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The elucidation of the mechanism of action of growth factors has emerged as one of the fundamental problems in biological sciences and is proving critical for understanding the causes underlying the unrestrained proliferation of cancer cells. The research activities of this laboratory are focused on the identification of extracellular factors and intracellular signal transduction pathways that stimulate cells to divide. We discovered that neuropeptides (e.g., peptides of the bombesin family) which act as molecular messengers in a rich network of information exchange throughout the organism, are potent cellular growth factors for multiple cell types in culture and function as autocrine/paracrine mitogens for human cancer cells. We study the transmission of the neuropeptide signal from surfacereceptors to the nucleus along a number of transduction pathways, typically protein kinase cascades, that act in a synergistic and combinatorial fashion to promote cell proliferation. Our work revealed that regulatory peptides trigger a complex set of molecular responses and specific protein kinase cascades including kinase C and A, mitogen-activated protein kinases (MAPKs) and p70 S6 ribosomal protein kinase. Recently, we reported on the cloning and expression analysis of a novel protein kinase termed protein kinase D (PKD). PKD is directly activated by phorbol esters and also is part of a novel phosphorylation cascade downstream of protein kinase C. Future research activities in this area include a detailed mutational analysis to define the contribution of different domains of PKD to its regulation and to modulate its expression to determine the role of PKD in cell regulation. In addition to serine/threonine protein kinase cascades, our studies demonstrated that neuropeptides also stimulate a rapid increase in the tyrosine phosphorylation of multiple substrates including focal adhesion kinase (FAK), paxillin, and Crk-associated substrate (CAS). These proteins which localize at focal adhesion plaques, are implicated in cell migration, proliferation, and transformation. Our work is dissecting the molecular mechanisms by which neuropeptides and growth factors induce these downstream pathways and is elucidating the role of these pathways in cell proliferation.
The elucidation of the mechanism of action of growth factors has emerged as one of the fundamental problems in biological sciences and is proving critical for understanding the causes underlying the unrestrained proliferation of cancer cells. The research activities of this laboratory are focused on the identification of extracellular factors and intracellular signal transduction pathways that stimulate cells to divide. We discovered that neuropeptides (e.g., peptides of the bombesin family) which act as molecular messengers in a rich network of information exchange throughout the organism, are potent cellular growth factors for multiple cell types in culture and function as autocrine/paracrine mitogens for human cancer cells. We study the transmission of the neuropeptide signal from surfacereceptors to the nucleus along a number of transduction pathways, typically protein kinase cascades, that act in a synergistic and combinatorial fashion to promote cell proliferation. Our work revealed that regulatory peptides trigger a complex set of molecular responses and specific protein kinase cascades including kinase C and A, mitogen-activated protein kinases (MAPKs) and p70 S6 ribosomal protein kinase. Recently, we reported on the cloning and expression analysis of a novel protein kinase termed protein kinase D (PKD). PKD is directly activated by phorbol esters and also is part of a novel phosphorylation cascade downstream of protein kinase C. Future research activities in this area include a detailed mutational analysis to define the contribution of different domains of PKD to its regulation and to modulate its expression to determine the role of PKD in cell regulation. In addition to serine/threonine protein kinase cascades, our studies demonstrated that neuropeptides also stimulate a rapid increase in the tyrosine phosphorylation of multiple substrates including focal adhesion kinase (FAK), paxillin, and Crk-associated substrate (CAS). These proteins which localize at focal adhesion plaques, are implicated in cell migration, proliferation, and transformation. Our work is dissecting the molecular mechanisms by which neuropeptides and growth factors induce these downstream pathways and is elucidating the role of these pathways in cell proliferation.
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Jessica Nevarez-Mejia,Yi-Ping Jin,Harry Pickering,Rajesh Parmar, Nicole M. Valenzuela,Rebecca A. Sosa,Sebastiaan Heidt, Gregory A. Fishbein,Enrique Rozengurt,William M. Baldwin,Robert L. Fairchild,Elaine F. Reed
American Journal of Transplantationno. 3 (2023): 406-418
Sushovan Guha,Guido Eibl,Krisztina Kisfalvi, Robert S. Fan,Marie Burdick, Howard Reber,Oscar J. Hines, Robert Strieter,Enrique Rozengurt
crossref(2023)
Sushovan Guha,Guido Eibl,Krisztina Kisfalvi, Robert S. Fan,Marie Burdick, Howard Reber,Oscar J. Hines, Robert Strieter,Enrique Rozengurt
crossref(2023)
American Journal of Transplantation (2023)
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HUMAN IMMUNOLOGY (2023): 40-40
American journal of physiology. Gastrointestinal and liver physiologyno. 3 (2023): G239-G250
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