A5084984241- Angiogenesis and VEGF in Cancer
- Protein Kinase Regulation and GTPase Signaling
- Retinal Diseases and Treatments
- PI3K/AKT/mTOR signaling in cancer
- Retinal and Macular Surgery
- Cell Adhesion Molecules Research
- Glaucoma and retinal disorders
- Retinal Development and Disorders
- Cancer, Hypoxia, and Metabolism
- Fibroblast Growth Factor Research
- Cancer-related Molecular Pathways
- Protein Tyrosine Phosphatases
- Corneal Surgery and Treatments
- Protease and Inhibitor Mechanisms
- Chronic Myeloid Leukemia Treatments
- Sphingolipid Metabolism and Signaling
- Retinal and Optic Conditions
- Proteoglycans and glycosaminoglycans research
- Corneal surgery and disorders
- Intraocular Surgery and Lenses
- Ubiquitin and proteasome pathways
- Platelet Disorders and Treatments
- FOXO transcription factor regulation
- Cytokine Signaling Pathways and Interactions
- Ocular Oncology and Treatments
University of Illinois Chicago
2016-2025
Smith-Kettlewell Eye Research Institute
2010-2024
University of Virginia
2024
Clinical Research Consortium
2022
Harvard University
2010-2021
Illinois College
2021
University of Illinois Urbana-Champaign
2021
Aalborg University Hospital
2019-2021
Massachusetts Eye and Ear Infirmary
2009-2018
Orthopaedic Research
2018
Systemic sclerosis (scleroderma) is characterized by immunologic abnormalities, injury of endothelial cells, and tissue fibrosis. Abnormal oxidative stress has been documented in scleroderma linked to fibroblast activation. Since platelet-derived growth factor (PDGF) stimulates the production reactive oxygen species (ROS) since IgG from patients with reacts human fibroblasts, we tested hypothesis that have serum autoantibodies stimulate PDGF receptor (PDGFR), activating collagen-gene expression.
Rina Plattner, Lisa Kadlec, Kris A. DeMali, Andrius Kazlauskas, and Ann Marie Pendergast Department of Pharmacology Cancer Biology, Duke University Medical Center, Durham, North Carolina 27710 USA; Shepens Eye Research Institute, Harvard School, Boston, Massachusetts 02114 USA
The ras proto-oncogene products appear to relay intracellular signals via the Ras guanosine triphosphatase (GTPase) activator protein, GAP. In dog epithelial cells expressing human platelet-derived growth factor (PDGF) receptors, binding of PDGF caused approximately one-tenth total GAP molecules complex with receptor. Studies mutant receptors showed that maximum association required both receptor kinase activity and phosphorylatable tyrosine residues at identified sites autophosphorylation.
The B cell antigen receptor complex is a hetero-oligomeric structure composed of binding, membrane immunoglobulin, and transducer-transporter substructures. substructure disulfide-linked dimers immunoglobulin (Ig)-α Ig-β/γ subunits that are products the mb-1(α) B29 (β/γ) genes. Although associates with Src family kinases activated after ligation, site interaction these other cytoplasmic effector molecules unknown. tails Ig-α Ig-β chains were found to associate distinct sets molecules. chain...
Human platelet-derived growth factor receptors (PDGFRs) expressed in human Hep G2 cells internalized and concentrated a juxtanuclear region near the Golgi network within 10 minutes after were treated with PDGF. A PDGFR mutant (F5) that lacks high-affinity binding sites for Src homology 2 domain-containing proteins phosphatidylinositol-3 kinase (PI-3 kinase), Ras guanosine triphosphatase activating protein, phospholipase C-γ, phosphotyrosine phosphatase (Syp) remained at cell periphery....
In response to binding of platelet-derived growth factor (PDGF), the PDGF receptor (PDGFR) beta subunit is phosphorylated on tyrosine residues and associates with numerous signal transduction enzymes, including GTPase-activating protein ras (GAP) phosphatidylinositol 3-kinase (PI3K). Previous studies have shown that association PI3K requires phosphorylation 751 (Y751) in kinase insert this region forms at least a portion site for PI3K. study, vitro GAP PDGFR was investigated. Like PI3K, only...
It has been demonstrated that the lipid products of phosphoinositide 3-kinase (PI3K) can associate with Src homology 2 (SH2) domains specific signaling molecules and modify their actions. In current experiments, phosphatidylinositol 3,4,5-trisphosphate (PtdIns-3,4,5-P<sub>3</sub>) was found to bind C-terminal SH2 domain phospholipase Cγ (PLCγ) an apparent <i>K</i> <sub>d</sub> 2.4 μm displace from activated platelet-derived growth factor receptor (PDGFR). To investigate <i>in...
Ligand-stimulated autophosphorylation of the platelet-derived growth factor receptor (PDGFR) beta subunit creates a number binding sites for SH2-containing proteins. One PDGFR-associated proteins is 64-kDa protein unknown identity and function. We present data indicating that associates with activated PDGFR Syp (also called SH-PTP2, PTP-1D, or SH-PTP3), ubiquitously expressed protein-tyrosine phosphatase. Phosphorylation Tyr-1009 in C terminus required stable association Syp, suggesting...
The binding of cytoplasmic signaling proteins such as phospholipase C-gamma 1 and Ras GTPase-activating protein to autophosphorylated growth factor receptors is directed by their noncatalytic Src homology region 2 (SH2) domains. p85 alpha regulatory subunit phosphatidylinositol (PI) 3-kinase, which associates with several receptor protein-tyrosine kinases, also contains two SH2 Both domains, when expressed individually fusion in bacteria, bound stably the activated beta for platelet-derived...