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Charles S. Abrams, M.D.
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Francis C. Wood Professor
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Department: Medicine
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Graduate Group Affiliations
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Contact information
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Perelman Center for Advanced Medicine
48 South Pavilion, 6th Floor, Room 6-622
Philadelphia, PA 19104
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48 South Pavilion, 6th Floor, Room 6-622
Philadelphia, PA 19104
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Office: (215) 898-1058
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Email:
abrams@upenn.edu
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abrams@upenn.edu
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Publications
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Education:
21 b B.E.S. 1b (Bioengineering) c
35 The Johns Hopkins University, 1980.
21 9 M.D. 15 (Medicine) c
3b Yale University School of Medicine, 1984.
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21 b B.E.S. 1b (Bioengineering) c
35 The Johns Hopkins University, 1980.
21 9 M.D. 15 (Medicine) c
3b Yale University School of Medicine, 1984.
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Links
99 Search PubMed for articles
46 Cell and Molecular Biology graduate group faculty webpage.
57 Biochemistry & Molecular Biophysics graduate group faculty webpage.
7c Hematology / Oncology Faculty
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Permanent link99 Search PubMed for articles
46 Cell and Molecular Biology graduate group faculty webpage.
57 Biochemistry & Molecular Biophysics graduate group faculty webpage.
7c Hematology / Oncology Faculty
c
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38 Phospholipid signaling in platelet and T-cells.
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3f Key words: Pleckstrin, PH domains, cytoskeleton.
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26 Description of Research
8
596 Inappropriate platelet activation contributes to vascular diseases including stroke and myocardial ischemia. Our laboratory is focused on phospholipid signaling in platelets and its contribution to inappropriate platelet activation. Ongoing projects are directed at understanding the roles of pleckstrin and lipid kinases in platelets. Pleckstrin (p47) was once solely known as an early marker of platelet activation; more recently it has been noted to contain the prototypic Pleckstrin Homology motif. Over the past half dozen years, work derived from our laboratory has demonstrated that pleckstrin plays a dominant role in the reorganization of the platelet, and lymphocyte, cytoskeleton. Furthermore, our laboratory has established these effects are regulated by pleckstrin phosphorylation, require critical lipid-binding residues contained with the amino-terminal Pleckstrin Homology domain, and have implicated an effector for this process to be the small GTP-binding protein, Rac. Additional work from our laboratory has helped define the role of phospholipid kinases in the pathway that is initiated by G-protein coupled receptors and ultimately leads to actin reorganization. Our studies use molecular and cellular biologic techniques to examine blood cell biology, and involve expression mutagenesis, single cell microinjection, genetic library screening, and murine homologous gene targeting ("gene knock-out").
8
20 Rotation projects
8
27 pleckstrin2 and actin assembly
25 PIP5K Ig and focal adhesions
8
1e Lab personnel:
2b Andrew Louden - Postdoctoral Fellow
27 Feng Wang - Postdoctoral Fellow
2a Seun-Ah Yang - Postdoctoral Fellow
27 Tami Bach - Postdoctoral Fellow
1f Michael Hu - Technician
20 Lurong Lian - Technician
28 Qing Chen - Undergraduate Student
26 29
27
Description of Research Expertise
2b Research Interests8
38 Phospholipid signaling in platelet and T-cells.
8
3f Key words: Pleckstrin, PH domains, cytoskeleton.
8
26 Description of Research
8
596 Inappropriate platelet activation contributes to vascular diseases including stroke and myocardial ischemia. Our laboratory is focused on phospholipid signaling in platelets and its contribution to inappropriate platelet activation. Ongoing projects are directed at understanding the roles of pleckstrin and lipid kinases in platelets. Pleckstrin (p47) was once solely known as an early marker of platelet activation; more recently it has been noted to contain the prototypic Pleckstrin Homology motif. Over the past half dozen years, work derived from our laboratory has demonstrated that pleckstrin plays a dominant role in the reorganization of the platelet, and lymphocyte, cytoskeleton. Furthermore, our laboratory has established these effects are regulated by pleckstrin phosphorylation, require critical lipid-binding residues contained with the amino-terminal Pleckstrin Homology domain, and have implicated an effector for this process to be the small GTP-binding protein, Rac. Additional work from our laboratory has helped define the role of phospholipid kinases in the pathway that is initiated by G-protein coupled receptors and ultimately leads to actin reorganization. Our studies use molecular and cellular biologic techniques to examine blood cell biology, and involve expression mutagenesis, single cell microinjection, genetic library screening, and murine homologous gene targeting ("gene knock-out").
8
20 Rotation projects
8
27 pleckstrin2 and actin assembly
25 PIP5K Ig and focal adhesions
8
1e Lab personnel:
2b Andrew Louden - Postdoctoral Fellow
27 Feng Wang - Postdoctoral Fellow
2a Seun-Ah Yang - Postdoctoral Fellow
27 Tami Bach - Postdoctoral Fellow
1f Michael Hu - Technician
20 Lurong Lian - Technician
28 Qing Chen - Undergraduate Student
26 29
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14f Trivedi, C.M., Luo, Y., Yin, Z., Zhang, M., Floss, T., Goettlicher, M., Ruiz, P., Wurst, W., Ferrari, V., Abrams, C.S., Gruber, P., Epstein, J.A.: HDAC2 regulates the cardiac hypertrophic response by modulating GSK3β activity. Nature Medicine 13: 324-331, 2007.
178 Wang, Y., Chen, X., Lian, L., Tang, T., Stalker, T.J., Sasaki, T., Brass, L.F., Choi, J.K., Hartwig, J.H., Abrams, C.S.: Loss of PIP5KIβ demonstrates that rapid PIP2 synthesis is required for IP3 formation. Proceedings of the National Academy of Science (U.S.A.) 105: 14064-14069, 2008 Notes: Track II.
15e Pan, W., Choi, S.-C., Wang, H., Qin, Y., Volpicelli-Daley, L., Swan, L., Lucast, L., Khooo, C., Zhang, X., Li, L., Abrams, C.S., Sokol, S.Y., Wu, D.: Wnt3a-mediated formation of phosphatidylinositol 4,5-bisphosphate regulates LRP6 phosphorylation. Science 321: 1350-1353, 2008.
16d Wang, Y., Litvinov, R.I., Chen, X., Lian, L., Bach, T.L., Petrich, B., Monkley, S., Critchley, D., Birnbaum, M.J., Weisel, J.W., Hartwig, J.H., Abrams, C.S.: Loss of PIP5Kγ, but not PIP5Kβ, impairs the integrity of the membrane cytoskeleton. J. Clinical Investigation 118(2): 812-819, 2008.
18e Mao, Y.S., Yamaga, M., Zhu, X., Wei, M., Sun, H.-Q., Wang, J., Yun, M., Wang, Y., Di Paolo, G., Bennett, M., Mellman, I.S., Abrams, C.S., De Camilli, P.V., Lu, C.Y., and Yin, H.L.: Essential and unique roles of PIP5Kγ and α in Fcγ receptor-mediated phagocytosis J. Cell Biology Journal of Cell Biology 184: 281-296, 2009.
101 Lian, L., Wang, W., Flick, M., Choi, J., Scott, E., Degen, J., Lemmon, M.A., Abrams, C.S.: Loss of pleckstrin defines a novel pathway for PKC-mediated exocytosis. Blood In press, 2009.
c1 Min, S.H., Abrams, C.S.: Why do phosphatidylinositol kinases have so many isoforms? Biochemical J 423(1): 99-108, 2009.
173 Volpicelli-Daley, L.A., Lucast, L., Gong, L.-W., Liu, L., Sasaki, J., Sasaki, T., Abrams, C.S., Kanaho, Y., De Camilli, P.: Phosphatidylinositol 4-phosphate 5-kinases (PIPKIs) and phosphatidylinositol 4,5 bisphosphate [PI(4,5)P2] synthesis in the brain. J. Biologic Chemistry Page: 28708-14, 2010.
142 Mitsios, J.V., Prévost, N., Kasirer-Friede, A., Gutierrez, E., Groisman, A., Abrams, C.S., Litvinov, R.I., Zemljic-Harpf, A., Ross, R.S., Shattil, S., J.: What is vinculin needed for in platelets? J. Thrombosis & Haemostasis Page: 2294-2304, 2010.
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Selected Publications
13e Wang, Y., Chen, X., Lian, L., Bach, T.L., Golden, J., Morrisey, E.M., Abrams, C.S.: PIP5Kγ is required for cardiovascular and neuronal development. Proceedings of the National Academy of Science (U.S.A.) 104(28): 11748-53, 2007 Notes: Track II.14f Trivedi, C.M., Luo, Y., Yin, Z., Zhang, M., Floss, T., Goettlicher, M., Ruiz, P., Wurst, W., Ferrari, V., Abrams, C.S., Gruber, P., Epstein, J.A.: HDAC2 regulates the cardiac hypertrophic response by modulating GSK3β activity. Nature Medicine 13: 324-331, 2007.
178 Wang, Y., Chen, X., Lian, L., Tang, T., Stalker, T.J., Sasaki, T., Brass, L.F., Choi, J.K., Hartwig, J.H., Abrams, C.S.: Loss of PIP5KIβ demonstrates that rapid PIP2 synthesis is required for IP3 formation. Proceedings of the National Academy of Science (U.S.A.) 105: 14064-14069, 2008 Notes: Track II.
15e Pan, W., Choi, S.-C., Wang, H., Qin, Y., Volpicelli-Daley, L., Swan, L., Lucast, L., Khooo, C., Zhang, X., Li, L., Abrams, C.S., Sokol, S.Y., Wu, D.: Wnt3a-mediated formation of phosphatidylinositol 4,5-bisphosphate regulates LRP6 phosphorylation. Science 321: 1350-1353, 2008.
16d Wang, Y., Litvinov, R.I., Chen, X., Lian, L., Bach, T.L., Petrich, B., Monkley, S., Critchley, D., Birnbaum, M.J., Weisel, J.W., Hartwig, J.H., Abrams, C.S.: Loss of PIP5Kγ, but not PIP5Kβ, impairs the integrity of the membrane cytoskeleton. J. Clinical Investigation 118(2): 812-819, 2008.
18e Mao, Y.S., Yamaga, M., Zhu, X., Wei, M., Sun, H.-Q., Wang, J., Yun, M., Wang, Y., Di Paolo, G., Bennett, M., Mellman, I.S., Abrams, C.S., De Camilli, P.V., Lu, C.Y., and Yin, H.L.: Essential and unique roles of PIP5Kγ and α in Fcγ receptor-mediated phagocytosis J. Cell Biology Journal of Cell Biology 184: 281-296, 2009.
101 Lian, L., Wang, W., Flick, M., Choi, J., Scott, E., Degen, J., Lemmon, M.A., Abrams, C.S.: Loss of pleckstrin defines a novel pathway for PKC-mediated exocytosis. Blood In press, 2009.
c1 Min, S.H., Abrams, C.S.: Why do phosphatidylinositol kinases have so many isoforms? Biochemical J 423(1): 99-108, 2009.
173 Volpicelli-Daley, L.A., Lucast, L., Gong, L.-W., Liu, L., Sasaki, J., Sasaki, T., Abrams, C.S., Kanaho, Y., De Camilli, P.: Phosphatidylinositol 4-phosphate 5-kinases (PIPKIs) and phosphatidylinositol 4,5 bisphosphate [PI(4,5)P2] synthesis in the brain. J. Biologic Chemistry Page: 28708-14, 2010.
142 Mitsios, J.V., Prévost, N., Kasirer-Friede, A., Gutierrez, E., Groisman, A., Abrams, C.S., Litvinov, R.I., Zemljic-Harpf, A., Ross, R.S., Shattil, S., J.: What is vinculin needed for in platelets? J. Thrombosis & Haemostasis Page: 2294-2304, 2010.
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