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Relevant bibliographies by topics / Apc protein

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Academic literature on the topic 'Apc protein'

Author: Grafiati

Published: 10 March 2023

Last updated: 31 July 2025

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Journal articles on the topic "Apc protein"

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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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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Dissertations / Theses on the topic "Apc protein"

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Tickenbrock, Lara. "Das Tumorsuppressor-Protein APC strukturelle und biochemische Aspekte /." [S.l.] : [s.n.], 2002. http://deposit.ddb.de/cgi-bin/dokserv?idn=966017064.

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Hankey, William C. IV. "Chromatin-associated functions of the APC tumor suppressor protein." The Ohio State University, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=osu1480198247672881.

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Cuddihy, Jane. "The non-Wnt functions of APC : unravelling the link between APC and apoptosis." Thesis, University of Dundee, 2016. https://discovery.dundee.ac.uk/en/studentTheses/bfb0d6ce-149b-4152-a591-943d61e2c714.

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Colorectal cancer (CRC) is the second most common cause of cancer-related death in the UK and Western world. More than 90% of sporadic CRCs harbour mutations in the multi-functional tumour suppressor gene Adenomatous polyposis coli (<i>Apc</i>). The most commonly studied function of APC is its role as a scaffold for the β-catenin destruction complex involved in Wnt signalling. However, APC binds many other proteins. For example, it directly binds to and stabilises microtubules and actin. These non-Wnt related functions of APC are poorly understood. My PhD examines non-Wnt functions of APC. To

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Vijaya, Chandra Shree Harsha [Verfasser], and Jürgen [Akademischer Betreuer] Behrens. "Functional analysis of truncated APC protein in human colorectal cancers = Funktionelle Analyse von verkürztem APC Protein in humanem kolorektalen Krebs / Shree Harsha Vijaya Chandra. Betreuer: Jürgen Behrens." Erlangen : Universitätsbibliothek der Universität Erlangen-Nürnberg, 2011. http://d-nb.info/1015474802/34.

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Yu, Yao. "Endothelial cell signalling of APC and thrombin : the involvement of protein kinase C." Thesis, Imperial College London, 2013. http://hdl.handle.net/10044/1/18048.

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Activated protein C (APC) is a natural anticoagulant. In addition to this well-described function, APC also mediates endothelial cell (EC) cytoprotection, including anti-apoptotic, anti-inflammatory and endothelial barrier integrity stabilising effects. APC confers these effects through proteolytic activation of protease activated receptor 1 (PAR1), but only when it is bound to its receptor, endothelial protein C receptor (EPCR). Interestingly, thrombin exerts opposing cellular responses (including induction of endothelial hyperpermeability) through activation of PAR1. How activation of the sa

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Shen, Ying. "Regulation of EphA4 expression through the APC-mediated ubiquitin-proteasome pathway /." View abstract or full-text, 2007. http://library.ust.hk/cgi/db/thesis.pl?BICH%202007%20SHEN.

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Mills, Kate May. "A novel role for Adenomatous Polyposis Coli protein in the transport of mitochondria." Thesis, The University of Sydney, 2015. http://hdl.handle.net/2123/14184.

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Adenomatous Polyposis Coli (APC) is a multifunctional tumour suppressor protein, contributing to pathways in normal cell growth and differentiation. APC gene mutation is one of the earliest events in the progression of colorectal cancer (CRC), and typically gives rise to a truncated protein lacking C-terminal sequences, initiating deregulation of key cellular pathways. This thesis describes a new role for APC in mitochondrial transport. Silencing of wild-type APC by siRNA induced a redistribution of mitochondria from the cell periphery to the perinuclear region. Subsequently, novel interaction

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Dieckhoff, Patrick. "Protein modification and degradation in the cell cycle of the yeast Saccharomyces cerevisiae." Doctoral thesis, [S.l. : s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=972638644.

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Quyn, Aaron J. "The role of the APC protein in mitotic spindle orientation and tissue organisation in gut epithelium." Thesis, University of Dundee, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.505629.

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Zimmermann, Julia Janina [Verfasser]. "Untersuchung des Einflusses verschiedender Liganden auf die Inaktivierungskinetik von aktiviertem Protein C (APC) / Julia Janina Zimmermann." Bonn : Universitäts- und Landesbibliothek Bonn, 2015. http://d-nb.info/1080591761/34.

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Books on the topic "Apc protein"

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Näthke, Inke S. APC proteins. Springer Science+Business Media, 2009.

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S, Näthke Inke, and McCartney Brooke M, eds. APC proteins. Springer Science+Business Media, 2009.

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S, Näthke Inke, and McCartney Brooke M, eds. APC proteins. Springer Science+Business Media, 2009.

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Inuzuka, Hiroyuki. SCF and APC E3 ubiquitin ligases in tumorigenesis. Springer, 2014.

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Näthke, Inke S., and Brooke M. McCartney, eds. APC Proteins. Springer New York, 2009. http://dx.doi.org/10.1007/978-1-4419-1145-2.

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S, Näthke Inke, and McCartney Brooke M, eds. APC proteins. Springer Science+Business Media, 2009.

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Scott, Deborah. Determination of the effect of activated protein C (APC) upon the anticoagulant activity of various forms of heparin as determined in-vitro in normal human plasma. The Author], 2003.

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B, Holland I., ed. ABC proteins: From bacteria to man. Academic Press, 2003.

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Ahcène, Boumendjel, Boutonnat Jean, and Robert Jacques M. D, eds. ABC transporters and multidrug resistance. John Wiley & Sons, 2009.

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Nowakowski, Dan Wlodzimierz. Novel Activities of Adenomatous Polyposis Coli (APC) Protein and Type III Neuregulin 1 in the Developing Nervous System. 2010.

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Book chapters on the topic "Apc protein"

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Tripodi, A. "Activated protein C (APC) resistance." In Laboratory Techniques in Thrombosis - a Manual. Springer Netherlands, 1999. http://dx.doi.org/10.1007/978-94-011-4722-4_17.

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Kent, Amy, Karin Leiderman, Anna C. Nelson, et al. "Studying the Effects of Oral Contraceptives on Coagulation Using a Mathematical Modeling Approach." In Mathematical Modeling for Women’s Health. Springer Nature Switzerland, 2024. http://dx.doi.org/10.1007/978-3-031-58516-6_4.

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AbstractThe use of oral contraceptives (OCs) is known to increase the risk of thrombosis, but the mechanisms underlying this risk and the determinants of the tests that assess this risk are not fully understood. In this study, we used a mathematical model to study the effects of an OC containing levonorgestrel (lev) on blood clotting. Lev is reported to change the plasma levels of blood clotting factors. The mathematical model used in this study simulates coagulation reactions in a small injury under flow, takes clotting factors as inputs, and outputs time courses of the coagulation enzyme thr

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Prasad, Ramesh, Abhishek Roy, and Prosenjit Sen. "Functional Aspects of Activated Protein C (APC) in Regulating Homeostasis and Disease." In Proteases in Human Diseases. Springer Singapore, 2017. http://dx.doi.org/10.1007/978-981-10-3162-5_18.

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Hoffmann, J. N., M. W. Laschke, B. Vollmar, et al. "Aktiviertes Protein C (APC) bei der Sepsis: Zelluläre und mikrohämodynamische Mechanismen der Protektion." In Zurück in die Zukunft. Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-642-55611-1_378.

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Hoffmann, Johannes N., B. Vollmar, M. W. Laschke, D. Inthorn, F. W. Schildberg, and M. D. Menger. "Aktiviertes Protein C (APC) bei der Sepsis: Zelluläre und mikrohämodynamische Mechanismen der Protektion." In Deutsche Gesellschaft für Chirurgie. Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-642-19024-7_90.

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Brocardo, Mariana, and Beric R. Henderson. "Detection of Cytoplasmic and Nuclear Localization of Adenomatous Polyposis Coli (APC) Protein in Cells." In Methods in Molecular Biology. Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-249-6_6.

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Uttenreuther-Fischer, M. M., B. Vetter, C. Hellmann, et al. "Thromboembolien im Kindesalter: Einflüsse nichtgenetischer Faktoren und die Rolle der Resistenz gegen aktiviertes Protein C (APC-R) und des Protein-C-Mangels." In 28. Hämophilie-Symposion Hamburg 1997. Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-59915-6_16.

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Gradehandt, Gernot, Johannes Hampl, Nadja Kleber, et al. "Requirements of Exogenous Protein Antigens for Presentation to CD4+ T lymphocytes By MHC Class II-Positive APC." In Advances in Experimental Medicine and Biology. Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-2930-9_4.

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Catimel, Bruno, John D. Wade, M. Faux, Anthony Burgess, Laszlo Otvos, and Edouard Nice. "The Use of a Synthetic Biotinylated Peptide Probe for the Isolation of Adenomatous Polyposis Coli (APC) Tumor Suppressor Protein Complexes." In Peptides: The Wave of the Future. Springer Netherlands, 2001. http://dx.doi.org/10.1007/978-94-010-0464-0_466.

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Bachmaier, Sabine, and Michael Boshart. "Kinetoplastid AGC Kinases." In Protein Phosphorylation in Parasites. Wiley-VCH Verlag GmbH & Co. KGaA, 2013. http://dx.doi.org/10.1002/9783527675401.ch05.

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Conference papers on the topic "Apc protein"

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Nagpal, Satchit, and Joseph Sang-II Kwon. "Enhancing Protein Crystal Purity through Adaptive Kinetic Monte Carlo Modeling and Control of Surface Morphology." In 2024 American Control Conference (ACC). IEEE, 2024. http://dx.doi.org/10.23919/acc60939.2024.10644312.

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B, Anup Bhat, Tanish Sunilkumar, and Ayush Prabhu. "Mining sequential patterns from protein sequences associated with aggregation diseases." In 2024 IEEE 3rd World Conference on Applied Intelligence and Computing (AIC). IEEE, 2024. http://dx.doi.org/10.1109/aic61668.2024.10730824.

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de Four, N. J., R. M. Bertina, and F. Havgrkate. "STIMULATION OF FIBRINOLYSIS BY ACTIVATED PROTEIN C (APC)." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642961.

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In 1960 Mammen and Seegers reported the discovery of a new protein (autoprothrombin II-A, APC) with both anticoagulant and profibrinolytic activity. They found that APC accelerated clot lysis in vitro and proposed that this was due to a reduction of plasmin - inhibitory activity. Many years later Comp et al (J Clin Inv 68: 1221) reported that the infusion of APC into dogs resulted in an increase in circulating plasminogen activator activity. This observation stimulated more extensive studies of the profibrinolytic effects of APC.In our laboratories we have studied the effect of human APC on cl

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Heeb, M. J., F. Espana, M. Geiger, D. Collen, D. C. Stump, and J. H. Griffin. "IMMUNOLOGICAL SIMILARITIES BETWEEN PLASMA AND URINARY PROTEIN C INHIBITORS (PCIs) AND URINARY UROKINASE INHIBITOR (UKI)." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643816.

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Plasma PCIs have similar MW (∼ 57K), amino acid composition, and heparin dependence (Suzuki et al 1983, JBC 258:163) as urinary UKI (Stump et al 1986, JBC 261:12759). Urinary PCI of ∼ 50K MW has a similar heparin dependence and urokinase (UK) competes with activated protein C (APC) for this PCI (Geiger et al 1986, Circ. 74:11-234). For comparison, three forms of PCI, one from urine and two from plasma, were purified, and each exhibited heparin-dependent UK and APC inhibitory activity and formed heparin-dependent complexes with APC. The APC-PCI complexes were visible on immunoblots (nondenaturi

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van der Meer, F. J. M., N. H. van Tilburg, I. K. van der Linden, E. Briét, and R. M. Bertina. "A SECOND INHIBITOR OF ACTIVATED PROTEIN C (APC)." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643817.

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The inactivation of APC in plasma, as measured with the chromogenic substrate S2366, follows, in the absence of heparin, pseudo-first order kinetics. The ti of about 20 minutes is independent of the APC concentration (31-500 nM) and increases linearly with the dilution of the plasma. These observations suggest that the concentration of the APC inhibitor in plasma is much higher than 500 nM, which is much higher than the concentration of 88 nM reported by Suzuki for the protein C inhibitor (PCI).In the presence of heparin (5 IU/ml) the inactivation of APC becomes biphasic. Fast inactivation wit

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Joost, S., A. Koedam, Joost C. M. Meijers, Jan J. Sixma, and Bonno N. Bouma. "VON WILLEBRAND FACTOR PROTECTS FACTOR VIII FROM INACTIVATION BY ACTIVATED PROTEIN C AND PROTEIN S." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643618.

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Activated protein C (APC) inactivated the cofactors factor V (FV) and factor VIII (FVIII). In the case of FV, this reaction and the respective roles of Ca2+ , phospholipids and protein S have been well documented. We investigated the role of protein S and von Willebrand factor (VWF) on the inactivation of FVIII.Purified human factor VIII (3 units/ml) was incubated with protein C (0.2 μg/ml) in the presence of 8 μg/ml phospholipid, 5 mM CaCl, and 1 unit/ml hirudin. Factor VIII coagulant activity decreased with a pseudo first-order rate constant of 0.09 min . The reaction rate increased linearly

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Hessing, Martin, Joost C. M. Meijers, Jan A. van Mourik, and Bonno N. Bouma. "MONOCLONAL ANTIBODIES TO HUMAN PROTEIN S AND C4b-BINDING PROTEIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644291.

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Protein S (PS) circulates in plasma both free and in reversible association with the complement component C4b-binding protein (C4bp). Only free PS is functional as a cofactor for activated protein C (APC). Cleavage of PS by thrombin at a site near the r-carboxyglutamic acid domain is associated with a loss of cofactor activity. This may be a control mechanism for the anticoagulant activity of APC. These observations led us to investigate the role of C4bp and thrombin in the regulation of PS. Complex formation between purified PS and C4bp was studied in plasma and in a system with purified comp

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Dahiback, Bjorn, Ake Lundwall, Andreas Hillarp, Johan Malm, and Johan Stenflo. "STRUCTURE AND FUNCTION OF VITAMIN K-DEPENDENT PROTEIN S, a cofactor to activated protein C which also interacts with the complement protein C4b-binding protein." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642960.

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Protein S is a single chain (Mr 75.000) plasma protein. It is a cofactor to activated protein C (APC) in the regulation of coagulation factors Va and Villa. It has high affinity for negatively charged phospolipids and it forms a 1:1 complex with APC on phospholipid surfaces, platelets and on endothelial cells. Patients with heterozygous protein S deficiency have a high incidence of thrombosis. Protein S is cleaved by thrombin, which leads to a loss of calcium binding sites and of APC cofactor activity. Protein S has two to three high affinity (KD 20uM) calcium binding sites - unrelated to the

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Schwarz, H. P., and W. Muntean. "LOW TOTAL PROTEIN S ANTIGEN BUT HIGH PROTEIN S ACTIVITY DUE TO DECREASED C4b-BINDING PROTEIN (C4b-BP) LEVELS IN NEWBORNS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643610.

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Vitamin K-dependent coagulation proteins are known to be decreased in the neonatal period. So far no data have been published on protein S (PS), the vitamin K-dependent cofactor for the antithrombotic enzyme, activated protein C (APC) in this period. We determined, therefore, PS antigen, PS activity and C4b-BP,a regulatory protein of the classical complement pathway to which PS is complexed, in 36 neonates. Total PS antigen in newborns was below the range associated with thromboembolism in patients congenitally deficient in this protein (22±9.6%, mean±SD). None of these infants had clinical or

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Suzuki, Koji, Yoshihiro Deyashiki, Junji Nishioka, Kazunori Toma, and Shuji Yamamoto. "THE INHIBITOR OF ACTIVATED PROTEIN C: STRUCTURE AND FUNCTION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642963.

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In the final step of protein C pathway, activated protein C (APC) is neutralized with a plasma inhibitor, termed protein C inhibitor (PCI). PCI was first described by Marlar and Griffin (1980) and then isolated from human plasma as a homogeneous form and characterized by the authors (1983). PCI is a single chain glycoprotein with M 57,000 and a plasma concentration of 5 ug/ml. Analysis of a cDNA nucleotide sequence has clarified that a precursor of human PCI consists of a mature protein of 387 amino acid residues (M 43,759) and a signal peptide of 19 amino acid residues. Only one cysteine resi

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Reports on the topic "Apc protein"

1

Ray, Ranjan. The Regulation of the Angiogenic Factor FGF-Binding Protein (FGF-BP) by the APC/beta-Catenin Signaling Pathway in the Progression of Breast Cancer. Defense Technical Information Center, 2002. http://dx.doi.org/10.21236/ada406733.

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Stylianou, Dora, and Anna T. Riegel. The Regulation of the Angiogenic Factor FGF Binding Protein (FGF-BP) by the APC/Beta-Catenin Signaling Pathway in the Progression of Breast Cancer. Defense Technical Information Center, 2003. http://dx.doi.org/10.21236/ada423021.

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Stylianou, Dora C. The Regulation of the Angiogenic Factor FGF Binding Protein (FGF-BP) by the APC/Beta-Catenin Signaling Pathway in the Progression of Breast Cancer. Defense Technical Information Center, 2004. http://dx.doi.org/10.21236/ada425854.

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4

Bercovier, Herve, Raul Barletta, and Shlomo Sela. Characterization and Immunogenicity of Mycobacterium paratuberculosis Secreted and Cellular Proteins. United States Department of Agriculture, 1996. http://dx.doi.org/10.32747/1996.7573078.bard.

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Our long-term goal is to develop an efficient acellular vaccine against paratuberculosis based on protein antigen(s). A prerequisite to achieve this goal is to analyze and characterize Mycobacterium paratuberculosis (Mpt) secreted and cellular proteins eliciting a protective immune response. In the context of this general objective, we proposed to identify, clone, produce, and characterize: the Mpt 85B antigen and other Mpt immunoreactive secreted proteins, the Mpt L7/L12 ribosomal protein and other immunoreactive cellular proteins, Mpt protein determinants involved in invasion of epithelial c

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Yedidia, I., H. Senderowitz, and A. O. Charkowski. Small molecule cocktails designed to impair virulence targets in soft rot Erwinias. United States-Israel Binational Agricultural Research and Development Fund, 2020. http://dx.doi.org/10.32747/2020.8134165.bard.

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Chemical signaling between beneficial or pathogenic bacteria and plants is a central factor in determining the outcome of plant-microbe interactions. Pectobacterium and Dickeya (soft rot Erwinias) are the major cause of soft rot, stem rot, and blackleg formed on potato and ornamentals, currently with no effective control. Our major aim was to establish and study specific bacterial genes/proteins as targets for anti-virulence compounds, by combining drug design tools and bioinformatics with experimental work. The approach allowed us to identify and test compounds (small molecules) that specific

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Lekostaj, Jacqueline K. The Role of ABC Proteins in Drug Resistant Breast Cancer Cells. Defense Technical Information Center, 2008. http://dx.doi.org/10.21236/ada485613.

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Pleeter, Perri, and Jacqueline K. Lekostaj. The Role of ABC Proteins in Drug Resistant Breast Cancer Cells. Defense Technical Information Center, 2009. http://dx.doi.org/10.21236/ada504701.

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Lekostaj, Jacqueline K. The Role of ABC Proteins in Drug-Resistant Breast Cancer Cells. Defense Technical Information Center, 2007. http://dx.doi.org/10.21236/ada470298.

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Reichel, Ina, Michael Zisman, and Massimo Placidi. Aperture studies for the AP2 anti-proton Line at Fermilab. Office of Scientific and Technical Information (OSTI), 2003. http://dx.doi.org/10.2172/821765.

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Reichel, Ina, Michael Zisman, and Massimo Placidi. Aperture Studies for the AP2 Anti-Proton Line at Fermilab. Office of Scientific and Technical Information (OSTI), 2003. http://dx.doi.org/10.2172/1967371.

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