- Growth Hormone and Insulin-like Growth Factors
- Metabolism, Diabetes, and Cancer
- Cancer, Hypoxia, and Metabolism
- Ubiquitin and proteasome pathways
- Amyotrophic Lateral Sclerosis Research
- PI3K/AKT/mTOR signaling in cancer
- Glycosylation and Glycoproteins Research
- Pancreatic function and diabetes
- Epigenetics and DNA Methylation
- Cell Adhesion Molecules Research
- Cancer Cells and Metastasis
- Occupational and environmental lung diseases
- Cancer-related gene regulation
- Protein Kinase Regulation and GTPase Signaling
- Cancer Research and Treatments
- Cancer-related Molecular Pathways
- RNA modifications and cancer
- Proteoglycans and glycosaminoglycans research
- S100 Proteins and Annexins
- Cytokine Signaling Pathways and Interactions
- Fibroblast Growth Factor Research
- RNA Research and Splicing
- Cancer, Lipids, and Metabolism
- Wnt/β-catenin signaling in development and cancer
- Redox biology and oxidative stress
Temple University
2020-2025
Philadelphia University
2016-2025
Sidney Kimmel Cancer Center
2011-2024
Thomas Jefferson University
2012-2024
Temple College
2023
Robert Bosch (Germany)
2011
University of Milan
1997
Columbia University
1997
The adapter protein Grb10 belongs to a superfamily of related proteins, including Grb7, -10, and -14 Caenorhabditis elegans Mig10. is an interacting partner the insulin-like growth factor I receptor (IGF-IR) insulin (IR). Previous work showed inhibitory effect mouse (mGrb10α) on IGF-I-mediated mitogenesis (A. Morrione et al., J. Biol. Chem. 272:26382-26387, 1997). With mGrb10α as bait in yeast two-hybrid screen, Nedd4 (mNedd4-1), ubiquitin ligase, was previously isolated 274: 24094-24099,...
R− cells are 3T3-like fibroblasts generated from mouse embryos nullizygous for a targeted disruption of the genes encoding type 1 insulin-like growth factor (IGF) receptor (IGF1R). These fail to proliferate in serum-free medium supplemented with purified factors, contrast their wild-type counterparts. However, when overexpress insulin stably integrated plasmid, R−/IR cells, they become capable growing solely or IGF-II, but not IGF-I. Moreover, introduction into an additional plasmid...
We have recently discovered that the insulin-like growth factor receptor I (IGF-IR) is up-regulated in human invasive bladder cancer and promotes migration invasion of transformed urothelial cells. The proteoglycan decorin, a key component tumor stroma, can positively regulate IGF-IR system normal However, there are no available data on role decorin modulating activity cells or models. Here we show expression inversely correlated with low high grade cancers (n = 20 each). Decorin bound...
Although the growth factor progranulin was discovered more than two decades ago, functional receptor remains elusive. Here, we that EphA2, a member of large family Ephrin tyrosine kinases, is signaling for progranulin. Recombinant bound with high affinity to EphA2 in both solid phase and solution. Interaction caused prolonged activation receptor, downstream stimulation mitogen-activated protein kinase Akt, promotion capillary morphogenesis. Furthermore, found an autoregulatory mechanism...
Abstract The growth factor proepithelin (also known as progranulin, acrogranin, PC-derived factor, or granulin-epithelin precursor) is a secreted glycoprotein that functions an important regulator of cell growth, migration, and transformation. Proepithelin overexpressed in great variety cancer lines clinical specimens breast, ovarian, renal well glioblastomas. In this study, we have investigated the effects on bladder cells using human recombinant purified to homogeneity from 293-EBNA cells....
Abstract The adaptor protein Grb10 is an interacting partner of the IGF‐I receptor (IGF‐IR) and insulin (IR). Previous work from our laboratory has established role as a negative regulator IGF‐IR‐dependent cell proliferation. We have shown that binds E3 ubiquitin ligase Nedd4 promotes IGF‐I‐stimulated ubiquitination, internalization, degradation IGF‐IR, thereby giving rise to long‐term attenuation signaling. Recent biochemical evidence suggests tyrosine‐kinase receptors (RTK) may not be...
The insulin receptor isoform A (IR-A) binds both and insulin-like growth factor (IGF)-II, although the affinity for IGF-II is 3–10-fold lower than depending on a cell tissue context. Notably, in mouse embryonic fibroblasts lacking IGF-IR expressing solely IR-A (R−/IR-A), more potent mitogen insulin. As endocytosis degradation provide spatial temporal regulation of signaling events, we hypothesized that could affect biological responses by differentially regulating trafficking. Using R−/IR-A...
// Roberta Matà 1, * , Chiara Palladino Maria Luisa Nicolosi 1 Anna Rita Lo Presti Malaguarnera Marco Ragusa 2 Daniela Sciortino Andrea Morrione 3 Marcello Maggiolini 4 Veronica Vella 5, 6 Antonino Belfiore Endocrinology, Department of Health Sciences, University Magna Graecia Catanzaro, Italy Biomedical and Biotechnological Sciences Biology, Genetics BioInformatics Unit, Catania, Urology Biology Prostate Cancer Program, Kimmel Center, Thomas Jefferson University, Philadelphia, PA,...
The type 1 insulin-like growth factor receptor (IGF-IR) plays an important role in the of cells both <i>in vivo</i> and vitro</i>. IGF-IR is also capable inducing differentiation a number cell types, raising question how same can send two seemingly contradictory signals, one for differentiation. Using 32D cells, which are murine hemopoietic we show that activated induce along granulocytic pathway manner similar to granulocyte colony-stimulating factor. We find major substrates IGF-IR,...
After an initial burst of cell proliferation, the type 1 insulin-like growth factor receptor (IGF-IR) induces granulocytic differentiation 32D IGF-IR cells, interleukin-3-dependent murine hemopoietic line devoid insulin substrate-1 (IRS-1). The combined expression and IRS-1 (32D IGF-IR/IRS-1 cells) inhibits IGF-I-mediated differentiation, causes malignant transformation cells. Because role in changing fate cells from (and subsequent death) to transformation, we have looked for differences...
We have utilized the yeast two-hybrid system to identify proteins interacting with mouse Grb10, an adapter protein known interact both insulin and insulin-like growth factor-I receptors. isolated a cDNA clone containing C2 domain of Nedd4, ubiquitin ligase (E3) that also contains hect (homologous E6-APcarboxyl-terminus) three WW domains. The interaction Grb10 in was confirmed using full-length it abolished by deleting last 148 amino acids region includes SH2 newly identified BPS domain....
The insulin-like growth factor-I receptor (IGF-IR), plays a key role in regulating mammalian development and growth, is frequently deregulated cancer contributing to tumor initiation progression. Discoidin domain 1 (DDR1), collagen tyrosine-kinase, as well overexpressed implicated Thus, we investigated whether functional cross-talk between the IGF-IR DDR1 exists any progression.Using human breast cells found that constitutively associated with IGF-IR. However, this interaction was enhanced...