0B68 Caro, Jaime - Thomas Jefferson University
Thomas Jefferson University
Sidney Kimmel Medical College
Department of Medicine

Caro, Jaime

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Jaime Caro, MD

Contact Dr. Caro

1020 Locust Street
Suite 394
Philadelphia, PA 19107

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

Research & 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.


Most Recent Peer-Reviewed Publications

  1. Control of glycolytic flux by AMP-activated protein kinase in tumor cells adapted to low ph1
  2. The autophagic tumor stroma model of cancer or "battery-operated tumor growth": A simple solution to the autophagy paradox
  3. HIF1-alpha functions as a tumor promoter in cancer associated fibroblasts, and as a tumor suppressor in breast cancer cells: Autophagy drives compartment-specific oncogenesis
  4. Autophagy in cancer associated fibroblasts promotes tumor cell survival: Role of hypoxia, HIF1 induction and NFκB activation in the tumor stromal microenvironment
  5. Functional conservation of erythropoietin signaling in zebrafish
  6. Hypoxia, glucose metabolism and the Warburg's effect
  7. 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
  8. 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
  9. Immunophilin-ligands FK506 and CsA inhibit HIF1α expression by a VHL- and ubiquitin-independent mechanism
  10. Histone deacetylase inhibitors repress the transactivation potential of hypoxia-inducible factors independently of direct acetylation of HIF-α
  11. Characterization of hARD2, a processed hARD1 gene duplicate, encoding a human protein N-α-acetyltransferase
  12. Histone deacetylase inhibitors induce VHL and ubiquitin-independent proteasomal degradation of hypoxia-inducible factor 1α
  13. Expression and hypoxia-responsiveness of 6-phosphofructo-2-kinase/fructose- 2,6-bisphosphatase 4 in mammary gland malignant cell lines
  14. 6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase gene family overexpression in human lung tumor
  15. Interaction between HIF-1α (ODD) and hARD1 does not induce acetylation and destabilization of HIF-1α
  16. Overexpression of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-4 in the human breast and colon malignant tumors
  17. 6-Phosphofructo-2-kinase (pfkfb3) gene promoter contains hypoxia-inducible factor-1 binding sites necessary for transactivation in response to hypoxia
  18. Allan j. Erslev, m.d.: truly a great dane (1919-2003).
  19. Hypoxic regulation of the 6-phosphofructo-2-kinase/fructose-2,6- bisphosphatase gene family (PFKFB-1-4) expression in vivo
  20. MAPK signaling up-regulates the activity of hypoxia-inducible factors by its effects on p300