by activated Ras proteins. This study shows that glucose and the activated Ras2Val19 protein syn

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Deane, Rashid, Barbra LaRue, Abhay P. Sagare, Francis J. Castellino, Zhihui Zhong, and Berislav V. Zlokovic. "Endothelial Protein C Receptor-Assisted Transport of Activated Protein C across the Mouse Blood—Brain Barrier." Journal of Cerebral Blood Flow & Metabolism 29, no. 1 (2008): 25–33. http://dx.doi.org/10.1038/jcbfm.2008.117.

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Activated protein C (APC), a serine-protease with anticoagulant, anti-inflammatory, and cytoprotective activities, is neuroprotective and holds potential to treat different neurologic disorders. It is unknown whether APC crosses the blood—brain barrier (BBB) to reach its therapeutic targets in the brain. By using a brain vascular perfusion technique, we show that 125I-labeled plasma-derived mouse APC enters the brain from cerebrovascular circulation by a concentration-dependent mechanism. The permeability surface area product of 125I-APC (0.1 nmol/L) in different forebrain regions ranged from

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Van Walderveen, Maria Christina, Leslie R. Berry, and Anthony Chan. "Covalent Antithrombin-Heparin Complex Catalysis of Activated Protein C Inhibition by Protein C Inhibitor." Blood 114, no. 22 (2009): 3167. http://dx.doi.org/10.1182/blood.v114.22.3167.3167.

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Abstract Abstract 3167 Poster Board III-107 Introduction Thrombin (IIa), when bound to thrombomodulin (TM), readily converts protein C (PC) into activated PC (APC). APC functions as an anticoagulant by inactivating activated factors V (FVa) and VIII (FVIIIa), and indirectly reduces IIa generation. Once formed, APC activity is controlled through inhibition by PC inhibitor (PCI), a reaction that is catalyzed by heparin (H). Chan et al. developed a covalent antithrombin-heparin (ATH) complex with increased anticoagulant activity compared to H. The current investigation looked at the role and mech

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Barth, Angela I. M., Anne L. Pollack, Yoram Altschuler, Keith E. Mostov та W. James Nelson. "NH2-terminal Deletion of β-Catenin Results in Stable Colocalization of Mutant β-Catenin with Adenomatous Polyposis Coli Protein and Altered MDCK Cell Adhesion". Journal of Cell Biology 136, № 3 (1997): 693–706. http://dx.doi.org/10.1083/jcb.136.3.693.

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β-Catenin is essential for the function of cadherins, a family of Ca2+-dependent cell–cell adhesion molecules, by linking them to α-catenin and the actin cytoskeleton. β-Catenin also binds to adenomatous polyposis coli (APC) protein, a cytosolic protein that is the product of a tumor suppressor gene mutated in colorectal adenomas. We have expressed mutant β-catenins in MDCK epithelial cells to gain insights into the regulation of β-catenin distribution between cadherin and APC protein complexes and the functions of these complexes. Full-length β-catenin, β-catenin mutant proteins with NH2-term

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Joslyn, G., D. S. Richardson, R. White, and T. Alber. "Dimer formation by an N-terminal coiled coil in the APC protein." Proceedings of the National Academy of Sciences 90, no. 23 (1993): 11109–13. http://dx.doi.org/10.1073/pnas.90.23.11109.

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Mutations in the human APC gene are associated with an inherited predisposition to colon cancer. APC codes for polypeptides of approximately 2800 amino acids, with sequence homologies to coiled-coil proteins in the first 900 residues. To determine the oligomerization properties of the APC protein, we used genetic and biochemical approaches to examine the ability of APC fragments to self-associate. A subdomain comprising the first 55 amino acids of APC was found to form a stable, parallel, helical dimer, as expected for a coiled coil. The location of a key dimerization element at the N terminus

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Sun, Yong-Hui, Lei Shen, and Björn Dahlbäck. "Gla domain–mutated human protein C exhibiting enhanced anticoagulant activity and increased phospholipid binding." Blood 101, no. 6 (2003): 2277–84. http://dx.doi.org/10.1182/blood-2002-06-1691.

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Protein C is a member of the vitamin K– dependent protein family. Proteins in this family have similar γ-carboxyglutamic acid (Gla)–rich domains, but their affinities for negatively charged phospholipid membranes vary more than 1000-fold. We have shown that it is possible to enhance anticoagulant activity and membrane affinity of protein C by selective mutagenesis of the Gla domain. In this study, 3 new mutants, Q10G11N12 (QGN), S23E32D33Y44 (SEDY), and Q10G11N12S23E32D33Y44 (QGNSEDY), were created. In plasma-based coagulation assays, the activated form of QGNSEDY (QGNSEDY-APC) demonstrated ap

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Vorlaufer, Elisabeth, and Jan-Michael Peters. "Regulation of the Cyclin B Degradation System by an Inhibitor of Mitotic Proteolysis." Molecular Biology of the Cell 9, no. 7 (1998): 1817–31. http://dx.doi.org/10.1091/mbc.9.7.1817.

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The initiation of anaphase and exit from mitosis depend on the anaphase-promoting complex (APC), which mediates the ubiquitin-dependent proteolysis of anaphase-inhibiting proteins and mitotic cyclins. We have analyzed whether protein phosphatases are required for mitotic APC activation. In Xenopus egg extracts APC activation occurs normally in the presence of protein phosphatase 1 inhibitors, suggesting that the anaphase defects caused by protein phosphatase 1 mutation in several organisms are not due to a failure to activate the APC. Contrary to this, the initiation of mitotic cyclin B proteo

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HACKENG, Tilman M., Subramanian YEGNESWARAN, Arthur E. JOHNSON, and John H. GRIFFIN. "Conformational changes in activated protein C caused by binding of the first epidermal growth factor-like module of protein S." Biochemical Journal 349, no. 3 (2000): 757–64. http://dx.doi.org/10.1042/bj3490757.

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The first epidermal growth factor-like module of human plasma protein S (EGF1, residues 76–116) was chemically synthesized and tested for its ability to inhibit the anticoagulant cofactor activity of protein S for the anticoagulant protease, activated protein C (APC). EGF1 completely inhibited the stimulation of APC activity by protein S in plasma coagulation assays, with 50% inhibition at approx. 1µM EGF1, suggesting direct binding of EGF1 to APC. To investigate a direct interaction between EGF1 and APC, fluorescence resonance energy transfer (FRET) experiments were employed. APC labelled in

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Yegneswaran, Subramanian, Phuong Nguyen, John Griffin, and Andrew Gale. "Prothrombin amino terminal region helps protect coagulation factor Va from proteolytic inactivation by activated protein C." Thrombosis and Haemostasis 101, no. 01 (2009): 55–61. http://dx.doi.org/10.1160/th08-07-0491.

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SummaryThe hypothesis that prothrombin (FII) protects coagulation factor Va (FVa) from proteolytic inactivation by activated protein C (APC) was tested using purified proteins. FII dose-dependently protected FVa from APC proteolysis under conditions where competition of proteins for binding to negatively-charged phospholipid surface was not relevant (i.e. either at high phospholipid vesicle concentrations or using soluble dicaproylphosphatidylserine at levels below its critical micellar concentration). Cleavages in FVa at both Arg506 and Arg306 by APC were inhibited by FII. FII did not alter t

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van der Meer, Felix J. M., Nico H. van Tilburg, Aat van Wijngaarden, Irma K. van der Linden, Ernest Briët та Rogier M. Bertina. "A Second Plasma Inhibitor of Activated Protein C: α1-Antitrypsin". Thrombosis and Haemostasis 62, № 02 (1989): 756–62. http://dx.doi.org/10.1055/s-0038-1646897.

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SummaryInactivation of activated protein C (APC) in normal human plasma was studied in the absence and presence of heparin. In the absence of heparin APC inactivation followed pseudo-first order kinetics. In the presence of heparin the neutralization of APC was found to be biphasic. Up to 500 nM APC could be readily inactivated in normal plasma, indicating that the concentration of the APC inhibitor must be higher than previously assumed. Plasma deficient in the protein C inhibitor (PCI-I, as described by Suzuki and coworkers) and deficient in p2-glycoprotein I still possessed APC neutralizing

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Wijnen, Merel van, Jeanette G. Stam, Cornells van't Veer, et al. "The Interaction of Protein S with the Phospholipid Surface Is Essential for the Activated Protein C-independent Activity of Protein S." Thrombosis and Haemostasis 76, no. 03 (1996): 397–403. http://dx.doi.org/10.1055/s-0038-1650590.

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SummaryProtein S is a vitamin-K dependent glycoprotein involved in the regulation of the anticoagulant activity of activated protein C (APC). Recent data showed a direct anticoagulant role of protein S independent of APC, as demonstrated by the inhibition of prothrombinase and tenase activity both in plasma and in purified systems. This anticoagulant effect of protein S can be explained either by a direct interaction of protein S with one of the components of the complexes and/or by the interference with the binding of these components to phospholipid surfaces.During our investigation we noted

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Ostapenko, Denis, Janet L. Burton, Ruiwen Wang, and Mark J. Solomon. "Pseudosubstrate Inhibition of the Anaphase-Promoting Complex by Acm1: Regulation by Proteolysis and Cdc28 Phosphorylation." Molecular and Cellular Biology 28, no. 15 (2008): 4653–64. http://dx.doi.org/10.1128/mcb.00055-08.

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ABSTRACT The ubiquitin ligase activity of the anaphase-promoting complex (APC)/cyclosome needs to be tightly regulated for proper cell cycle progression. Substrates are recruited to the APC by the Cdc20 and Cdh1 accessory proteins. The Cdh1-APC interaction is inhibited through phosphorylation of Cdh1 by Cdc28, the major cyclin-dependent protein kinase in budding yeast. More recently, Acm1 was reported to be a Cdh1-binding and -inhibitory protein in budding yeast. We found that although Acm1 is an unstable protein and contains the KEN-box and D-box motifs typically found in APC substrates, Acm1

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Mosnier, Laurent O., Jose A. Fernandez, Antonella Zampolli, Xia V. Yang, Zaverio M. Ruggeri, and John H. Griffin. "In Vivo Anti-Thrombotic Potency of Engineered Activated Protein C Variants." Blood 110, no. 11 (2007): 2704. http://dx.doi.org/10.1182/blood.v110.11.2704.2704.

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Abstract Activated protein C (APC) has both anticoagulant activity via inactivation of factors Va and VIIIa and cytoprotective activities on cells that include anti-apoptotic and anti-inflammatory activities, alterations of gene expression profiles and protection of endothelial barrier function. The relative importance of APC’s anticoagulant activity vs. APC’s direct cytoprotective effects on cells for reduction of mortality in severe sepsis patients and protective effects in animal injury models is not entirely clear. In this current study, genetically engineered APC variants with different a

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Perez-Casal, Margarita, Kenji Fukudome, and Cheng Hock Toh. "A Novel Mechanism of Endothelial Protein C Receptor Release, in Microparticulate Form, by Activated Protein C." Blood 104, no. 11 (2004): 1923. http://dx.doi.org/10.1182/blood.v104.11.1923.1923.

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Abstract Activated protein C (APC) administration is now used for treating patients with severe sepsis. We investigated its effect on primary, physiologically relevant cells and demonstrate a novel mechanism of endothelial protein C receptor (EPCR) release from the cell surface. Exposure of human umbilical vein endothelial cells or monocytes to APC (from physiological levels of 0.5 up to 100nM) resulted in the increasing release of EPCR-containing microparticles (EPCR-MP), as demonstrated by confocal microscopy. Further characterisation through flow cytometry showed a concomitant fall in EPCR

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Shea, Lei, Xuhua He, and Björn Dahlbäck. "Synergistic Cofactor Function of Factor V and Protein S to Activated Protein C in the Inactivation of the Factor Villa – Factor IXa Complex." Thrombosis and Haemostasis 78, no. 03 (1997): 1030–36. http://dx.doi.org/10.1055/s-0038-1657682.

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SummaryHuman factor V has been shown not only to be a precursor to procoagulant factor Va but also to express anticoagulant properties. Thus, factor V was recently found to potentiate the effect of protein S as cofactor to activated protein C (APC) in the inactivation of the factor VIIIa-factor IXa complex. The purpose of this study was to determine whether the APC-cofactor function of factor V was also expressed in the bovine protein C system and to elucidate the molecular background for the species specificity of APC. For this purpose, the effects of protein S and factor V on APC-mediated in

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Kulkarni, Kiran, Ziguo Zhang, Leifu Chang, Jing Yang, Paula C. A. da Fonseca, and David Barford. "Building a pseudo-atomic model of the anaphase-promoting complex." Acta Crystallographica Section D Biological Crystallography 69, no. 11 (2013): 2236–43. http://dx.doi.org/10.1107/s0907444913018593.

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The anaphase-promoting complex (APC/C) is a large E3 ubiquitin ligase that regulates progression through specific stages of the cell cycle by coordinating the ubiquitin-dependent degradation of cell-cycle regulatory proteins. Depending on the species, the active form of the APC/C consists of 14–15 different proteins that assemble into a 20-subunit complex with a mass of approximately 1.3 MDa. A hybrid approach of single-particle electron microscopy and protein crystallography of individual APC/C subunits has been applied to generate pseudo-atomic models of various functional states of the comp

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Barford, David. "Structure, function and mechanism of the anaphase promoting complex (APC/C)." Quarterly Reviews of Biophysics 44, no. 2 (2010): 153–90. http://dx.doi.org/10.1017/s0033583510000259.

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AbstractThe complex molecular events responsible for coordinating chromosome replication and segregation with cell division and growth are collectively known as the cell cycle. Progression through the cell cycle is orchestrated by the interplay between controlled protein synthesis and degradation and protein phosphorylation. Protein degradation is primarily regulated through the ubiquitin proteasome system, mediated by two related E3 protein ubiquitin ligases, the Skp1 cullin F-box (SCF) and the anaphase promoting complex (also known as the cyclosome) (APC/C). The APC/C is a multi-subunit cull

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Wang, Yang, Yoshiaki Azuma, David Moore, Neil Osheroff та Kristi L. Neufeld. "Interaction between Tumor Suppressor Adenomatous Polyposis Coli and Topoisomerase IIα: Implication for the G2/M Transition". Molecular Biology of the Cell 19, № 10 (2008): 4076–85. http://dx.doi.org/10.1091/mbc.e07-12-1296.

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The tumor suppressor adenomatous polyposis coli (APC) is implicated in regulating multiple stages of the cell cycle. APC participation in G1/S is attributed to its recognized role in Wnt signaling. APC function in the G2/M transition is less well established. To identify novel protein partners of APC that regulate the G2/M transition, APC was immunoprecipitated from colon cell lysates and associated proteins were analyzed by matrix-assisted laser desorption ionization/time of flight (MALDI-TOF). Topoisomerase IIα (topo IIα) was identified as a potential binding partner of APC. Topo IIα is a cr

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Váradi, K., J. Rosing, G. Tans, I. Pabinger, B. Keil, and H. P. Schwarz. "Factor V Enhances the Cofactor Function of Protein S in the APC-Mediated Inactivation of Factor VIII: Influence of the Factor VR506Q Mutation." Thrombosis and Haemostasis 76, no. 02 (1996): 208–14. http://dx.doi.org/10.1055/s-0038-1650556.

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SummaryFactor V and protein S are cofactors of activated protein C (APC) which accelerate APC-mediated factor VIII inactivation. The effects of factor V and protein S were quantitated in a reaction system in which plasma factor VIII was inactivated by APC and the loss of factor VIII activity was monitored in a factor X-activating system in which a chro-mogenic substrate was used to probe factor Xa formation. Factor V increased the rate of APC-mediated factor VIII inactivation in a dose-dependent manner in representative plasma samples with protein S or factor V deficiency, abnormal factor V (h

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Gruber, A., E. Mori, GJ del Zoppo, L. Waxman, and JH Griffin. "Alteration of fibrin network by activated protein C." Blood 83, no. 9 (1994): 2541–48. http://dx.doi.org/10.1182/blood.v83.9.2541.2541.

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Abstract The antithrombotic plasma enzyme, activated protein C (APC), may play a role in thrombolysis. In vitro, acceleration of clot lysis by APC depends on its ability to inhibit the activation of prothrombin. The effect of APC on the assembly and dispersion of fibrin network was studied using turbidimetry, plasmin digestion of fibrin, and electron microscopy of plasma clots. The addition of APC before clotting but not after clotting accelerated clot lysis. The rate of increase in the turbidity of clotting plasma was reduced by APC. The turbidity of plasma clots containing APC was directly r

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Gruber, A., E. Mori, GJ del Zoppo, L. Waxman, and JH Griffin. "Alteration of fibrin network by activated protein C." Blood 83, no. 9 (1994): 2541–48. http://dx.doi.org/10.1182/blood.v83.9.2541.bloodjournal8392541.

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The antithrombotic plasma enzyme, activated protein C (APC), may play a role in thrombolysis. In vitro, acceleration of clot lysis by APC depends on its ability to inhibit the activation of prothrombin. The effect of APC on the assembly and dispersion of fibrin network was studied using turbidimetry, plasmin digestion of fibrin, and electron microscopy of plasma clots. The addition of APC before clotting but not after clotting accelerated clot lysis. The rate of increase in the turbidity of clotting plasma was reduced by APC. The turbidity of plasma clots containing APC was directly related to

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Feistritzer, Clemens, Laurent O. Mosnier, Enrico Di Cera, John H. Griffin, and Matthias Riewald. "Efficient Barrier Protective Signaling by Activated Protein C Is Mechanistically Linked to Protein C Activation on Endothelial Cells." Blood 106, no. 11 (2005): 28. http://dx.doi.org/10.1182/blood.v106.11.28.28.

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Abstract Protein C (PC) is activated by thrombomodulin-bound thrombin on the endothelial cell surface and activated protein C (APC) inhibits blood coagulation in a negative feedback loop. Endothelial PC receptor (EPCR) can bind PC/APC and activation of EPCR-bound PC is enhanced. Exogenous APC has barrier protective effects on endothelial cells that depend on EPCR binding and protease activated receptor-1 (PAR1) cleavage and that may contribute to the anti-inflammatory effects of APC. Plasma APC concentrations in vivo are low compared to the substrate PC and in order to induce protective signal

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Fernandez, Jose A., Hiroshi Deguchi, Natalie M. Pecheniuk, Subramanian Yegneswaran, Carole L. Banka, and John H. Griffin. "Plasma High Density Lipoprotein and Anticoagulant Response to Activated Protein C (APC) and Protein S." Blood 118, no. 21 (2011): 2249. http://dx.doi.org/10.1182/blood.v118.21.2249.2249.

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Abstract Abstract 2249 Previously we reported that plasma high density lipoprotein (HDL) enhances activated protein C (APC)/protein S (PS) anticoagulant action in plasma clotting and factor Va inactivation assays (APC/PS enhancement) and that lower HDL levels are found in male venous thrombosis patients or in patients with recurrent venous thrombosis versus controls, giving rise to our hypothesis that HDL helps protect against venous thrombosis. In this study, we sought (1) to identify which HDL particles enhance APC/PS activity, (2) to assess correlations between this activity and HDL particl

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Mosnier, Laurent O., Antonella Zampolli, Edward J. Kerschen, et al. "Hyperantithrombotic, noncytoprotective Glu149Ala-activated protein C mutant." Blood 113, no. 23 (2009): 5970–78. http://dx.doi.org/10.1182/blood-2008-10-183327.

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Abstract Activated protein C (APC) reduces mortality in severe sepsis patients. APC exerts anticoagulant activities via inactivation of factors Va and VIIIa and cytoprotective activities via endothelial protein C receptor and protease-activated receptor-1. APC mutants with selectively altered and opposite activity profiles, that is, greatly reduced anticoagulant activity or greatly reduced cytoprotective activities, are compared here. Glu149Ala-APC exhibited enhanced in vitro anticoagulant and in vivo antithrombotic activity, but greatly diminished in vitro cytoprotective effects and in vivo r

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Seré, Kristin M., Jan Rosing, and Tilman M. Hackeng. "Inhibition of thrombin generation by protein S at low procoagulant stimuli: implications for maintenance of the hemostatic balance." Blood 104, no. 12 (2004): 3624–30. http://dx.doi.org/10.1182/blood-2004-03-1146.

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The activated protein C (APC)–independent anticoagulant activity of protein S on tissue factor–induced thrombin generation was quantified in plasma. In absence of APC, protein S significantly decreased the endogenous thrombin potential (ETP) in a concentration-dependent manner. The APC-independent anticoagulant activity of protein S in plasma was not affected by phospholipid concentrations but strongly depended on tissue factor concentrations: protein S inhibited the ETP from 6% at 140 pM tissue factor to 74% at 1.4 pM tissue factor. Plasma with both 60% protein S and 140% prothrombin showed a

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Li, Xian, Sara J. Bidarian, Martha Sim, Xiaohong Song та Jeremy P. Wood. "Protein S Coordinates the Inhibition of Prothrombinase By Tfpiα and Activated Protein C". Blood 134, Supplement_1 (2019): 2386. http://dx.doi.org/10.1182/blood-2019-130799.

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Background: Protein S (PS), a vitamin K-dependent plasma glycoprotein, functions as a cofactor for the anticoagulants activated protein C (APC) and tissue factor (TF) pathway inhibitor alpha (TFPIa), which inhibit factors Va (FVa) and Xa (FXa), respectively. Although it is unclear which of these functions is/are important in vivo, homozygous deficiency of PS is associated with life-threatening thrombosis shortly after birth. FVa and FXa form the prothrombinase complex, which generates thrombin, suggesting that PS has a role in the direct inhibition of thrombin production. However, neither the

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Mosnier, Laurent O., Berislav V. Zlokovic, and John H. Griffin. "The cytoprotective protein C pathway." Blood 109, no. 8 (2006): 3161–72. http://dx.doi.org/10.1182/blood-2006-09-003004.

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Abstract Protein C is best known for its mild deficiency associated with venous thrombosis risk and severe deficiency associated with neonatal purpura fulminans. Activated protein C (APC) anticoagulant activity involves proteolytic inactivation of factors Va and VIIIa, and APC resistance is often caused by factor V Leiden. Less known is the clinical success of APC in reducing mortality in severe sepsis patients (PROWESS trial) that gave impetus to new directions for basic and preclinical research on APC. This review summarizes insights gleaned from recent in vitro and in vivo studies of the di

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Ahnström, Josefin, Helena M. Andersson, Kevin Canis та ін. "Activated protein C cofactor function of protein S: a novel role for a γ-carboxyglutamic acid residue". Blood 117, № 24 (2011): 6685–93. http://dx.doi.org/10.1182/blood-2010-11-317099.

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Abstract Protein S has an important anticoagulant function by acting as a cofactor for activated protein C (APC). We recently reported that the EGF1 domain residue Asp95 is critical for APC cofactor function. In the present study, we examined whether additional interaction sites within the Gla domain of protein S might contribute to its APC cofactor function. We examined 4 residues, composing the previously reported “Face1” (N33S/P35T/E36A/Y39V) variant, as single point substitutions. Of these protein S variants, protein S E36A was found to be almost completely inactive using calibrated automa

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Griffin, John H., Berislav V. Zlokovic, and Laurent O. Mosnier. "Activated protein C: biased for translation." Blood 125, no. 19 (2015): 2898–907. http://dx.doi.org/10.1182/blood-2015-02-355974.

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Abstract The homeostatic blood protease, activated protein C (APC), can function as (1) an antithrombotic on the basis of inactivation of clotting factors Va and VIIIa; (2) a cytoprotective on the basis of endothelial barrier stabilization and anti-inflammatory and antiapoptotic actions; and (3) a regenerative on the basis of stimulation of neurogenesis, angiogenesis, and wound healing. Pharmacologic therapies using recombinant human and murine APCs indicate that APC provides effective acute or chronic therapies for a strikingly diverse range of preclinical injury models. APC reduces the damag

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Yasuda, Kyota, Huaye Zhang, David Loiselle, Timothy Haystead, Ian G. Macara, and Stavroula Mili. "The RNA-binding protein Fus directs translation of localized mRNAs in APC-RNP granules." Journal of Cell Biology 203, no. 5 (2013): 737–46. http://dx.doi.org/10.1083/jcb.201306058.

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RNA localization pathways direct numerous mRNAs to distinct subcellular regions and affect many physiological processes. In one such pathway the tumor-suppressor protein adenomatous polyposis coli (APC) targets RNAs to cell protrusions, forming APC-containing ribonucleoprotein complexes (APC-RNPs). Here, we show that APC-RNPs associate with the RNA-binding protein Fus/TLS (fused in sarcoma/translocated in liposarcoma). Fus is not required for APC-RNP localization but is required for efficient translation of associated transcripts. Labeling of newly synthesized proteins revealed that Fus promot

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Maral, Meltem, and Arzum Erdem. "Carbon Nanofiber-Ionic Liquid Nanocomposite Modified Aptasensors Developed for Electrochemical Investigation of Interaction of Aptamer/Aptamer–Antisense Pair with Activated Protein C." Biosensors 13, no. 4 (2023): 458. http://dx.doi.org/10.3390/bios13040458.

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Selective and sensitive detection of human activated protein C (APC) was performed herein by using carbon nanofiber (CNF) and ionic liquid (IL) composite modified pencil graphite electrode (PGE) and electrochemical impedance spectroscopy (EIS) technique. A carbon nanomaterial-based electrochemical aptasensor was designed and implemented for the first time in this study for the solution-phase interaction of DNA-Apt with its cognate protein APC as well as APC inhibitor aptamer–antidote pair. The applicability of this assay developed for the determination of APC in fetal bovine serum (FBS) and it

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Burton, Janet L., and Mark J. Solomon. "Hsl1p, a Swe1p Inhibitor, Is Degraded via the Anaphase-Promoting Complex." Molecular and Cellular Biology 20, no. 13 (2000): 4614–25. http://dx.doi.org/10.1128/mcb.20.13.4614-4625.2000.

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ABSTRACT Ubiquitination and subsequent degradation of critical cell cycle regulators is a key mechanism exploited by the cell to ensure an irreversible progression of cell cycle events. The anaphase-promoting complex (APC) is a ubiquitin ligase that targets proteins for degradation by the 26S proteasome. Here we identify the Hsl1p protein kinase as an APC substrate that interacts with Cdc20p and Cdh1p, proteins that mediate APC ubiquitination of protein substrates. Hsl1p is absent in G1, accumulates as cells begin to bud, and disappears in late mitosis. Hsl1p is stabilized by mutations inCDH1

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Barth, Angela I. M., Kathleen A. Siemers, and W. James Nelson. "Dissecting interactions between EB1, microtubules and APC in cortical clusters at the plasma membrane." Journal of Cell Science 115, no. 8 (2002): 1583–90. http://dx.doi.org/10.1242/jcs.115.8.1583.

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End-binding protein (EB) 1 binds to the C-terminus of adenomatous polyposis coli (APC) protein and to the plus ends of microtubules (MT) and has been implicated in the regulation of APC accumulation in cortical clusters at the tip of extending membranes. We investigated which APC domains are involved in cluster localization and whether binding to EB1 or MTs is essential for APC cluster localization. Armadillo repeats of APC that lack EB1- and MT-binding domains are necessary and sufficient for APC localization in cortical clusters; an APC fragment lacking the armadillo repeats, but containing

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46

Okajima, Kenji, Shin Koga, Megumi Kaji, et al. "Effect of Protein C and Activated Protein C on Coagulation and Fibrinolysis in Normal Human Subjects." Thrombosis and Haemostasis 63, no. 01 (1990): 048–53. http://dx.doi.org/10.1055/s-0038-1645685.

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SummaryAlthough protein C (PC) and activated protein C (APC) have been postulated to be useful for treating patients with thrombosis, their critical effect remains to be studied in human subjects. To examine whether purified PC or APC are useful for treating patients with thrombosis without showing any adverse effect, wc studied effects on coagulation and fibrinolysis in normal human subjects.When highly purified human PC was administered intravenously to healthy subjects, plasma levels of immunoreactive PC decreased with a half-life of 10.9 h. Intravenously administered APC decreased with a h

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Lee, Yong-Seok, Sun-Lim Choi, Heejung Jun, et al. "AU-rich element-binding protein negatively regulates CCAAT enhancer-binding protein mRNA stability during long-term synaptic plasticity in Aplysia." Proceedings of the National Academy of Sciences 109, no. 38 (2012): 15520–25. http://dx.doi.org/10.1073/pnas.1116224109.

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The consolidation of long-term memory for sensitization and synaptic facilitation in Aplysia requires synthesis of new mRNA including the immediate early gene Aplysia CCAAT enhancer-binding protein (ApC/EBP). After the rapid induction of ApC/EBP expression in response to repeated treatments of 5-hydroxytryptamine (5-HT), ApC/EBP mRNA is temporarily expressed in sensory neurons of sensory-to-motor synapses. However, the molecular mechanism underlying the rapid degradation of ApC/EBP transcript is not known. Here, we cloned an AU-rich element (ARE)-binding protein, ApAUF1, which functions as a d

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Coburn, Jessica, M. Scott Wells, Nicholas B. D. Phelps, T. Gibson Gaylord, and Deborah A. Samac. "Acceptance of a Protein Concentrate from Alfalfa (Medicago sativa) by Yellow Perch (Perca flavescens) Fed a Formulated Diet." Fishes 6, no. 2 (2021): 9. http://dx.doi.org/10.3390/fishes6020009.

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The majority of plant proteins used in aquatic feeds are derived from seed meals, which may contain antinutritional factors. Protein concentrates from plant foliage have received less attention in fish feeding trials. Alfalfa protein concentrate (APC) is derived from fresh alfalfa foliage that contains approximately 52% protein and is low in fiber. A feeding trial was done to assess growth and feed efficiency responses of yellow perch (Perca flavescens) fed a formulated diet with 180 g/kg APC replacing all fishmeal compared to a control isonitrogenous diet with fishmeal. Yellow perch accepted

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D'Angelo, A., MS Lockhart, SV D'Angelo, and FB Jr Taylor. "Protein S is a cofactor for activated protein C neutralization of an inhibitor of plasminogen activation released from platelets." Blood 69, no. 1 (1987): 231–37. http://dx.doi.org/10.1182/blood.v69.1.231.231.

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Abstract Platelets stimulated with thrombin release an inhibitor of plasminogen activator (PAI), which has been shown previously to be neutralized by activated protein C (APC). The requirements for optimal neutralization of PAI activity were investigated. The releasate of gel-filtered human platelets stimulated with thrombin served as a source of PAI. When 6 X 10(8) platelets/mL were incubated with thrombin (1 IU/mL), the releasate contained 18 to 26 ng/mL PAI as determined by incubation of the releasate with urokinase and measurement of residual urokinase activity on plasminogen (S2251). Prei

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D'Angelo, A., MS Lockhart, SV D'Angelo, and FB Jr Taylor. "Protein S is a cofactor for activated protein C neutralization of an inhibitor of plasminogen activation released from platelets." Blood 69, no. 1 (1987): 231–37. http://dx.doi.org/10.1182/blood.v69.1.231.bloodjournal691231.

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Platelets stimulated with thrombin release an inhibitor of plasminogen activator (PAI), which has been shown previously to be neutralized by activated protein C (APC). The requirements for optimal neutralization of PAI activity were investigated. The releasate of gel-filtered human platelets stimulated with thrombin served as a source of PAI. When 6 X 10(8) platelets/mL were incubated with thrombin (1 IU/mL), the releasate contained 18 to 26 ng/mL PAI as determined by incubation of the releasate with urokinase and measurement of residual urokinase activity on plasminogen (S2251). Preincubation

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