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Rodney M. Camire, Ph.D.
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Professor of Pediatrics (Hematology)
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Member, The Children's Hospital of Philadelphia Research Institute
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Member, UPENN, Cardiovascular Institute
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Member, CHOP, Raymond G. Perelman Center for Cellular and Molecular Therapeutics
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Member, UPENN-CHOP, Blood Center for Patient Care and Discovery
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Associate Chief Scientific Strategy Officer, The Children's Hospital of Philadelphia Research Institute
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Department: Pediatrics
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Graduate Group Affiliations
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- Pharmacology e
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Contact information
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The Children's Hospital of Philadelphia
3a The Colket Translational Research Bldg., Room 5018
3f 3501 Civic Center Blvd.
Philadelphia, PA 19104-4399
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3a The Colket Translational Research Bldg., Room 5018
3f 3501 Civic Center Blvd.
Philadelphia, PA 19104-4399
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Office: 215-590-9968
32 Fax: 215-590-3660
32 Lab: 215-590-3873
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32 Fax: 215-590-3660
32 Lab: 215-590-3873
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Publications
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Links
98 Search PubMed for articles
85 The Children's Hospital of Philadelphia
99 The Children's Hospital of Philadelphia Research Institute
88 UPENN School of Medicine Site
95 Raymond G. Perelman Center for Cellular and Molecular Therapeutics
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98 Search PubMed for articles
85 The Children's Hospital of Philadelphia
99 The Children's Hospital of Philadelphia Research Institute
88 UPENN School of Medicine Site
95 Raymond G. Perelman Center for Cellular and Molecular Therapeutics
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Education:
21 9 B.A. 19 (Biochemistry) c
2d Saint Anselm College, 1994.
21 a Ph.D. 19 (Biochemistry) c
2e University of Vermont, 1998.
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Permanent link21 9 B.A. 19 (Biochemistry) c
2d Saint Anselm College, 1994.
21 a Ph.D. 19 (Biochemistry) c
2e University of Vermont, 1998.
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21 Description of Research:
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31a My laboratory is interested in understanding the components of the blood coagulation system, how they interface with activated cells, and how disturbances in their function lead to bleeding and thrombosis. We are also interested in developing therapeutic approaches (protein and gene-based) to mitigate these events which are major causes of morbidity and mortality worldwide. We are interested in questions related to the enzymology, biochemistry, and molecular genetics of enzyme complexes involved in blood coagulation. Numerous systems are employed to answer these questions including kinetic, biophysical, and structural approaches in addition to using in vivo models to make meaningful contributions to the field. The current areas of investigation in the laboratory include:
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15b 1. Molecular basis of procofactor activation: We are interested in understanding how FV and FVIII are preserved as inactive procofactors and defining their mechanism of activation. Our work has uncovered surprising and unexpected observations that have fundamentally shifted current thinking about FV activation and its regulation by TFPI.
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1fb 2. Structural correlates of protease function-basic and translational research: We seek to better understand how processing of inactive serine protease zymogens such as FX and FIX, to their active forms contributes to the expression of binding sites critical to their function. Knowledge from these biochemical studies has been applied to translational studies, some in collaboration with companies, to develop novel protein therapeutics to treat bleeding in hemophilia, trauma, or other conditions.
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11c 3. Imaging coagulation reactions in vivo. We have taken advantage of fluorescence approaches developed for physical studies of coagulation enzyme function to develop enabling technologies that permit quantitative measurements of enzyme complex assembly and function in vivo.
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12e 4. Employ gene therapy strategies for hemophilia A/B by employing novel modifications to the protein cofactor, factor VIII or zymogen FIX. Using different bioengineering strategies we are interested in modifying FVIII or FIX with unique properties that could be useful in a gene-based approach.
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a5 Keywords: serine proteinase, recombinant protein expression, blood coagulation, macromolecular enzyme complex, hemophilia, translational research, thrombosis.
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Description of Research Expertise
99 We study the molecular basis of blood coagulation to better understand disorders of hemostasis and develop new therapeutic approaches.8
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21 Description of Research:
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31a My laboratory is interested in understanding the components of the blood coagulation system, how they interface with activated cells, and how disturbances in their function lead to bleeding and thrombosis. We are also interested in developing therapeutic approaches (protein and gene-based) to mitigate these events which are major causes of morbidity and mortality worldwide. We are interested in questions related to the enzymology, biochemistry, and molecular genetics of enzyme complexes involved in blood coagulation. Numerous systems are employed to answer these questions including kinetic, biophysical, and structural approaches in addition to using in vivo models to make meaningful contributions to the field. The current areas of investigation in the laboratory include:
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15b 1. Molecular basis of procofactor activation: We are interested in understanding how FV and FVIII are preserved as inactive procofactors and defining their mechanism of activation. Our work has uncovered surprising and unexpected observations that have fundamentally shifted current thinking about FV activation and its regulation by TFPI.
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1fb 2. Structural correlates of protease function-basic and translational research: We seek to better understand how processing of inactive serine protease zymogens such as FX and FIX, to their active forms contributes to the expression of binding sites critical to their function. Knowledge from these biochemical studies has been applied to translational studies, some in collaboration with companies, to develop novel protein therapeutics to treat bleeding in hemophilia, trauma, or other conditions.
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11c 3. Imaging coagulation reactions in vivo. We have taken advantage of fluorescence approaches developed for physical studies of coagulation enzyme function to develop enabling technologies that permit quantitative measurements of enzyme complex assembly and function in vivo.
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12e 4. Employ gene therapy strategies for hemophilia A/B by employing novel modifications to the protein cofactor, factor VIII or zymogen FIX. Using different bioengineering strategies we are interested in modifying FVIII or FIX with unique properties that could be useful in a gene-based approach.
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a5 Keywords: serine proteinase, recombinant protein expression, blood coagulation, macromolecular enzyme complex, hemophilia, translational research, thrombosis.
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ef Gupta S, Bunce MW, Cid EA, Camire RM, Shapiro AD.: Acquired factor V inhibitor in a case of pediatric venous thrombosis. Res Pract Thromb Haemost 9: 102646, Nov 2024.
151 Poncz M, Zaitsev SV, Ahn H, Kowalska MA, Bdeir K, Dergilev KV, Ivanciu L, Camire RM, Cines DB, Stepanova V.: Packaging of supplemented urokinase into alpha granules of in vitro-grown megakaryocytes for targeted nascent clot lysis. Blood Adv 8: 3798-3809, Jul 2024.
164 Wurtzel JGT, Lazar S, Askari S, Zhao X, Severa JR, Ayombil F, Michael JV, Camire RM, McKenzie SE, Stalker TJ, Ma P, Goldfinger LE.: Plasma growth factors maintain constitutive translation in platelets to regulate reactivity and thrombotic potential. Blood Adv 8: 1550-1566, Jan 2024.
12a Cao W, Trask AR, Bignotti AI, George LA, Doshi BS, Sabatino DE, Yada N, Zheng L, Camire RM, Zheng XL.: Coagulation factor VIII regulates von Willebrand factor homeostasis in vivo. J Thromb Haemost 21(12): 3477-3489, Dec 2023.
1e9 Kaczmarek R, Piñeros AR, Patterson PE, Bertolini TB, Perrin GQ, Sherman A, Born J, Arisa S, Arvin MC, Kamocka MM, Martinez MM, Dunn KW, Quinn SM, Morris JJ, Wilhelm AR, Kaisho T, Munoz-Melero M, Biswas M, Kaplan MH, Linnemann AK, George LA, Camire RM, Herzog RW.: Factor VIII trafficking to CD4+ T cells shapes its immunogenicity and requires several types of antigen-presenting cells. Blood 142: 290-305, Jul 2023.
dd Ivanciu L, Arruda VR, Camire RM.: Factor IXa variants resistant to plasma inhibitors enhance clot formation in vivo. Blood 141: 2022-2032, Feb 2023.
10f Ayombil F, Petrillo T, Kim H, Camire RM.: Regulation of factor V by the anticoagulant protease activated protein C: Influence of the B-domain and TFPIα J Biol Chem 298(11): 102558-102568, Sep 2022.
169 Maag A, van Rein N, Schuijt TJ, Kopatz WF, Kruijswijk D, Thomassen S, Hackeng TM, Camire RM, van der Poll T, Meijers JCM, Bos MHA, van 't Veer C.: Major bleeding during oral anticoagulant therapy associated with factor V activation by factor Xa. J Thromb Haemost 20(2): 328-338, Feb 2022.
13a Milstone LM, Jackson C, Becker RC, Camire R, Knabb R, Mann K, Ruf W, Wexler RR, Wood J.: Discussion of talks from the symposium: Factor X: From thrombokinase to oral anti-coagulants and beyond. J Thromb Thrombolysis 52(2): 408-413, Oct 2021.
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Selected Publications
139 Ayombil F, Toso R, Camire RM.: Basic regions of factor V and tissue factor pathway inhibitor mediate heavy chain and acidic region interactions on factor V revealed by tethered chemical cleavage. J Thromb Haemost 23(8): 2449-2460, Aug 2025.ef Gupta S, Bunce MW, Cid EA, Camire RM, Shapiro AD.: Acquired factor V inhibitor in a case of pediatric venous thrombosis. Res Pract Thromb Haemost 9: 102646, Nov 2024.
151 Poncz M, Zaitsev SV, Ahn H, Kowalska MA, Bdeir K, Dergilev KV, Ivanciu L, Camire RM, Cines DB, Stepanova V.: Packaging of supplemented urokinase into alpha granules of in vitro-grown megakaryocytes for targeted nascent clot lysis. Blood Adv 8: 3798-3809, Jul 2024.
164 Wurtzel JGT, Lazar S, Askari S, Zhao X, Severa JR, Ayombil F, Michael JV, Camire RM, McKenzie SE, Stalker TJ, Ma P, Goldfinger LE.: Plasma growth factors maintain constitutive translation in platelets to regulate reactivity and thrombotic potential. Blood Adv 8: 1550-1566, Jan 2024.
12a Cao W, Trask AR, Bignotti AI, George LA, Doshi BS, Sabatino DE, Yada N, Zheng L, Camire RM, Zheng XL.: Coagulation factor VIII regulates von Willebrand factor homeostasis in vivo. J Thromb Haemost 21(12): 3477-3489, Dec 2023.
1e9 Kaczmarek R, Piñeros AR, Patterson PE, Bertolini TB, Perrin GQ, Sherman A, Born J, Arisa S, Arvin MC, Kamocka MM, Martinez MM, Dunn KW, Quinn SM, Morris JJ, Wilhelm AR, Kaisho T, Munoz-Melero M, Biswas M, Kaplan MH, Linnemann AK, George LA, Camire RM, Herzog RW.: Factor VIII trafficking to CD4+ T cells shapes its immunogenicity and requires several types of antigen-presenting cells. Blood 142: 290-305, Jul 2023.
dd Ivanciu L, Arruda VR, Camire RM.: Factor IXa variants resistant to plasma inhibitors enhance clot formation in vivo. Blood 141: 2022-2032, Feb 2023.
10f Ayombil F, Petrillo T, Kim H, Camire RM.: Regulation of factor V by the anticoagulant protease activated protein C: Influence of the B-domain and TFPIα J Biol Chem 298(11): 102558-102568, Sep 2022.
169 Maag A, van Rein N, Schuijt TJ, Kopatz WF, Kruijswijk D, Thomassen S, Hackeng TM, Camire RM, van der Poll T, Meijers JCM, Bos MHA, van 't Veer C.: Major bleeding during oral anticoagulant therapy associated with factor V activation by factor Xa. J Thromb Haemost 20(2): 328-338, Feb 2022.
13a Milstone LM, Jackson C, Becker RC, Camire R, Knabb R, Mann K, Ruf W, Wexler RR, Wood J.: Discussion of talks from the symposium: Factor X: From thrombokinase to oral anti-coagulants and beyond. J Thromb Thrombolysis 52(2): 408-413, Oct 2021.
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