Steroids up-regulate p66Shc longevity protein in growth regulation by inhibiting its ubiquitination

PLoS ONE

Volumn 6, Issue 1, 2011, Pages

  Kumar, Santosh ^a   Kumar, Satyendra ^a   Rajendran, Mythilypriya ^a   Alam, Syed Mahfuzul ^a   Lin, Fen Fen ^a   Cheng, Pi Wan ^a,b   Lin, Ming Fong ^a,b  

^a UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

^b UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANDROGEN; ANTINEOPLASTIC AGENT; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; CYCLOHEXAMIDE; DACTINOMYCIN; LACTACYSTIN; LEUPEPTIN; PROTEIN P66SHC; PROTEIN SHC; UNCLASSIFIED DRUG; SHC1 PROTEIN, HUMAN; STEROID; STEROID RECEPTOR;

ANTINEOPLASTIC ACTIVITY; ARTICLE; CANCER CELL; CANCER INHIBITION; CELL GROWTH; CELL LEVEL; CELL PROLIFERATION; CONTROLLED STUDY; DRUG RESPONSE; FEMALE; GROWTH REGULATION; HUMAN; HUMAN CELL; MALE; OVARY CANCER; PROSTATE CANCER; UBIQUITINATION; UPREGULATION; CHEMISTRY; DRUG EFFECT; GENETICS; METABOLISM; OVARY TUMOR; PATHOLOGY; PHYSIOLOGY; PROSTATE TUMOR; TUMOR CELL LINE;

CELL LINE, TUMOR; CELL PROLIFERATION; FEMALE; HUMANS; MALE; OVARIAN NEOPLASMS; PROSTATIC NEOPLASMS; RECEPTORS, STEROID; SHC SIGNALING ADAPTOR PROTEINS; STEROIDS; UBIQUITINATION; UP-REGULATION;

EID: 79251536860     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0015942     Document Type: Article

References (44)

1. Ravichandran KS (2001) Signaling via Shc family adapter proteins. Oncogene 20: 6322-6330.
2. Migliaccio E, Giorgio M, Mele S, Pelicci G, Reboldi P, et al. (1999) The p66shc adaptor protein controls oxidative stress response and life span in mammals. Nature 402: 309-313.
3. Migliaccio E, Mele S, Salcini AE, Pelicci G, Lai KM, et al. (1997) Opposite effects of the p52Shc/p46Shc and p66Shc splicing isoforms on the EGF receptor-MAP kinase-fos signaling pathway. EMBO Journal 16: 706-716.
4. Ventura A, Maccarana M, Raker VA, Pelicci PG (2004) A cryptic targeting signal induces isoform-specific localization of p46Shc to mitochondria. Journal of Biological Chemistry 279: 2299-2306.
5. Alam SM, Rajendran M, Ouyang S, Veeramani S, Zhang L, et al. (2009) A novel role of Shc adaptor proteins in steroid hormone-regulated cancers. Endocrine-Related Cancer 16: 1-16.
6. Li N, Batzer A, Daly R, Yajnik V, Skolnik E, et al. (1993) Guanine-nucleotidereleasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling. Nature 363: 85-88.
7. Nemoto S, Finkel T (2002) Redox regulation of forkhead proteins through a p66shc-dependent signaling pathway. Science 295: 2450-2452.
8. Napoli C, Martin-Padura I, de Nigris F, Giorgio M, Mansueto G, et al. (2003) Deletion of the p66Shc longevity gene reduces systemic and tissue oxidative stress, vascular cell apoptosis, and early atherogenesis in mice fed a high-fat diet. PNAS 100: 2112-2116.
9. Xie Y, Hung MC (1996) p66Shc isoform down-regulated and not required for HER-2/neu signaling pathway in human breast cancer cell lines with HER-2/neu overexpression. Biochemical and Biophysical Research Communications 221: 140-145.
10. Jackson JG, Yoneda T, Clark GM, Yee D (2000) Elevated levels of p66 shc are found in breast cancer cell lines and primary tumors with high metastatic potential. Clinical Cancer Research 6: 1135-1139.
11. Stevenson LE, Frackelton AR, Jr. (1998) Constitutively tyrosine phosphorylated p52 Shc in breast cancer cells: correlation with ErbB2 and p66 Shc expression. Breast Cancer Research and Treatment 49: 119-128.
12. Davol PA, Bagdasaryan R, Elfenbein GJ, Maizel AL, Frackelton AR, Jr. (2003) Shc proteins are strong, independent prognostic markers for both node negative and node positive primary breast cancer. Cancer Research 63: 6772-6783.
13. Abdollahi A, Gruver BN, Patriotis C, Hamilton TC (2003) Identification of epidermal growth factor-responsive genes in normal rat ovarian surface epithelial cells. Biochemical and Biophysical Research Communications 18: 188-197.
14. Lee MS, Igawa T, Chen SJ, Van Bemmel D, Lin JS, et al. (2004) p66Shc protein is upregulated by steroid hormones in hormone-sensitive cancer cells and in primary prostate carcinomas. International Journal of Cancer 108: 672-678.
15. Park YJ, Kim TY, Lee SH, Kim H, Kim SW, et al. (2005) p66shc expression in proliferating thyroid cells is regulated by thyrotropin receptor signaling. Endocrinology 146: 2473-2480.
16. Grossman SR, Lyle S, Resnick MB, Sabo E, Lis RT, et al. (2007) p66 Shc tumor levels show a strong prognostic correlation with disease outcome in stage IIA colon cancer. Clinical Cancer Research 13: 5798-5804.
17. Veeramani S, Igawa T, Yuan TC, Lin FF, Lee MS, et al. (2005) Expression of p66(Shc) protein correlates with proliferation of human prostate cancer cells. Oncogene 24: 7203-7212.
18. Natalicchio A, Laviola L, De Tullio C, Renna LA, Montrone C, et al. (2004) Role of the p66Shc isoform in insulin-like growth factor I receptor signaling through MEK/Erk and regulation of actin cytoskeleton in rat myoblasts. Journal of Biological Chemistry 279: 43900-43909.
19. Ventura A, Luzi L, Pacini S, Baldari CT, Pelicci PG (2004) The p66Shc longevity gene is silenced through epigenetic modifications of an alternative promoter. Journal of Biological Chemistry 277: 22370-22376.
20. Khanday FA, Yamamori T, Mattagajasingh I, Zhang Z, Bugayenko A, et al. (2006) Rac1 Leads to Phosphorylation-dependent Increase in Stability of the p66shc Adaptor Protein: Role in Rac1-induced Oxidative Stress. Molecular Biology of the Cell 17: 122-129.
21. Ciechanover A, Schwartz AL (1998) The ubiquitin-proteasome pathway: the complexity and myriad functions of proteins death. PNAS 95: 2727-2730.
22. Chau V, Tobias JW, Bachmair A, Marriott D, Ecker DJ, et al. (1989) A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science 243: 1576-83.
23. Hochstrasser M (1996) Ubiquitin-dependent protein degradation. Annual Review of Genetics 30: 405-39.
24. Hershko A, Ciechanover A (1998) The ubiquitin system. Annual Review of Biochemistry 67: 425-479.
25. Pickart CM (2004) Back to the future with ubiquitin. Cell 116: 181-190.
26. Hicke L (2001) Protein regulation by monoubiquitin. Nature Reviews Molecular Cell Biology 2: 195-201.
27. Di Fiore PP, Polo S, Hofmann K (2003) When ubiquitin meets ubiquitin receptors: a signalling connection. Nature Reviews Molecular Cell Biology 4: 491-497.
28. Lin MF, Meng TC, Rao PS, Chang C, Schonthal AH, et al. (1998) Expression of human prostatic acid phosphatase correlates with androgen-stimulated cell proliferation in prostate cancer cell lines. Journal of Biological Chemistry 273: 5939-5947.
29. Meng TC, Lin MF (1998) Tyrosine phosphorylation of c-ErbB-2 is regulated by the cellular form of prostatic acid phosphatase in human prostate cancer cells. Journal of Biological Chemistry 273: 22096-22104.
30. Igawa T, Lin FF, Lee MS, Karan D, Batra SK, et al. (2002) Establishment and characterization of androgen-independent human prostate cancer LNCaP cell model. Prostate 50: 222-235.
31. Eissa NT, Yuan J, Haggerty CM, Choo EK, Moss J (1998) Cloning and characterization of human inducible nitric oxide synthase splice variants: A domain, encoded by exons 8 and 9, is critical for dimerization. PNAS 95: 7625-7630.
32. Veeramani S, Yuan TC, Lin FF, Lin MF (2008) Mitochondrial redox signaling by p66Shc is involved in regulating androgenic growth stimulation of human prostate cancer cells. Oncogene 27: 5057-5068.
33. Masiello D, Cheng S, Bubley GJ, Lu ML, Balk SP (2002) Bicalutamide functions as an androgen receptor antagonist by assembly of a transcriptionally inactive receptor. Journal of Biological Chemistry 277: 26321-26326.
34. Trinei M, Giorgio M, Cicalese A, Barozzi S, Ventura A, et al. (2002) A p53-p66Shc signaling pathway controls intracellular redox status, levels of oxidationdamaged DNA and oxidative stress-induced apoptosis. Oncogene 30: 3872-3878.
35. Bourdon JC (2007) p53 and its isoforms in cancer. British Journal of Cancer 97: 277-282.
36. Lebiedzinska M, Duszynski J, Rizzuto R, Pinton P, Wieckowski MR (2009) Agerelated changes in levels of p66Shc and serine 36-phosphorylated p66Shc in organs and mouse tissues. Archives of Biochemistry and Biophysics 486: 73-80.
37. Lin HK, Altuwaijri S, Lin WJ, Kan PY, Collins LL, Chang C (2002) Proteasome activity is required for androgen receptor transcriptional activity via regulation of androgen receptor nuclear translocation and interaction with coregulators in prostate cancer cells. Journal of Biological Chemistry 277: 36570-36576.
38. Voges D, Zwick P, Baumeister W (1999) The 26S proteasome: a molecular machine designed for controlled proteolysis. Annual Review of Biochemistry 68: 1015-1068.
39. Rechsteiner M, Rogers SW (1996) PEST sequences and regulation by proteolysis. Trends in Biochemical Sciences 21: 267-271.
40. Fenteany G, Schreiber SL (1998) Lactacystin, proteasome function, and cell fate. Journal of Biological Chemistry 273: 8545-8548.
41. Hough R, Pratt G, Rechsteiner M (1987) Purification of two high molecular weight proteases from rabbit reticulocyte lysate. Journal of Biological Chemistry 262: 8303-8313.
42. Waxman L, Fagan JM, Goldberg L (1987) Demonstration of two distinct high molecular weight proteases in rabbit reticulocytes, one of which degrades ubiquitin conjugates. Journal of Biological Chemistry 262: 2451-2457.
43. Eytan E, Ganoth D, Armon T, Hershko A (1989) ATP-dependent incorporation of 20S protease into the 26S complex that degrades proteins conjugated to ubiquitin. PNAS 86: 7751-7755.
44. Driscoll J, Goldberg AL (1990) The proteasome (multicatalytic protease) is a component of the 1500-kDa proteolytic complex which degrades ubiquitinconjugated proteins. Journal of Biological Chemistry 265: 4789-4792.