RICERCA ITALIANA     

Similar research programs:

• 1 - Studies on the molecular mechanisms of abnormal parathyroid proliferation and function, and identification and clinical use of molecular markers of sporadic and familial parathyroid cancer. New insights on the prevalence of skeletal, neuropsychological and metabolic manifestations of primary hyperparathyroidism, their relationship with calcium sensing receptor polymorphisms and course after parathyroidectomy.
• 2 - Genetics, biology and clinics of paragangliomas: mitochondrial succinate-dehydrogenase mutations as a model for studying transmission, growth, variability and treatment of neural crest-derived tumors.
• 3 - Diagnostic and therapeutic implications of the new clinic and molecular knowledges of medullary thyroid carcinoma del .
• 4 - Hereditary spastic paraplegias: a genetic, functional and clinical study
• 5 - Development and progression of hepatocellular carcinoma: molecular mechanisms and therapeutic implications.
• 6 - Biochemical and genetic studies of autistic disorder
• 7 - Variability and function of mitochondrial mutations in physiological and pathological conditions
• 8 - New insights into the mutational load and into the possibilities of cytogenetic and molecular monitoring of myeloid dysplasia/neoplasia
• 9 - Hypoxia-induced angiogenetic genes: susceptibility factors to Amyotrophic Lateral Sclerosis ?
• 10 - Molecular analysis of erythropoiesis: Post-genomic and functional approach

Scientific and education field classification

• Field: Scienze mediche
  • GENETICA MEDICA
  • MALATTIE DEL SANGUE
  • PEDIATRIA GENERALE E SPECIALISTICA

International Patent Classification

• CHEMISTRY; METALLURGY
  • BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • MEASURING OR TESTING PROCESSES INVOLVING ENZYMES OR MICRO-ORGANISMS (immunoassay G01N33/53); COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
    • MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF (biocides, pest repellants or attractants, or plant growth regulators, containing micro-organisms, viruses, microbial fungi, enzymes, fermentates or substances produced by or extracted from micro-organisms or animal material A01N63/00; food compositions A21, A23; medicinal preparations A61K; chemical aspects of, or use of materials for, bandages, dressings, absorbent pads or surgical articles A61L; fertilisers C05); PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS (preservation of living parts of humans or animals A01N1/02); MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA (micro-biological testing media C12Q)

Geographical classification

• Region: Campania

Bibliografia

1. Gordeeux VR, David W. Stockton DWand Prchal J Congenital polycythemias/erythrocytoses. Haematologica 2005; 90:109-116
2.Mary F. McMullin, D. Bareford, P. Campbell, A. R. Green, Claire Harrison,Beverley Hunt, D. Oscier, M. I. Polkey, J. T. Reilly, E. Rosenthal, Kate Ryan, T. C. Pearson and Bridget Wilkins Guidelines for the diagnosis, investigation and management of polycythaemia/erythrocytosis. Br J Haematol. 2005 Jul;130:174-95.
3. Crews, S.T., and Fan, C.M. 1999. Remembrance of things PAS: regulation of development by bHLH-PAS proteins. Curr. Opin. Genet. Dev. 9:580–587.
4. Hogenesch, J.B., et al. 2000. The basic helix-loop-helix-PAS protein MOP9 is a brain-specific heterodimeric partner of circadian and hypoxia factors. J. Neurosci. 20:RC83.
5. Semenza, G.L. 2000. HIF1: mediator of physiological and pathophysiological responses to hypoxia. J. Appl. Physiol. 88:1474–1480.
6. Carrero, P., et al. 2000. Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxiainducible factor 1a. Mol. Cell Biol. 20:402–415.
7. Ema, M., et al. 1999. EMBO J. 18:1905–1914.
8. Arany, Z., et al. 1996. An essential role for p300/CBP in the cellular response to hypoxia. Proc. Natl. Acad. Sci. U. S. A. 93:12969–12973.
9.Wang, G.L., et al. 1995. Hypoxiainduciblefactor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension. Proc. Natl. Acad. Sci. U. S. A. 92:5510–5514.
10. Huang, L.E., et al. 1996. J. Biol. Chem. 271:32253–32259.
11.Kallio, P.J. et al. 1997.Activation of hypoxia-inducible factor 1a: posttranscriptional regulation and conformational change by recruitment of the Arnt transcription factor. Proc. Natl. Acad. Sci. U. S. A. 94:5667–5672.
12. Yu, A.Y., et al. 1998. Temporal, spatial, and oxygen-regulated expression of hypoxia-inducible factor-1 in the lung. Am. J. Physiol. 275:L818–L826.
13. Kallio PJ, et al. Regulation of the hypoxia-inducible transcription factor 1_ by the ubiquitin-proteasome pathway. J Biol Chem 274: 6519–6525, 1999.
14. Salceda S and Caro J. Hypoxia-inducible factor 1_ (HIF-1_) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes. J Biol Chem 272: 22642–22647, 1997.
15. Cockman ME et al. Hypoxia inducible factor-_ binding and ubiquitylation by the von Hippel-Lindau tumor suppressor protein. J Biol Chem 275: 25733–25741, 2000.
16. Maxwell PH et al.The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis. Nature 399: 271–275, 1999.
17. Kamura T, et al. Activation of HIF1_ ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex. Proc Natl Acad Sci USA 97: 10430–10435, 2000.
18. Sutter CH, et al. Hypoxia-inducible factor 1_ protein expression is controlled by oxygen-regulated ubiquitination that is disrupted by deletions and missense mutations. Proc Natl Acad Sci USA 97: 4748–4753, 2000.
19. Ohh M et al. Ubiquitination of hypoxia-inducible factor requires direct binding to the _-domain of the von Hippel-Lindau protein. Nat Cell Biol 2: 423–427, 2000.
20. Tanimoto K, et al.. Mechanism of regulation of the hypoxia-inducible factor-1_ by the von Hippel-Lindau tumor suppressor protein. EMBO J 19: 4298–4309, 2000.
21. Ivan M et al. HIF_ targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing. Science 292: 464–468, 2001.
22. Jaakkola P et al. Targeting of HIF-_ to the von Hippel-Lindau ubiquitylation complex by O2 regulated prolyl hydroxylation. Science 292: 468–472, 2001.
23. Yu F, et al. HIF-1_ binding to VHL is regulated by stimulus-sensitive proline hydroxylation. Proc Natl Acad Sci USA 98: 9630–9635, 2001.
24. Masson N, et al.. Independent function of two destruction domains in hypoxia-inducible factor-_ chains activated by prolyl hydroxylation. EMBO J 20 5197–5206, 2001.
25. Hirsila M, et al. Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor. J Biol Chem 278: 30772–30780, 2003.
26. Maynard MA, et al.. Multiple splice variants of the human HIF-3_ locus are targets of the von Hippel-Lindau E3 ubiquitin ligase complex. J Biol Chem 278: 11032–11040, 2003.
27. Bruick RK and McKnight SL. A conserved family of prolyl-4-hydroxylases that modify HIF. Science 294: 1337–1340, 2001.
28. Epstein AC et al. C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 107: 43–54, 2001.
29. Ivan M et al. Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor. Proc Natl Acad Sci USA 99: 13459–13464, 2002.
30. Jiang BH, et al. Hypoxia-inducible factor 1 levels vary exponentially over a physiologically relevant range of O2 tension. Am J Physiol Cell Physiol 271: C1172–C1180, 1996.
31. Ang SO, Chen H, Hirota K, Gordeuk VR, Jelinek J, Guan Y, Liu E, Sergueeva AI, Miasnikova GY, Mole D, Maxwell PH, Stockton DW, Semenza GL, Prchal JT. Disruption of oxygen homeostasis underlies congenital Chuvash polycythemia. Nat Genet. 2002 ;32:614-21
32. Sergeyeva A, Gordeuk VR, Tokarev YN, Sokol L, Prchal JF, Prchal JT. Congenital polycythemia in Chuvashia. Blood. 1997;89:2148-54.
33.Gordeuk VR, Sergueeva AI, Miasnikova GY, Okhotin D, Voloshin Y, Choyke PL, Butman JA, Jedlickova K, Prchal JT, Polyakova LA. Congenital disorder of oxygen sensing: association of the homozygous Chuvash polycythemia VHL mutation with thrombosis and vascular abnormalities but not tumors. Blood. 2004;103:3924-32.
34. Ang SO, Chen H, Gordeuk VR, Sergueeva AI, Polyakova LA, Miasnikova GY, Kralovics R, Stockton DW, Prchal JT Endemic polycythemia in Russia: mutation in the VHL gene. Blood Cells Mol Dis. 2002 Jan-Feb;28(1):57-62.
35. Pastore YD, Jelinek J, Ang S, Guan Y, Liu E, Jedlickova K, Krishnamurti L, Prchal JT. Mutations in the VHL gene in sporadic apparently congenital polycythemia. Blood 2003;101:1591-1595
36. Pastore Y, Jedlickova K, Guan Y, Liu E, Fahner J, Hasle H, Prchal JF, Prchal JT. Mutations of von Hippel-Lindau tumor-suppressor gene and congenital polycythemia. Am J Hum Genet 2003;73:412-419.
37. Percy MJ, McMullin MF, Jowitt SN, Potter M, Treacy M, Watson WH, Lappin TR. Chuvash-type congenital polycythemia in 4 families of Asian and Western European ancestry. Blood 2003;102:1097-1099.
38. Cario H, Schwarz K, Jorch N, Kyank U, Petrides PE, Schneider DT, Uhle R, Debatin KM, Kohne E. Mutations in the von Hippel-Lindau (VHL) tumor suppressor gene and VHL-haplotype analysis in patients with presumable congenital erythrocytosis. Haematologica. 2005;90:19-24.
39. Bento MC, Chang KT, Guan Y, Liu E, Caldas G, Gatti RA, Prchal JT Congenital polycythemia with homozygous and heterozygous mutations of von Hippel-Lindau gene: five new Caucasian patients. Haematologica. 2005;90:128-9.
40. Randi ML, Murgia A, Putti MC, Martella M, Casarin A, Opocher G, Fabris F. Low frequency of VHL gene mutations in young individuals with polycythemia and high serum erythropoietin. Haematologica. 2005;90:689-91.

Keywords

HYPOXIA, O2-SENSING MECHANISMS, POLYCYTHEMIA, VON HIPPEL-LINDAU, HIF1-ALPHA, PROLINE HYDROXYLASE (PHD), CHUVASH POLYCYTHEMIA, ERYTHROPOIETIN, ERYTHROPOIETIN RECEPTOR