Area:
Molecular Biology, Cell Biology
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High-probability grants
According to our matching algorithm, Bruce I. Terman is the likely recipient of the following grants.
Years |
Recipients |
Code |
Title / Keywords |
Matching score |
1999 — 2005 |
Terman, Bruce I |
R01Activity Code Description: To support a discrete, specified, circumscribed project to be performed by the named investigator(s) in an area representing his or her specific interest and competencies. |
Vegf Induced Signal Transduction
DESCRIPTION: (Applicant's Description) Anglogenesis (the formation of new blood capillaries) is an important component of several normal physiological processes including development and wound healing. Angiogenesis also contributes to the onset and spread of disease, for example in cancer angiogenesis provides tumor cells with essential nutrients and thus contributes to tumor growth. An anti-angiogenesis strategy for fighting cancer is attractive because this would target endothelial cells and potentially avoid the drug resistance observed when targeting tumor cells. Vascular Endothelial Growth Factor (VEGF) has received consideration as a target for angiogenesis inhibition for several reasons: Its expression by tumor cells is augmented by a lack of nutrients, VEGF's actions are specific to endothelial cells, and blocking VEGF's actions will inhibit the growth of tumors grown in mice. Information on the signal transduction pathways activated by VEGF is limited. Previously, our laboratory discovered the KDR gene and identified it as a receptor for VEGF. KDR is a receptor tyrosine kinase and we have identified four autophosphorylation sites. The experiments proposed in this application are directed at two goals. First, we wish to understand at a molecular level how KDR autophosphorylation recruits cell signaling proteins. Second, we have designed experiments to clarify the cellular consequence of specific receptor/signaling protein interactions. Four Specific Aims are proposed to accomplish these goals. Specific Aim 1 will determine whether there are autophosphorylation sites in addition to the ones reported earlier. Specific Aim 2 will test the hypothesis that receptor autophosphorylation in the kinase domain is required for maximum catalytic activity. Specific Aim 3 is directed at clarifying the signaling proteins which interact with receptor autophosphorylation sites. Specific Aim 4 is directed at clarifying endothelial cellular response which are dependent upon receptor phosphorylation at specific tyrosines.
|
1 |
2001 — 2004 |
Terman, Bruce I |
R01Activity Code Description: To support a discrete, specified, circumscribed project to be performed by the named investigator(s) in an area representing his or her specific interest and competencies. |
Role of Hspg in Vegf Binding to Kdr
DESCRIPTION (Applicant's abstract): A new experimental strategy for treating ischemia of the human myocardium is to use angiogenic growth factors to induce neovascularization. This approach is based upon recent findings showing that in the adult heart the genes encoding angiogenic growth factors and their receptors are expressed in areas surrounding ischemic myocardium, but at levels that are insufficient to provide robust formation of collaterals. Administration of angiogenic growth factors can be viewed as an amplification of a normal response of the myocardia to ischemia. Vascular endothelial growth factor (VEGF) serves as a major angiogenic factor in normal cardiac development, and its use in therapeutic angiogenesis is currently undergoing clinical evaluation. VEGF binds to two high affinity endothelial cell receptor, KDR and FLT1. The interaction of VEGF with KDR is dependent upon other cell surface molecules, in particular heparan sulfate proteoglycans (NSPG). Little information is available as to the mechanisms by which HSPGs allow for growth factor binding. My application proposes three Specific Aims for clarifying those mechanisms. Specific Aim 1 tests the hypothesis that HSPGs interact with KDR in order to facilitate receptor dimerization and VEGF binding. The proposed experiments build upon previously obtained results that support this hypothesis. Specific Aim 2 is directed at identifying the proteoglycan involved in VEGF binding to KDR. Experiments are proposed for testing whether a known pro teoglycan is responsible; or if not, for purifying the protein and identifying its amino acid sequence. Specific Aim 3 is directed at testing whether the relevant HSPG participates in VEGF-induced signaling events. The rationale for this study relates to the recent information derived from the literature indicating that HSPGs participate in the signal transduction pathways by which cells respond to their extracellular environment.
|
1 |
2005 |
Terman, Bruce I |
R01Activity Code Description: To support a discrete, specified, circumscribed project to be performed by the named investigator(s) in an area representing his or her specific interest and competencies. |
Nck and Crk in Vegf-Induced Endothelial Cells Migration @ Albert Einstein Col of Med Yeshiva Univ
DESCRIPTION (provided by applicant): The growth of new blood capillaries from existing vessels (angiogenesis) is essential for development, tissue regeneration and remodeling. Angiogenesis also contributes to pathologic conditions including tumor growth and metastasis, diabetic retinopathy, rheumatoid arthritis, psoriasis, and cardiovascular diseases. Vascular Endothelial Growth Factor (VEGF) is a critical pro-angiogenic factor that stimulates multiple signal transduction pathways through binding to its receptor KDR. VEGF has received attention as a target for angiogenesis inhibition for several reasons, including the observations that blocking VEGF's actions by several experimental approaches inhibits the growth of tumors in animal models. Endothelial cell migration is a crucial step in angiogenesis; however, the cellular mechanisms that mediate this process remain unclear. Our preliminary data indicate that the cell signaling proteins Nck and Crk play important roles in VEGF-induced cell migration. Both proteins are recruited to KDR after VEGF treatment, although their interaction with receptor is indirect and mediated by the FRS2 scaffolding protein. The introduction of dominant negative (DN) inhibitors of Crk or Nck into endothelial cells has dramatic effects on VEGF-induced responses related to migration. The DNs inhibit focal complex turnover as they lead to a loss in the formation of new focal complexes and a significant increase in the size of existing focal complexes. This is accompanied by a loss in cell adhesion. The DNs also blocked VEGF-induced changes in F-actin dynamics. We plan to continue these studies by proposing three Specific Aims. AIM1 focuses on clarifying molecular aspects of how Nck and Crk are recruited to the cell surface after VEGF treatment. AIM 2 examines in detail the signaling pathway by which Nck regulates cell migration. AIM 3 asks how Crk functions in VEGF-induced cell migration.
|
0.934 |