Wikipedia

Jonathan Stamler

Jonathan Solomon Stamler (born June 23, 1959) is an English-born American physician and scientist. He is known for his discovery of protein S-nitrosylation, the addition of a nitric oxide (NO) group to cysteine residues in proteins, as a ubiquitous cellular signal to regulate enzymatic activity and other key protein functions in bacteria, plants and animals, and particularly in transporting NO on cysteines in hemoglobin as the third gas in the respiratory cycle.[1][2][3]

Jonathan S. Stamler
Jonathan Stamler in his laboratory
Born
Jonathan Solomon Stamler

(1959-06-23) June 23, 1959 (age 65)
Wallingford, Oxfordshire, England
NationalityAmerican
Alma mater
Known forIdentification of S-nitrosylation as a protein post-translational modification, characterizing its regulatory enzymes, and defining its physiological and disease relevance
Awards
  • Pew Scholar
  • HHMI Investigator
  • Outstanding Investigator Award in Basic Science (American Federation for Medical Research Foundation)
  • Korsemyer Award (ASCI Award; finalist)
  • Ewing Marion Kauffman Innovator
  • Coulter Translational Partnership Research Award
  • American Heart Association Distinguished Scientist Award
Scientific career
Fields
Institutions

Early life and education

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Stamler was born in Wallingford, England on June 23, 1959 [4] to a British father and American mother, and lived in multiple countries (United Kingdom, Switzerland, Israel, United States) as a youth due to his father's global career. He played on the Israeli national (under 18) tennis team.

He graduated with a bachelor's degree from Brandeis University in 1981, and earned his M.D. degree from Icahn School of Medicine at Mount Sinai in 1985.[4] His residency and fellowship training in pulmonary medicine and in cardiovascular medicine was at Brigham and Women’s Hospital at Harvard Medical School.[4]

Career and research

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Academic appointments

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Stamler was appointed assistant professor in medicine at Harvard Medical School in 1993, and associate professor then Professor in Medicine at Duke University School of Medicine in 1993 and 1996, respectively, with recognition as the George Barth Geller Professor for Research in Cardiovascular Diseases in 2004.[4] He was an Investigator with the Howard Hughes Medical Institute from 1997 to 2005.[4][5] In 2009, Stamler became Robert S. and Sylvia K. Reitman Family Foundation Distinguished Chair in Cardiovascular Innovation and Professor of Medicine, Professor of Biochemistry and founding Director of the Institute for Transformative Molecular Medicine at Case Western Reserve University School of Medicine and University Hospitals Cleveland Medical Center.[4][6] In 2012, Stamler founded and became Director of the Harrington Discovery Institute at University Hospitals Cleveland Medical Center, and in 2016 was named Harrington Discovery Institute President.[4][7][8]

Research

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At the start of Stamler's research career, nitric oxide (NO) gas had recently been identified as a signaling molecule that mediated vasodilation[9] by binding to the heme cofactor in the enzyme soluble guanylyl cyclase to produce cyclic guanosine monophosphate (cGMP).[10] However, most actions of NO being discovered at that time were not mediated by guanylyl cyclase/cGMP,[11] and high affinity binding of NO to the heme in red blood cell hemoglobin would inhibit NO actions in the vasculature,[10] presenting a quandary.

Stamler would provide a general mechanism to explain NO function in biology, which requires redox-activation of NO to NO+ (nitrosonium ion) to allow its conjugation to all main classes of proteins, and would thereby establish the prototypic redox-based cellular signaling mechanism in biology. Redox activation of NO would also provide a chemical route to stabilize NO bioactivity and escape hemoglobin inactivation.

Specifically, Stamler recognized that NO can be redox-activated [12] to bind cysteine residues in proteins[13][14][15][16] and thiols in other molecules (e.g., glutathione, coenzyme A) to form S-nitrosothiols (SNOs) that are protected from heme inactivation thus providing a means to stabilize and regulate NO bioactivity,[14][17][18][19] and he then identified the first endogenous SNOs.[14][17][15] Stamler further demonstrated that SNO modification of proteins, which he coined 'S-nitrosylation' to denote a signaling function, can regulate enzyme activity by modifying active site or allosteric site cysteines.[13][14][16] He and his colleagues would show that protein S-nitrosylation is widespread, regulating essentially all main classes of proteins: enzymes, globins, transcription factors, receptors, G proteins, protein kinases, ion channels and micro RNA processing machinery.[1][20] That is, NO in the form of an SNO is a cellular signal that acts through post-translational modification of target proteins, akin to protein phosphorylation or ubiquitination.[21] Approximately 10,000 proteins, at >20,000 sites, have been reported to be nitrosylated, and it has been predicted that 70% of the proteome is SNO-modified across phylogeny.[22][23]

More recently, Stamler and coworkers have demonstrated that protein S-nitrosylation is enzymatic, entailing specific enzymes that convert NO to SNO (S-nitrosothiol synthases), transfer NO groups to specific residues in proteins (transnitrosylases), and remove specific SNO groups from proteins (protein denitrosylases).[18][24][25] Enzymatic S-nitrosylation was identified first with hemoglobin (including nitrosylase and SNO synthase activities)[26][27][28][29] and then later with multienzyme machinery in E. coli.[24]

Stamler's studies have established physiological significance for protein S-nitrosylation in diverse cellular processes (receptor signaling, apoptosis, gene regulation, metabolism and immunity), and fundamental physiological functions (skeletal muscle contractility, airway tone, cardiac response to adrenergic stimulation, neuroprotection and development).[21][30] He has also discovered novel cellular functions (red blood cell mediated vasodilation) [20][31] and revealed a new physiological principle: NO carried by an invariant hemoglobin cysteine residue is essential for oxygen delivery to tissues through vasodilation of the microcirculation, redefining the respiratory cycle as a 3-gas system (O2/NO/CO2).[1][2][3][20][31][32][33][34] The SNO-hemoglobin content of RBCs is low in multiple clinical conditions characterized by microvascular dysfunction and tissue hypoxia, including pulmonary hypertension, chronic obstructive pulmonary disease, peripheral arterial disease and sickle cell disease, thereby impairing vasodilation by RBCs.[35][36] Further, since hemoglobin S-nitrosylation is rapidly lost upon blood storage, the oxygen delivery capability of transfused blood is impaired.[37][38][39]

More broadly, accumulated evidence has demonstrated that S-nitrosylation of proteins plays important roles in many diseases, from heart failure to cancer to neurodegenerative disease.[40][41][42][43] Stamler’s studies have shown aberrant S-nitrosylation in asthma,[44][45] pulmonary hypertension,[46] heart failure,[47][48] diabetes,[49] kidney injury,[50][51] and infectious diseases.[52][53]

Examining the hemoglobins of microbes and the parasitic worm Ascaris, Stamler found that ancient forms of hemoglobin either eliminate NO enzymatically (bacteria and yeast) or utilize it to eliminate oxygen from its anaerobic environment (Ascaris), showing that the primordial function of hemoglobin was in NO processing not oxygen transport.[54][55][56][57] Stamler also identified trans-kingdom SNO signaling (operating between species as a general language between microbiota and animal host), since microbiota that produce NO can lead to widespread protein S-nitrosylation in a Caenorhabditis elegans host with profound genetic and physiological consequences.[30] Stamler also identified the enzymatic mechanism of nitroglycerin bioactivation and tolerance, thus solving a longstanding mystery (i.e., the generation of NO from nitroglycerin was awarded a Nobel Prize in 1998, but how was not understood).[58]

Entrepreneurial and philanthropic activities

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Stamler is a co-founder of multiple biotechnology companies, including several that have had public offerings, and he has also licensed additional discoveries to large pharma.[4] He is also known for a track record of innovation and entrepreneurship as a founder of institutes, medical societies, innovation platforms and impact investment funds. His work has been covered in numerous lay publications, including the front page and science sections of the New York Times, as well as Time Magazine and The Economist, in books on the history of science and luck, and in works on outlier innovators.

Stamler is the founder the Harrington Project, a collaboration between the non-profit Harrington Discovery Institute at University Hospitals Health System in Cleveland,[4][7][8] (where he serves as president) and two mission-aligned for-profit partner organizations (Biomotiv, Advent-Harrington Impact Fund) to shepherd laboratory discovery through translation and into biotechnology commercialization and approved therapy.[4][59] Under Stamler’s leadership, Harrington Discovery Institute has partnered with medical charities and non-profit organizations to target specific diseases, including the Foundation Fighting Blindness,[60] Alzheimer's Drug Discovery Foundation,[61] American Cancer Society, and Oxford University (Oxford-Harrington Rare Disease Centre).[62] He has built philanthropic partnerships with Morgan Stanley Wealth Management (Morgan Stanley GIFT Cures powered by Harrington Discovery Institute) and raised impact funds for investment companies (Biomotiv) and on Wall Street (Advent-Harrington Impact Fund with Advent Life Sciences; Morgan Stanley platform) that have totaled ~ $900 million for therapeutics research and development.[63][64][65][66]

References

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  1. ^ a b c Blakeslee, Sandra (1996-03-21). "Surprise Discovery in Blood: Hemoglobin Has Bigger Role". The New York Times. Retrieved 2019-01-11.
  2. ^ a b Blakeslee, Sandra (1997-07-22). "What Controls Blood Flow? Blood". The New York Times. Retrieved 2019-01-11.
  3. ^ a b Saunders, Fenella (1997-01-01). "The NO & SNO Cycle". www.discovermagazine.com. Retrieved 2019-01-11.
  4. ^ a b c d e f g h i j Jonathan Stamler curriculum vitae (PDF), retrieved 2019-01-11[permanent dead link‍]
  5. ^ "Jonathan S. Stamler". hhmi.org/. Howard Hughes Medical Institute. Retrieved 2019-01-11.
  6. ^ "Director of Institute for Transformative Molecular Medicine, Inaugural Robert S. and Sylvia K. Reitman Family Foundation Distinguished Chair in Cardiovascular Innovation Announced". case.edu. Case Western Reserve University. 2009-09-17. Archived from the original on 2016-02-14. Retrieved 2019-01-11.
  7. ^ a b Zeitner, Brie (2012-02-29). "Jonathan Stamler named director, Bob Keith to head drug development of Harrington project". The Plain Dealer.
  8. ^ a b Rosenblum, Jonah (2016-02-11). "Stamler gains 'genius' tag as Harrington Discovery Institute director". Cleveland Jewish News. Retrieved 2019-01-11.
  9. ^ "1998 Nobel Prize in Medicine or Physiology". Nobel Foundation. Retrieved 2019-01-11.
  10. ^ a b Murad, Ferid (1994). "The nitric oxide-cyclic GMP signal transduction system for intracellular and intercellular communication". Recent Prog Horm Res. 49: 239–248. doi:10.1016/b978-0-12-571149-4.50016-7. ISBN 9780125711494. PMID 7511827.
  11. ^ Garg, UC; Hasid, A (August 1990). "Nitric oxide-generating vasodilators inhibit mitogenesis and proliferation of BALB/C 3T3 fibroblasts by a cyclic GMP-independent mechanism". Biochem Biophys Res Commun. 171 (1): 474–479. doi:10.1016/0006-291x(90)91417-q. PMID 1697465.
  12. ^ Stamler, JS; Singel, DJ; Loscalzo, J (1992). "Biochemistry of nitric oxide and its redox-activated forms". Science. 258 (5090): 1898–1902. Bibcode:1992Sci...258.1898S. doi:10.1126/science.1281928. PMID 1281928.
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  16. ^ a b Stamler, JS; Simon, DI; Jaraki, O; Osborne, JA; Francis, S; Mullins, M; Singel, D; Loscalzo, J (1992-09-01). "S-nitrosylation of tissue-type plasminogen activator confers vasodilatory and antiplatelet properties on the enzyme". Proc Natl Acad Sci U S A. 89 (17): 8087–8091. Bibcode:1992PNAS...89.8087S. doi:10.1073/pnas.89.17.8087. PMC 49861. PMID 1325644.
  17. ^ a b Gaston B, Reilly J, Drazen JM, Fackler J, Ramdev P, Arnelle D, Mullins ME, Sugarbaker DJ, Chee C, Singel DJ, Loscalzo J, Stamler JS (1993). "Endogenous nitrogen oxides and bronchodilator S-nitrosothiols in human airways". Proc Natl Acad Sci U S A. 90 (23): 10957–10961. Bibcode:1993PNAS...9010957G. doi:10.1073/pnas.90.23.10957. PMC 47900. PMID 8248198.
  18. ^ a b Benhar, M; Forrester, MT; Stamler, JS (October 2009). "Protein denitrosylation: enzymatic mechanisms and cellular function". Nat Rev Mol Cell Biol. 10 (10): 721–732. doi:10.1038/nrm2764. PMID 19738628. S2CID 24437719.
  19. ^ Anand P, Hausladen A, Wang YJ, Zhang GF, Stomberski C, Brunengraber H, Hess DT, Stamler JS (2014). "Identification of S-nitroso-CoA reductases that regulate protein S-nitrosylation". Proc Natl Acad Sci U S A. 111 (52): 18572–18577. Bibcode:2014PNAS..11118572A. doi:10.1073/pnas.1417816112. PMC 4284529. PMID 25512491.
  20. ^ a b c Jia, L; Bonaventura, C; Bonaventura, J; Stamler, JS (1996-03-21). "S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control". Nature. 380 (6571): 221–226. Bibcode:1996Natur.380..221J. doi:10.1038/380221a0. PMID 8637569. S2CID 4314697.
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  22. ^ Stomberski, C; Hess, DT; Stamler, JS (2018-04-01). "Protein S-Nitrosylation: Determinants of Specificity and Enzymatic Regulation of S-Nitrosothiol-Based Signaling". Antioxidants & Redox Signaling. 30 (10): 1331–1351. doi:10.1089/ars.2017.7403. PMC 6391618. PMID 29130312.
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  24. ^ a b Seth D, Hess DT, Hausladen A, Wang L, Wang YJ, Stamler JS (2018). "A Multiplex Enzymatic Machinery for Cellular Protein S-nitrosylation". Mol Cell. 69 (3): 451–464.e6. doi:10.1016/j.molcel.2017.12.025. PMC 5999318. PMID 29358078.
  25. ^ "New Nitric Oxide-Converting Enzymes Discovered". genengnews.com. Mary Ann Liebert Inc. 2018-01-19.
  26. ^ Pawloski, JR; Hess, DT; Stamler, JS (2001). "Export by red blood cells of nitric oxide bioactivity". Nature. 409 (6820): 622–626. doi:10.1038/35054560. PMID 11214321. S2CID 4387513.
  27. ^ Angelo, M; Singel, DJ; Stamler, JS (2006). "An S-nitrosothiol (SNO) synthase function of hemoglobin that utilizes nitrite as a substrate". Proc. Natl. Acad. Sci. USA. 103 (22): 8366–8371. Bibcode:2006PNAS..103.8366A. doi:10.1073/pnas.0600942103. PMC 1482500. PMID 16717191.
  28. ^ Stamler, JS; Hess, DT (2010). "Nascent Nitrosylases". Nature Cell Biology. 12 (11): 1024–1026. doi:10.1038/ncb1110-1024. PMID 20972426. S2CID 6508227.
  29. ^ Premont, RT; Singel, DJ; Stamler, JS (2022). "The enzymatic function of the honorary enzyme: S-nitrosylation of hemoglobin in physiology and medicine". Molecular Aspects of Medicine. 84: 101056. doi:10.1016/j.mam.2021.101056. PMC 8821404. PMID 34852941.
  30. ^ a b Seth, P; Hsieh, PN; Jamal, S; Wang, L; Gygi, SP; Jain, MK; Coller, J; Stamler, JS (2019-02-21). "Regulation of MicroRNA Machinery and Development by Interspecies S-Nitrosylation". Cell. 176 (5): 1014–1025. doi:10.1016/j.cell.2019.01.037. PMC 6559381. PMID 30794773.
  31. ^ a b Stamler, JS; Jia, L; Eu, JP; McMahon, TJ; Demchenko, IT; Bonaventura, J; Gernert, K; Piantadosi, CA (1997-06-27). "Blood flow regulation by S-nitrosohemoglobin in the physiological oxygen gradient". Science. 276 (5321): 2034–2037. doi:10.1126/science.276.5321.2034. PMID 9197264.
  32. ^ Zhang, R; Hess, DT; Qian, Z; Hausladen, A; Fonseca, F; Chaube, R; Reynolds, JD; Stamler, JS (2015-05-19). "Hemoglobin βCys93 is essential for cardiovascular function and integrated response to hypoxia". Proc Natl Acad Sci U S A. 112 (20): 6425–6430. Bibcode:2015PNAS..112.6425Z. doi:10.1073/pnas.1502285112. PMC 4443356. PMID 25810253.
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  35. ^ Pawloski, JR; Hess, DT; Stamler, JS (2005-02-15). "Impaired vasodilation by red blood cells in sickle cell disease". Proc Natl Acad Sci U S A. 102 (7): 2531–2536. Bibcode:2005PNAS..102.2531P. doi:10.1073/pnas.0409876102. PMC 548996. PMID 15699345.
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  37. ^ Reynolds, JD; Ahearn, GS; Angelo, M; Zhang, J; Cobb, F; Stamler, JS (October 2007). "S-nitrosohemoglobin deficiency: a mechanism for loss of physiological activity in banked blood". Proc Natl Acad Sci U S A. 104 (43): 17058–17062. Bibcode:2007PNAS..10417058R. doi:10.1073/pnas.0707958104. PMC 2040473. PMID 17940022.
  38. ^ Reynolds, JD; Bennett, KM; Cina, AJ; Diesen, DL; Henderson, MB; Matto, F; Plante, A; Williamson, RA; Zandinejad, K; Demchenko, IT; Hess, DT; Piantadosi, CA; Stamler, JS (2013-07-09). "S-nitrosylation therapy to improve oxygen delivery of banked blood". Proc Natl Acad Sci U S A. 110 (28): 11529–11534. Bibcode:2013PNAS..11011529R. doi:10.1073/pnas.1306489110. PMC 3710799. PMID 23798386.
  39. ^ Park, Alice (2007-10-08). "Why Banked Blood Goes Bad". Time. Retrieved 2019-01-11.[dead link‍]
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  44. ^ Gaston, B; Sears, S; Woods, J; Hunt, J; Ponaman, M; McMahon, T; Stamler, JS (1998-05-02). "Bronchodilator S-nitrosothiol deficiency in asthmatic respiratory failure". Lancet. 351 (9112): 1317–1319. doi:10.1016/S0140-6736(97)07485-0. PMID 9643794. S2CID 28776994.
  45. ^ Que, LG; Liu, L; Yan, Y; Whitehead, GS; Gavett, SH; Schwartz, DA; Stamler, JS (2005-06-10). "Protection from experimental asthma by an endogenous bronchodilator". Science. 308 (5728): 1618–1621. Bibcode:2005Sci...308.1618Q. doi:10.1126/science.1108228. PMC 2128762. PMID 15919956.
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  47. ^ Hayashi, H; Hess, DT; Zhang, R; Sugi, K; Gao, H; Tan, BL; Bowles, DE; Milano, CA; Jain, MK; Koch, WJ; Stamler, JS (2018-05-03). "S-Nitrosylation of β-Arrestins Biases Receptor Signaling and Confers Ligand Independence". Mol Cell. 70 (3): 473–487. doi:10.1016/j.molcel.2018.03.034. PMC 5940012. PMID 29727618.
  48. ^ "Heart disease severity may depend on nitric oxide levels". ScienceDaily. 2018-05-14. Retrieved 2019-01-11.
  49. ^ Qian, Q; Zhang, Z; Orwig, A; Chen, S; Ding, WX; Xu, Y; Kunz, RC; Lind, NRL; Stamler, JS; Yang, L (2018-02-01). "S-Nitrosoglutathione Reductase Dysfunction Contributes to Obesity-Associated Hepatic Insulin Resistance via Regulating Autophagy". Diabetes. 67 (2): 193–207. doi:10.2337/db17-0223. PMC 10515702. PMID 29074597.
  50. ^ Zhou, HL; Zhang, R; Anand, P; Stomberski, CT; Qian, Z; Hausladen, A; Wang, L; Rhee, EP; Parikh, SM; Karumanchi, SA; Stamler, JS (2019-01-10). "Metabolic reprogramming by the S-nitroso-CoA reductase system protects against kidney injury". Nature. 565 (7737): 96–100. Bibcode:2019Natur.565...96Z. doi:10.1038/s41586-018-0749-z. PMC 6318002. PMID 30487609.
  51. ^ "Re-programming the body's energy pathway boosts kidney self-repair". medicalexpress.com. Science X. 2018-11-28. Retrieved 2019-01-11.
  52. ^ de Jesús-Berríos M, Liu L, Nussbaum JC, Cox GM, Stamler JS, Heitman J (2003). "Enzymes that counteract nitrosative stress promote fungal virulence". Curr Biol. 13 (22): 1963–1968. Bibcode:2003CBio...13.1963D. doi:10.1016/j.cub.2003.10.029. PMID 14614821.
  53. ^ Elphinstone RE, Besla R, Shikatani EA, Lu Z, Hausladen A, Davies M, Robbins CS, Husain M, Stamler JS, Kain KC (2017). "S-Nitrosoglutathione Reductase Deficiency Confers Improved Survival and Neurological Outcome in Experimental Cerebral Malaria". Infect Immun. 85 (9): e00371-17. doi:10.1128/IAI.00371-17. PMC 5563579. PMID 28674030.
  54. ^ Hausladen, A; Gow, AJ; Stamler, JS (1998-11-24). "Nitrosative stress: metabolic pathway involving the flavohemoglobin". Proc Natl Acad Sci USA. 95 (24): 14100–14105. Bibcode:1998PNAS...9514100H. doi:10.1073/pnas.95.24.14100. PMC 24333. PMID 9826660.
  55. ^ Liu, L; Zeng, M; Hausladen, A; Heitman, J; Stamler, JS (2000-04-25). "Protection from nitrosative stress by yeast flavohemoglobin". Proc Natl Acad Sci USA. 97 (9): 4672–4676. Bibcode:2000PNAS...97.4672L. doi:10.1073/pnas.090083597. PMC 18291. PMID 10758168.
  56. ^ Minning, DM; Gow, AJ; Bonaventura, J; Braun, R; Dewhirst, M; Goldberg, DE; Stamler, JS (1999-09-30). "Ascaris haemoglobin is a nitric oxide-activated 'deoxygenase'". Nature. 401 (6752): 497–502. Bibcode:1999Natur.401..497M. doi:10.1038/46822. PMID 10519555. S2CID 3486708.
  57. ^ Blakeslee, Sandra (1999-10-05). "Thanks to a 'Horrible Worm,' New Ideas on Hemoglobin". The New York Times. Retrieved 2019-01-11.
  58. ^ Chen, Z; Zhang, J; Stamler, JS (2002-06-11). "Identification of the enzymatic mechanism of nitroglycerin bioactivation". Proc Natl Acad Sci USA. 99 (12): 8306–8311. doi:10.1073/pnas.122225199. PMC 123063. PMID 12048254.
  59. ^ "BioMotiv Launches Novel Drug Development Operation, Names Leadership Team". prnewswire.com/ (Press release). PR Newswire. Retrieved 2022-05-16.
  60. ^ "Foundation Fighting Blindness and Harrington Discovery Institute Partner to Accelerate Drug Development for Critical Causes of Blindness". prnewswire.com/ (Press release). PR Newswire. Retrieved 2022-05-16.
  61. ^ "ADDF-Harrington". harringtondiscovery.org/. Harrington Discovery Institute. Retrieved 2022-05-16.
  62. ^ "Fund For Cures UK". fundforcures.org.uk/. Harrington Discovery Institute. Retrieved 2022-05-16.
  63. ^ "Morgan Stanley GIFT Cures". harringtondiscovery.org/. Harrington Discovery Institute. Retrieved 2022-05-16.
  64. ^ "Morgan Stanley GIFT Cures". msgiftcures.donorgift.org/. Morgan Stanley. Retrieved 2022-05-16.
  65. ^ "New Morgan Stanley GIFT Cures Program to Advance Drug Discovery Research into Life-Saving and Life-Enhancing Cures and Treatments". morganstanley.com/. Morgan Stanley. Retrieved 2022-05-16.
  66. ^ "Advent Life Sciences starts impact fund". globalimpactventuring.com/. Global Impact Venturing. Retrieved 2022-05-16.
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