Jaime Caro, M.D.

Contact Dr. Caro

1015 Walnut Street
Suite 804
Philadelphia, PA 19107

(215) 955-7775
(215) 955-9170 fax

Research and Clinical Interests
Dr. Caro's work is directed primarily to the understanding of the physiologic and molecular mechanisms that regulate the expression of genes in response to hypoxia. Hypoxia activates the protein expression and transcriptional activity of the hypoxia-inducible complex HIF-1. This complex, in turn, binds to specific hypoxia-responsive elements in the promoter region of hypoxia-inducible genes. The molecular activation of HIF proteins involves hydroxylase enzymes that control the survival and activity of HIF proteins in an oxygen- and iron-dependent way. Dr. Caro's laboratory is currently investigating the mechanisms by which these hydroxylases act as oxygen sensors and regulate gene expression. Within the genes regulated by HIF proteins are those involved in glucose metabolism, oxygen transport and angiogenesis. Thus, the understanding of the mechanisms that control the activity of HIF proteins may have an important role in new therapeutic approaches to ischemic diseases and tumor treatment.

Publications

Most recent Peer-reviewed Publications

1. Functional conservation of erythropoietin signaling in zebrafish
2. Hypoxia, glucose metabolism and the Warburg's effect
3. Constitutive/hypoxic degradation of HIF-α proteins by the proteasome is independent of von Hippel Lindau protein ubiquitylation and the transactivation activity of the protein
4. Hypoxic regulation of PFKFB-3 and PFKFB-4 gene expression in gastric and pancreatic cancer cell lines and expression of PFKFB genes in gastric cancers
5. Immunophilin-ligands FK506 and CsA inhibit HIF1α expression by a VHL- and ubiquitin-independent mechanism
6. Histone deacetylase inhibitors repress the transactivation potential of hypoxia-inducible factors independently of direct acetylation of HIF-α
7. Characterization of hARD2, a processed hARD1 gene duplicate, encoding a human protein N-α-acetyltransferase
8. Histone deacetylase inhibitors induce VHL and ubiquitin-independent proteasomal degradation of hypoxia-inducible factor 1α
9. Expression and hypoxia-responsiveness of 6-phosphofructo-2-kinase/fructose- 2,6-bisphosphatase 4 in mammary gland malignant cell lines
10. 6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase gene family overexpression in human lung tumor
11. Interaction between HIF-1α (ODD) and hARD1 does not induce acetylation and destabilization of HIF-1α
12. Overexpression of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-4 in the human breast and colon malignant tumors
13. 6-Phosphofructo-2-kinase (pfkfb3) gene promoter contains hypoxia-inducible factor-1 binding sites necessary for transactivation in response to hypoxia
14. Hypoxic regulation of the 6-phosphofructo-2-kinase/fructose-2,6- bisphosphatase gene family (PFKFB-1-4) expression in vivo
15. MAPK signaling up-regulates the activity of hypoxia-inducible factors by its effects on p300
16. Enhanced response to basiliximab in a patient with aplastic anemia after treatment with standard immunosuppression [6]
17. To what degree does cognitive impairment in Alzheimer's disease predict dependence of patients on caregivers?
18. Carboxyl-terminal transactivation activity of hypoxia-inducible factor 1α is governed by a von Hippel-Lindau protein-independent, hydroxylation-regulated association with p300/CBP
19. Hypoxia-inducible factor-1-mediated expression of the 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-3 (PFKFB3) gene: Its possible role in the warburg effect
20. Adenoviral E1A: everlasting tool, versatile applications, continuous contributions and new hypotheses.

View All Publications