Dr. Ulhas Naik

Professor

Contact

Naik

Office: 329 Wolf Hall
Lab: 256-259 Wolf Hall

Mailing address:
Cardiovascular and Cancer Biology Laboratory
Department of Biological Sciences
256 Wolf Hall
University of Delaware
Newark, DE 19716

Phone: (302) 831-0434
Fax: (302) 831-2281
E-mail: unaik@udel.edu

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Education

B.S., M.S., Ph.D.: University of Bombay, India
Postdoctoral: Cornell University Medical College
Postdoctoral: SUNY Health Science Center at Brooklyn

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Research Interests

Our major research interest is to understand the molecular mechanisms of signal transduction involved in cardiovascular diseases and cancer. Cell-cell interactions and cell-extracellular matrix interactions play key roles in these diseases. Our research focuses on the molecular mechanisms involved in the regulation of these interactions under physiological and pathophysiological conditions.

Understanding the regulation of integrin function through cytoplasmic signaling. Integrins are heterodimeric cell surface receptors that regulate cell-extracellular matrix interactions. The affinity of integrins to appropriate extracellular matrix proteins is modulated in response to cytoplasmic signals, rendering the integrin able to bind these ligands. Upon interaction with the extracellular matrix ligand, signals are also transduced through the integrin from the outside to the inside of the cell. Recent evidence suggests that the binding of proteins to integrin cytoplasmic domains may regulate this bi-directional signaling through the integrin, thereby regulating its function. It is therefore of interest to identify candidate cytoplasmic proteins that interact with integrin cytoplasmic domains and play a role in signal transduction through integrins. Integrin αIIbβ3 (also known as GPIIb/IIIa), the platelet fibrinogen receptor, is an excellent model for studying the mechanism of signal transduction through integrins (Naik and Parise, Curr. Op. Hematol, 1997, 4:317). Integrin αIIbβ3 links platelets to each other and also to exposed matrix proteins in the injured vascular wall, thus initiating both physiological hemostasis and pathological thrombosis. By using the yeast two-hybrid system, we have isolated a novel ˜22 kDa protein, called CIB, which binds specifically to the cytoplasmic domain of αIIb subunit but not to other integrin cytoplasmic domains (Naik et.al., JBC, 1997, 272:4651; Shock et.al., Biochem. J, 1999, 342:729). This protein is homologous to two known calcium-binding regulatory proteins, calcineurin B and calmodulin. My current research interest is to delineate the functional role of CIB in regulating bi-directional signaling through integrin αIIbβ3. We have recently found that CIB is involved in the mechanism of outside-in signaling that is required for platelets to fully-spread on immobilized fibrinogen (Naik et.al., Blood, 2003, 102:1355-1362). In our attempt to understand the underlying mechanism, we found that CIB affects this cell spreading through the activation of focal adhesion kinase, which is well-known to be involved in cell spreading and motility (Naik et.al., Blood, 2003, 102: 3629). Further studies in support of these findings have suggested that CIB may be involved in the regulation of actin dynamics, which may correlate to the platelet spreading and also fibroblast migration phenotype we find to be induced by CIB. Further understanding of the role of CIB in these processes would enhance our knowledge about such pathologies as myocardial infarction, stroke, and cancer metastasis. This project is funded by the National Institutes of Health (HL57630).

In addition, we have also found that CIB is expressed in a number of tissues and cell types where integrin αIIbβ3 is not expressed (Shock et.al, Biochem J, 1999, 342:729). Studies outside the platelet model have shown that, through its binding partner polo-like kinase 3 (Plk3), CIB regulates the cell cycle in human breast cancer cells, specifically through regulation of centrosome separation, and cytokinesis (Naik et.al., JBC, 2003, in revision). It was therefore of interest to understand the structure-function relationship of CIB. As such, I am currently in the process of determining the crystal structure of CIB to better understand how CIB changes its conformation upon calcium binding and regulates the function of a variety of proteins. Currently, the crystallization of both calcium-free and calcium-bound CIB is ongoing. This work is funded by the National Center for Research Resources (1P20RR155801).

Another research area of interest in our lab is focused on elucidating the role of cell adhesion molecules belonging to the immunoglobulin superfamily in the process of tumor-induced angiogenesis. We have recently cloned a novel cell adhesion molecule, JAM-1, which is involved in platelet activation, leukocyte transmigration, and in the regulation of tight junction integrity (Naik et.al., JCS, 2001, 114: 539; Naik and Eckfeld, J. Biol. Regul. Homeost. Agents, 2003, 17: 34). Recent findings from my laboratory have demonstrated that JAM-1 is a key player in the process of bFGF-induced angiogenesis. JAM-1 regulates bFGF-induced angiogenesis through its interaction with integrin αvβ3. Antibody blockade of JAM-1 inhibits bFGF-induced endothelial cell proliferation, migration, and tube formation (Naik et.al., Blood, 2003, 102: 2108; Naik et.al., Blood, 2003, in revision). Recently, we have found that knock-down of JAM-1 using siRNA inhibits bFGF-induced endothelial cell migration on vitronectin specifically through integrin αvβ3 (Naik et.al., Arterioscler Thromb. Vasc. Biol, 2003, 23: 2165). Since the discovery of JAM-1, it has been shown that a family of JAMs exist, which include JAM-2, JAM-3 and JAM-4. Current collaborative efforts are ongoing to understand the functional relationship between these family members in a variety of systems. Presently, I have successfully generated JAM-1 knock-out mice, which are currently being characterized phenotypically. Such studies will help delineate the molecular mechanism underlying the regulation of angiogenesis by JAM-1. This work is funded by the National Institutes of Health (HL63960) and the American Heart Association Pennsylvania and Delaware affiliate (9906203U).

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Current Projects

NIH, Role of JAM-1 in Cell Adhesion and Migration.
NIH, Modulation of Integrin Function by Cytoplasmic Signaling.
NIH, Center of Biomedical Research Excellence (COBRE) project 1: Structure-function Relationship of Calcium- and Integrin-binding Protein.
NASA, Surfactant Structure guide Membrane Protein Crystallization (with Eric Kaler).

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Teaching

BISC 207 - Introductory Biology I (Course Director)

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Research Group

Abdelaziz Bior, Ph.D. - Postdoctoral Fellow (Ph.D., Oklahoma State University). Effects of CIB1 and Plk-3 overexpression on cancer cell cycle.
Ananya Ghosh, M.S. - Graduate Student (M.S., Calcutta University, India). Functional role of CRASS protein and its regulation by CIB1.
Philip Kudish, M.S. - Research Associate (M.S., University of Delaware). Elucidation of signaling pathways during cancer cell migration and angiogenesis.
Meghna Naik, M.S. - Research Associate (M.S., Goa University, India). Functional roles of CIB1 in platelets and tumor cells; elucidation of signaling pathways during cell migration.
Chad Blamey, B.S. - Graduate Student (B.S., University of Colorado). Structure function relationship of CIB1 using macromolecular crystallography.
Zack Britton, B.S. - Graduate Student (B.S., Carnegie Melon University). Regulation of microtubules during platelet spreading.
Vesselina Cooke, B.S. - Graduate Student (B.S., Southwest Missouri State University). Functional role of JAM-A in vascular biology: investigation of JAM-A signaling pathway using knock-out mouse.
Miles Cowart, B.S. - Graduate Student (B.S., University of Delaware). Functional role of CRASS protein and its regulation by CIB1.
Katherine Maddox, B.S. - Graduate Student (B.S., University of Delaware). Physiological role of CIB family of calcium binding proteins.
Monica Mikhail, B.S. - Graduate Student (B.S., University of Delaware). Post translational modification of JAM-A in cancer cell metastasis.
Erik Welf, B.S. - Graduate Student (B.S., North Carolina State University). Modeling of crosstalk between cell proliferation and migration pathways in cancer cells.
Undergraduates: Colleen Cheong, Mini Manrai, Darrell McBride, Jim Parris, Laura Shankman, Allen Tseng

Naik lab group

The Laboratory for Cardiovascular and Cancer Biology

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Selected Publications

Naik, M.U., Naik, T.U., Suckow, A.T., Duncan, M.K. and Naik, U.P. Attenuation of junctional adhesion molecule-A is a contributing factor for breast cancer cell invasion. Can. Res. 2008; 68:April 1 2008.

Braiterman, L.T., Heffernan, S., Nyasae, L., Johns, D., See, A.P., Yutzy, R., McNickle, A., Herman, M., Sharma, A., Naik, U.P., Hubbard, A.L. JAM-A is both essential and inhibitory to the development of hepatic polarity in WIF-B cells. Am. J. Physiol. Gastrointest. Liver Physiol. 2008; 294:G576-G588.

Naik, T.U., Naik, M.U. and Naik, U.P. Junctional adhesion molecules in angiogenesis. Frontiers in Biosciences. 2008; 13:258-262.

Shao, M., Ghosh, A., Cooke, V.G., Naik, U.P. and Martin-Deleon, P.A. JAM-A is present in mammalian spermatozoa where it is essential for normal motility. Dev Biol. 2008; 313:246-255.

Bonner, M. and Naik, U.P. Regulation of platelet integrin α_IIbβ₃ signaling by cytoplasmic domain binding proteins. Frontiers in Biosciences. 2007; 12:2038-2049.

Kang, L.I., Wang, I., Suckow, A.T., Czymmek, K.J., Cooke, V.G., Naik, U.P. and Duncan, M.K. Deletion of JAM-A causes morphological defects in the corneal epithelium. International J. Biochemistry and Cell Biology. 2007; 39576-39585.

Kostyak, J.C. and Naik, U.P. Megakaryopoiesis: transcriptional insight into megakaryocyte maturation. Frontiers in Biosciences. 2007; 12:2050-2062.

Naik, M.U., and Naik, U.P. Junctional adhesion molecule-A-induced endothelial cell migration on vitronectin is integrin α_vβ₃ specific. J. Cell Sci. 2006; 119:490-499.

Cooke, V.G., Naik, M.U., and Naik, U.P. Impaired bFGF induced angiogenesis in JAM-A deficient mice. Arterioscler. Thromb. Vasc. Biol. 2006; 26:2005-2011.

Naik, U.P. Uncovering the dark side of PKCδ. Blood. 2006; 108:3959-3956.

Blamey, C.J., Ceccarelli, C., Naik, U.P., and Bahnson, B.J. The crystal structure of calcium- integrin- binding protein 1: insights into redox regulated functions. Protein Science 2005; 14:1214-1224.

Parris, J.J., Cooke, V.G., Skarnes, W.C., Duncan, M.K. and Naik, U.P. JAM-A expression during embryonic development. Developmental Dynamics 2005; 233:1517-1524.

Berger, B., Blamey, C.J. Naik, U.P., Bahnson, B.J. and Lenhoff, A. The roles of additives and precipitants in crystallization of calcium- and integrin-binding protein. Crystal Growth and Design 2005; 5:1499-1507.

Cui, W., Ning, J., Naik U.P. and Duncan M.K. OptiRNAi, an RNAi design tool. Computer Methods and Programs in Biomedicine. 2004; 75:67-73.

Cui, W., Ning, J., Naik U.P. and Duncan M.K. OptiRNAi, a web-based program to select siRNA sequences. Proceedings of the IEEE Bioinformatics Conference, Stanford, CA. 2003; 433-434.

Naik, U.P. and Eckfeld, K. Junctional adhesion molecule (JAM-1). J. Biol. Regul. Homeost. Agents. 2003; 17:341-347.

Naik, U.P. and Naik, M.U., Association of CIB1 with GPIIb/IIIa during outside-in signaling is required for platelet spreading on fibrinogen. Blood. 2003; 102:1355-1362.

Naik, M.U., Mousa, S.A. Parkos, C. and Naik, U.P. Signaling through JAM-1 and α_vβ₃ is required for the angiogenic action of bFGF: dissociation of the JAM-1 and α_vβ₃ complex. Blood. 2003; 102:2108-2114.

Naik, M.U. and Naik, U.P. Calcium- and Integrin-Binding protein regulates focal adhesion kinase activity during platelet spreading on immobilized fibrinogen. Blood. 2003; 102:3629-3636.

Naik, M.U., Vuppalanchi, D., and Naik, U.P. Essential role of junctional adhesion molecule-1 in basic fibroblast growth factor-induced endothelial cell migration. Arterioscler Thromb Vasc Biol. 2003; 23:2165-2171.

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Dr. Ulhas Naik Professor Contact Naik Office: 329 Wolf Hall Lab: 256-259 Wolf Hall Mailing address: Cardiovascular and Cancer Biology Laboratory Department of Biological Sciences 256 Wolf Hall University of Delaware Newark, DE 19716 Phone: (302) 831-0434 Fax: (302) 831-2281 E-mail: unaik@udel.edu Go to top of page Education B.S., M.S., Ph.D.: University of Bombay, India Postdoctoral: Cornell University Medical College Postdoctoral: SUNY Health Science Center at Brooklyn Go to top of page Research Interests Our major research interest is to understand the molecular mechanisms of signal transduction involved in cardiovascular diseases and cancer. Cell-cell interactions and cell-extracellular matrix interactions play key roles in these diseases. Our research focuses on the molecular mechanisms involved in the regulation of these interactions under physiological and pathophysiological conditions. Understanding the regulation of integrin function through cytoplasmic signaling. Integrins are heterodimeric cell surface receptors that regulate cell-extracellular matrix interactions. The affinity of integrins to appropriate extracellular matrix proteins is modulated in response to cytoplasmic signals, rendering the integrin able to bind these ligands. Upon interaction with the extracellular matrix ligand, signals are also transduced through the integrin from the outside to the inside of the cell. Recent evidence suggests that the binding of proteins to integrin cytoplasmic domains may regulate this bi-directional signaling through the integrin, thereby regulating its function. It is therefore of interest to identify candidate cytoplasmic proteins that interact with integrin cytoplasmic domains and play a role in signal transduction through integrins. Integrin αIIbβ3 (also known as GPIIb/IIIa), the platelet fibrinogen receptor, is an excellent model for studying the mechanism of signal transduction through integrins (Naik and Parise, Curr. Op. Hematol, 1997, 4:317). Integrin αIIbβ3 links platelets to each other and also to exposed matrix proteins in the injured vascular wall, thus initiating both physiological hemostasis and pathological thrombosis. By using the yeast two-hybrid system, we have isolated a novel ˜22 kDa protein, called CIB, which binds specifically to the cytoplasmic domain of αIIb subunit but not to other integrin cytoplasmic domains (Naik et.al., JBC, 1997, 272:4651; Shock et.al., Biochem. J, 1999, 342:729). This protein is homologous to two known calcium-binding regulatory proteins, calcineurin B and calmodulin. My current research interest is to delineate the functional role of CIB in regulating bi-directional signaling through integrin αIIbβ3. We have recently found that CIB is involved in the mechanism of outside-in signaling that is required for platelets to fully-spread on immobilized fibrinogen (Naik et.al., Blood, 2003, 102:1355-1362). In our attempt to understand the underlying mechanism, we found that CIB affects this cell spreading through the activation of focal adhesion kinase, which is well-known to be involved in cell spreading and motility (Naik et.al., Blood, 2003, 102: 3629). Further studies in support of these findings have suggested that CIB may be involved in the regulation of actin dynamics, which may correlate to the platelet spreading and also fibroblast migration phenotype we find to be induced by CIB. Further understanding of the role of CIB in these processes would enhance our knowledge about such pathologies as myocardial infarction, stroke, and cancer metastasis. This project is funded by the National Institutes of Health (HL57630). In addition, we have also found that CIB is expressed in a number of tissues and cell types where integrin αIIbβ3 is not expressed (Shock et.al, Biochem J, 1999, 342:729). Studies outside the platelet model have shown that, through its binding partner polo-like kinase 3 (Plk3), CIB regulates the cell cycle in human breast cancer cells, specifically through regulation of centrosome separation, and cytokinesis (Naik et.al., JBC, 2003, in revision). It was therefore of interest to understand the structure-function relationship of CIB. As such, I am currently in the process of determining the crystal structure of CIB to better understand how CIB changes its conformation upon calcium binding and regulates the function of a variety of proteins. Currently, the crystallization of both calcium-free and calcium-bound CIB is ongoing. This work is funded by the National Center for Research Resources (1P20RR155801). Another research area of interest in our lab is focused on elucidating the role of cell adhesion molecules belonging to the immunoglobulin superfamily in the process of tumor-induced angiogenesis. We have recently cloned a novel cell adhesion molecule, JAM-1, which is involved in platelet activation, leukocyte transmigration, and in the regulation of tight junction integrity (Naik et.al., JCS, 2001, 114: 539; Naik and Eckfeld, J. Biol. Regul. Homeost. Agents, 2003, 17: 34). Recent findings from my laboratory have demonstrated that JAM-1 is a key player in the process of bFGF-induced angiogenesis. JAM-1 regulates bFGF-induced angiogenesis through its interaction with integrin αvβ3. Antibody blockade of JAM-1 inhibits bFGF-induced endothelial cell proliferation, migration, and tube formation (Naik et.al., Blood, 2003, 102: 2108; Naik et.al., Blood, 2003, in revision). Recently, we have found that knock-down of JAM-1 using siRNA inhibits bFGF-induced endothelial cell migration on vitronectin specifically through integrin αvβ3 (Naik et.al., Arterioscler Thromb. Vasc. Biol, 2003, 23: 2165). Since the discovery of JAM-1, it has been shown that a family of JAMs exist, which include JAM-2, JAM-3 and JAM-4. Current collaborative efforts are ongoing to understand the functional relationship between these family members in a variety of systems. Presently, I have successfully generated JAM-1 knock-out mice, which are currently being characterized phenotypically. Such studies will help delineate the molecular mechanism underlying the regulation of angiogenesis by JAM-1. This work is funded by the National Institutes of Health (HL63960) and the American Heart Association Pennsylvania and Delaware affiliate (9906203U). Go to top of page Current Projects NIH, Role of JAM-1 in Cell Adhesion and Migration. NIH, Modulation of Integrin Function by Cytoplasmic Signaling. NIH, Center of Biomedical Research Excellence (COBRE) project 1: Structure-function Relationship of Calcium- and Integrin-binding Protein. NASA, Surfactant Structure guide Membrane Protein Crystallization (with Eric Kaler). Go to top of page Teaching BISC 207 - Introductory Biology I (Course Director) Go to top of page Research Group Abdelaziz Bior, Ph.D. - Postdoctoral Fellow (Ph.D., Oklahoma State University). Effects of CIB1 and Plk-3 overexpression on cancer cell cycle. Ananya Ghosh, M.S. - Graduate Student (M.S., Calcutta University, India). Functional role of CRASS protein and its regulation by CIB1. Philip Kudish, M.S. - Research Associate (M.S., University of Delaware). Elucidation of signaling pathways during cancer cell migration and angiogenesis. Meghna Naik, M.S. - Research Associate (M.S., Goa University, India). Functional roles of CIB1 in platelets and tumor cells; elucidation of signaling pathways during cell migration. Chad Blamey, B.S. - Graduate Student (B.S., University of Colorado). Structure function relationship of CIB1 using macromolecular crystallography. Zack Britton, B.S. - Graduate Student (B.S., Carnegie Melon University). Regulation of microtubules during platelet spreading. Vesselina Cooke, B.S. - Graduate Student (B.S., Southwest Missouri State University). Functional role of JAM-A in vascular biology: investigation of JAM-A signaling pathway using knock-out mouse. Miles Cowart, B.S. - Graduate Student (B.S., University of Delaware). Functional role of CRASS protein and its regulation by CIB1. Katherine Maddox, B.S. - Graduate Student (B.S., University of Delaware). Physiological role of CIB family of calcium binding proteins. Monica Mikhail, B.S. - Graduate Student (B.S., University of Delaware). Post translational modification of JAM-A in cancer cell metastasis. Erik Welf, B.S. - Graduate Student (B.S., North Carolina State University). Modeling of crosstalk between cell proliferation and migration pathways in cancer cells. Undergraduates: Colleen Cheong, Mini Manrai, Darrell McBride, Jim Parris, Laura Shankman, Allen Tseng The Laboratory for Cardiovascular and Cancer Biology Go to top of page Selected Publications Naik, M.U., Naik, T.U., Suckow, A.T., Duncan, M.K. and Naik, U.P. Attenuation of junctional adhesion molecule-A is a contributing factor for breast cancer cell invasion. Can. Res. 2008; 68:April 1 2008. Braiterman, L.T., Heffernan, S., Nyasae, L., Johns, D., See, A.P., Yutzy, R., McNickle, A., Herman, M., Sharma, A., Naik, U.P., Hubbard, A.L. JAM-A is both essential and inhibitory to the development of hepatic polarity in WIF-B cells. Am. J. Physiol. Gastrointest. Liver Physiol. 2008; 294:G576-G588. Naik, T.U., Naik, M.U. and Naik, U.P. Junctional adhesion molecules in angiogenesis. Frontiers in Biosciences. 2008; 13:258-262. Shao, M., Ghosh, A., Cooke, V.G., Naik, U.P. and Martin-Deleon, P.A. JAM-A is present in mammalian spermatozoa where it is essential for normal motility. Dev Biol. 2008; 313:246-255. Bonner, M. and Naik, U.P. Regulation of platelet integrin α_IIbβ₃ signaling by cytoplasmic domain binding proteins. Frontiers in Biosciences. 2007; 12:2038-2049. Kang, L.I., Wang, I., Suckow, A.T., Czymmek, K.J., Cooke, V.G., Naik, U.P. and Duncan, M.K. Deletion of JAM-A causes morphological defects in the corneal epithelium. International J. Biochemistry and Cell Biology. 2007; 39576-39585. Kostyak, J.C. and Naik, U.P. Megakaryopoiesis: transcriptional insight into megakaryocyte maturation. Frontiers in Biosciences. 2007; 12:2050-2062. Naik, M.U., and Naik, U.P. Junctional adhesion molecule-A-induced endothelial cell migration on vitronectin is integrin α_vβ₃ specific. J. Cell Sci. 2006; 119:490-499. Cooke, V.G., Naik, M.U., and Naik, U.P. Impaired bFGF induced angiogenesis in JAM-A deficient mice. Arterioscler. Thromb. Vasc. Biol. 2006; 26:2005-2011. Naik, U.P. Uncovering the dark side of PKCδ. Blood. 2006; 108:3959-3956. Blamey, C.J., Ceccarelli, C., Naik, U.P., and Bahnson, B.J. The crystal structure of calcium- integrin- binding protein 1: insights into redox regulated functions. Protein Science 2005; 14:1214-1224. Parris, J.J., Cooke, V.G., Skarnes, W.C., Duncan, M.K. and Naik, U.P. JAM-A expression during embryonic development. Developmental Dynamics 2005; 233:1517-1524. Berger, B., Blamey, C.J. Naik, U.P., Bahnson, B.J. and Lenhoff, A. The roles of additives and precipitants in crystallization of calcium- and integrin-binding protein. Crystal Growth and Design 2005; 5:1499-1507. Cui, W., Ning, J., Naik U.P. and Duncan M.K. OptiRNAi, an RNAi design tool. Computer Methods and Programs in Biomedicine. 2004; 75:67-73. Cui, W., Ning, J., Naik U.P. and Duncan M.K. OptiRNAi, a web-based program to select siRNA sequences. Proceedings of the IEEE Bioinformatics Conference, Stanford, CA. 2003; 433-434. Naik, U.P. and Eckfeld, K. Junctional adhesion molecule (JAM-1). J. Biol. Regul. Homeost. Agents. 2003; 17:341-347. Naik, U.P. and Naik, M.U., Association of CIB1 with GPIIb/IIIa during outside-in signaling is required for platelet spreading on fibrinogen. Blood. 2003; 102:1355-1362. Naik, M.U., Mousa, S.A. Parkos, C. and Naik, U.P. Signaling through JAM-1 and α_vβ₃ is required for the angiogenic action of bFGF: dissociation of the JAM-1 and α_vβ₃ complex. Blood. 2003; 102:2108-2114. Naik, M.U. and Naik, U.P. Calcium- and Integrin-Binding protein regulates focal adhesion kinase activity during platelet spreading on immobilized fibrinogen. Blood. 2003; 102:3629-3636. Naik, M.U., Vuppalanchi, D., and Naik, U.P. Essential role of junctional adhesion molecule-1 in basic fibroblast growth factor-induced endothelial cell migration. Arterioscler Thromb Vasc Biol. 2003; 23:2165-2171. 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University of Delaware • Department of Biological Sciences • 118 Wolf Hall • Newark, DE 19716