Andres Ferber
Thomas Jefferson University
Network
Latest external collaboration on country level. Dive into details by clicking on the dots.
Publication
Featured researches published by Andres Ferber.
Molecular and Cellular Biology | 1994
D Coppola; Andres Ferber; M Miura; Christian Sell; C D'Ambrosio; Raphael Rubin; Renato Baserga
When wild-type mouse embryo cells are stably transfected with a plasmid constitutively overexpressing the epidermal growth factor (EGF) receptor (EGFR), the resulting cells can grow in serum-free medium supplemented solely with EGF. Supplementation with EGF also induces in these cells the transformed phenotype (growth in soft agar). However, when the same EGFR expression plasmid is introduced and overexpressed in cells derived from littermate embryos in which the insulin-like growth factor I (IGF-I) receptor genes have been disrupted by homologous recombination, the resulting cells are unable to grow or to be transformed by the addition of EGF. Reintroduction into these cells (null for the IGF-I receptor) of a wild-type (but not of a mutant) IGF-I receptor restores EGF-mediated growth and transformation. Our results indicate that at least in mouse embryo fibroblasts, the EGFR requires the presence of a functional IGF-I receptor for its mitogenic and transforming activities.
Molecular and Cellular Biology | 1992
Pierluigi Porcu; Andres Ferber; Zbigniew Pietrzkowski; Charles T. Roberts; Martin L. Adamo; Derek LeRoith; Renato Baserga
We have used a plasmid expressing a temperature-sensitive (ts) mutant of simian virus 40 (SV40) T antigen, stably transfected into 3T3 cells, to study the role of insulinlike growth factor 1 (IGF-1) and its receptor in T-antigen-mediated growth. While 3T3 cells do not grow in serum-free medium, in 1% serum, or with the sole addition of either platelet-derived growth factor (PDGF) or IGF-1, cells expressing the tsA T antigen (BALB 58 cells) grow at 34 degrees C in either PDGF or 1% serum but not in IGF-1. At the restrictive temperature (39.6 degrees C), these cells can only grow in 10% serum. We show that BALB 58 cells, at 34 degrees C, have a markedly increased expression of IGF-1 and IGF-1 mRNA and that their growth in 1% serum (at 34 degrees C) is inhibited by an antisense oligodeoxynucleotide to the IGF-1 receptor RNA. When this tsA plasmid is stably transfected into cells constitutively overexpressing the human IGF-1 receptor cDNA, the resulting cell lines show a constitutively phosphorylated IGF-1 receptor and grow in serum-free medium at 34 degrees C (but not at 39.6 degrees C). A functional SV40 T antigen also increases the expression of a plasmid in which the reporter luciferase gene is under the control of a rat IGF-1 promoter. We conclude (i) that the SV40 T antigen induces the expression of IGF-1 and IGF-1 mRNA, at least in part by a transcriptional mechanism, thus altering the growth factors requirements, and (ii) that, in BALB/c3t3 cells, the SV40 T antigen necessitates a functional IGF-1 receptor for its growth-stimulating effect in low serum (or PDGF).
Annals of the New York Academy of Sciences | 2006
Jose Martinez; Andres Ferber; Tami L. Bach; Christopher H. Yaen
Abstract: The conversion of fibrinogen into fibrin and the association of fibrin(ogen) with activated platelets play a fundamental role in hemostasis because their interaction with the injured vessel prevents blood extravasation. Platelet aggregates and fibrin also participate in the occlusion of the vascular lumen in pathological conditions. Fibrin II also promotes the formation of new blood vessels, for example, during wound healing and tumor growth. Using an in vitro assay, we have studied the mechanism by which fibrin II induces formation of capillaries. Generation of fibrin II on top of an endothelial cell monolayer rapidly rearranged the ECs into a capillary network. In contrast, neither fibrin I nor fibrin 325 induced these morphogenetic changes, indicating that exposure of the N‐terminal peptide β15–42 is involved in this process. Binding studies, using the N‐terminal fragment of fibrin (NDSK II), showed that NDSK II binds to EC with high affinity, but neither NDSK nor NDSK325 bound specifically. Binding of NDSK II to endothelial cells was blocked with an antibody to VE‐cadherin. Direct association of NDSK II and VE‐cadherin was also demonstrated in a VE‐cadherin antibody capture assay. NDSK II bound specifically with the captured VE‐cadherin but NDSK or NDSK 325 did not associate with VE‐cadherin. Moreover, fibrin II associated with EC VE‐cadherin and this interaction triggered the formation of capillary‐like structures. A better understanding of the cellular responses to fibrin, identification of the fibrin binding site within VE‐cadherin and the intracellular signaling that follows this interaction, could yield important information that may translate into better control of the angiogenic process.
Biology of Blood and Marrow Transplantation | 2009
Joanne Filicko-O'Hara; Dolores Grosso; Phyllis Flomenberg; Thea M. Friedman; Janet Brunner; William R. Drobyski; Andres Ferber; Irina Kakhniashvili; Carolyn A. Keever-Taylor; Bijoyesh Mookerjee; Julie-An Talano; John I. Wagner; Robert Korngold; Neal Flomenberg
Although allogeneic hematopoietic progenitor cell transplant (HPCT) is curative therapy for many disorders, it is associated with significant morbidity and mortality, which can be related to graft-versus-host disease (GVHD) and the immunosuppressive measures required for its prevention and/or treatment. Whether the immunosuppression is pharmacologic or secondary to graft manipulation, the graft recipient is left at increased risk of the threatening opportunistic infection. Refractory viral diseases in the immunocompromised host have been treated by infusion of virus-specific lymphotyces and by unmanipulated donor lymphocyte infusion (DLI) therapy. L-leucyl-L-leucine methyl ester (LLME) is a compound that induces programmed cell death of natural killer (NK) cells, monocytes, granulocytes, most CD8(+) T cells, and a small fraction of CD4(+) T cells. We have undertaken a study of the use of LLME-treated DLI following T cell-depleted allogeneic HPCT, specifically to aid with immune reconstitution. In this ongoing clinical trial, we have demonstrated the rapid emergence of virus-specific responses following LLME DLI with minimal associated GVHD. This paper examines the pace of immune recovery and the rapid development of antiviral responses in 6 patients who developed viral infections during the time period immediately preceding or coincident with the administration of the LLME DLI.
Cancer Research | 1996
Consuelo D'Ambrosio; Andres Ferber; Mariana Resnicoff; Renato Baserga
Biology of Blood and Marrow Transplantation | 2007
Dionissios Neofytos; Ambrish Ojha; Bijoyesh Mookerjee; John L. Wagner; Joanne Filicko; Andres Ferber; Scott K. Dessain; Dolores Grosso; Janet Brunner; Neal Flomenberg; Phyllis Flomenberg
Journal of Cellular Physiology | 1995
Tiziana DeAngelis; Andres Ferber; Renato Baserga
Journal of Biological Chemistry | 1993
Andres Ferber; Chung Der Chang; Christian Sell; Andrej Ptasznik; Vincent J. Cristofalo; Karen Hubbard; Harvey L. Ozer; Martin L. Adamo; Charles T. Roberts; Derek LeRoith; Guillaume Duménil; Renato Baserga
Cancer Research | 1991
Krzysztof Reiss; Andres Ferber; Salvatore Travali; Pierluigi Porcu; Paul D. Phillips; Renato Baserga
Biology of Blood and Marrow Transplantation | 2001
Thea M. Friedman; Gabor Varadi; Deborah D Hopely; Joanne Filicko; John E. Wagner; Andres Ferber; Jose Martinez; Janet Brunner; Dolores Grosso; Liza McGuire; Robert Korngold; Neal Flomenberg