Wikipedia

Eva Neer

Eva Julia Neer (1937–2000) was an American physician (Columbia University P&S), biochemist, and cell-biology scientist who gained U.S. national research awards (FASEB, 1987; American Heart Association, 1996) for her discoveries on G-protein subunit structure and function. She described the physiological roles of these subunits as an integrated and versatile molecular system of signal transduction for membrane-receptor regulation of cell function. Her research concepts turned her into a world leader in G-protein studies and impinged widely on the general understanding of cell behavior.[1][2][3]

Eva Neer
Born
Eva Augenblick

1937
Warsaw, Poland
Died2000, age 62
Cambridge, Massachusetts
NationalityAmerican of Polish origin
EducationRadcliffe College, Columbia University
Known forG-protein subunit structure and function
SpouseRobert M. Neer
AwardsNational Academy of Sciences
Scientific career
FieldsBiochemist and cell-biologist
InstitutionsHarvard University

Biography

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Born Eva Augenblick in Warsaw, came to New York at age eight with her parents and grew up in Queens and Scarsdale.[4] Neer's family fled Warsaw at war's onset in 1939, emigrated first to Brazil, and soon after to the U.S.. In Warsaw, her father had practiced private corporate law, which he was unable to pursue in the US, but her parents inspired in Neer her love for scholarly endeavors.[2] She graduated with honors from Bronxville High School in 1955, being awarded a Regent’s college scholarship by the State Education Department.[5] Eva Augenblick attended Radcliffe College and graduated from Barnard College in 1959. A list of student acquaintances of hers at high school and college would include notable achievers such as economist Fischer Black, psychologist Robert L. Helmreich,[6] and endocrinologist Robert M. Neer[7] whom she married.[8] Neer graduated as a physician at Columbia University in 1963. Three years later, she joined Harvard University where she worked continuously for more than three decades. Neer has been singled out for her "efforts to help women advance up the academic ladder".[9] She died of complications from breast cancer in 2000, survived by her husband and two sons, Robert and Richard.[10] A personal account of Neer´s professional life was given by her close colleague David E. Clapham in an obituary note.[11]

Academic career

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Neer joined Harvard research staff in 1966. She was appointed Assistant Professor of Medicine in 1976, and full professor in 1991. She was ascribed to the Cardiology Division at Brigham and Women's Hospital. Neer served on the Board of Tutors in Biochemical Sciences at Harvard College, as well as on the Harvard Students Research Committee at the Harvard Medical School. She combined the tools of chemistry, biology, physics and molecular biology to explain how cells interpret the messages they get from light, hormones and neurotransmitters. The author of numerous papers, she was elected to both the U.S. National Academy of Sciences and the Institute of Medicine of the National Academy of Sciences and earned membership in the American Academy of Arts and Sciences and the Polish Institute of Arts and Sciences of America. She was honored with the FASEB prize for basic research in 1987 and the American Heart Association’s basic research prize in 1996. She was also an adviser to the National Institutes of Health.[1][2][3]

Research

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Neer's early research, performed under the guidance of Guido Guidotti,[12] was devoted to study aspects of hemoglobin chemistry. These included the role of sulfhydryl groups of α and β chains on the quaternary conformation of the molecule. She showed their importance in subunit interface interaction and functional cooperativity for oxygen binding. This binding is an essential property for oxygen transport in blood and is often referred as Bohr effect.[13]

While still at Guidotti's lab, Neer undertook independent research on the biochemical mechanisms of vasopressin's action on kidney's distal tubules. She described the purification and kinetic properties of vasopressin-sensitive adenylate cyclase from rat renal medulla.[14] It would be later shown that vasopressin[15] acts through a G protein-coupled receptor. This was the topic of Neer's work for most of her research career.

In order to dissect out different aspects of G protein messaging complexities Neer studied a variety of tissues including brain cortex, rat testis, pigeon erythrocytes, heart, brain, retina-rods. Some of her most cited research findings include:

  • Purification and properties of free and membrane-bound adenylate cyclase (1978)[16]
  • Size and detergent binding of adenylate cyclase from bovine cerebral cortex (1978)[17]
  • The site of α-chymotryptic activation of pigeon erythrocyte adenylate cyclase (1978)[18]
  • Calmodulin activates the isolated catalytic unit of brain adenylate cyclase (1981)[19]
  • Location and function of reactive sulfhydryl groups of α subunit 39 (1987)[20]
  • Action of G protein subunits on the cardiac muscarinic K+ channel (1987, 1988)[21][22]
  • Cloning and differential expression of α-subunit types in human tissues and cell types (1988)[23]
  • G-protein αs and αo synthesis in GH3 cells (1996)[24]
  • Structure-function aspects of activation of PLC by G protein subunits: site mutation studies. (1998)[25][26]

During the course of her career Neer authored a number of highly cited review articles on structural and functional aspects of G protein and its subunits. [27][28][29][30][31]

Awards and honors

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References

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  1. ^ a b "Professor of Medicine Eva J. Neer Dies at 62". Harvard Gazette. 2 March 2000. Retrieved 27 September 2017.
  2. ^ a b c "Remembering Dr. Eva Neer, read at the Faculty of Medicine meeting on Dec. 18, 2002". Harvard Gazette. 6 March 2003. Archived from the original on 2 January 2014. Retrieved 2 January 2014.
  3. ^ a b "Dr. Eva J. Neer, in memorial". BioMolecular Engineering Research Center. 21 February 2000. Archived from the original on 2 January 2014. Retrieved 2 January 2014.
  4. ^ Saxon, Wolfgang (26 February 2000). "Eva Julia Neer, 62, Biochemist Known for Work With Proteins". The New York Times. Retrieved 2 January 2014.
  5. ^ "HS,Yonkers,N.Y,May 13, 1955". Archives of the Yonkers NY Herald Statesman. Fultonhistory.com. Retrieved 2 January 2014.
  6. ^ [1][dead link‍]
  7. ^ "Dr. Robert M. Neer, MD - Boston, MA - Internal Medicine | Healthgrades.com". Archived from the original on 2 January 2014. Retrieved 2 January 2014.
  8. ^ Mehrling, Perry. "Fischer Black and the Revolutionary Idea of Finance". Dmmserver.com. Archived from the original on 4 March 2016. Retrieved 2 January 2014.
  9. ^ "Professor of Medicine Eva J. Neer Dies at 62". Archived from the original on 2 January 2014. Retrieved 1 January 2014.
  10. ^ "Eva Julia Neer, 62, Biochemist, Heart Researcher". Chicago Tribune. 28 February 2000. Retrieved 2 January 2014.
  11. ^ Clapham, David E. (2000). "Remembering Eva Neer". Cell. 101 (3): 247–248. doi:10.1016/S0092-8674(02)71135-5.
  12. ^ "Guido Guidotti". Molecular & Cellular Biology - Harvard University. Archived from the original on 15 November 2016. Retrieved 2 January 2014.
  13. ^ Neer, EJ; Guidotti, G (1970). "The recombination of α and β chains of human hemoglobin. Effect of sulfhydryl group modifications". J. Biol. Chem. 245 (3): 570–3. doi:10.1016/S0021-9258(18)63370-8. PMID 5412713.
  14. ^ Neer, EJ (1973). "The vasopressin-sensitive adenylate cyclase of the rat renal medulla". J. Biol. Chem. 248 (13): 4775–81. doi:10.1016/S0021-9258(19)43732-0. PMID 4352409.
  15. ^ Prat, AG; Ausiello, DA; Cantiello, HF (1993). "Vasopressin and protein kinase A activate G protein-sensitive epithelial Na+ channels". American Journal of Physiology. Cell Physiology. 265 (1 Pt 1): C218–23. doi:10.1152/ajpcell.1993.265.1.C218. PMID 8393279.
  16. ^ Neer, EJ (1978). "Physical and functional properties of adenylate cyclase from mature rat testis". J. Biol. Chem. 253 (16): 5808–12. doi:10.1016/S0021-9258(17)30340-X. PMID 670231.
  17. ^ Neer, EJ (1978). "Size and detergent binding of adenylate cyclase from bovine cerebral cortex". J. Biol. Chem. 253 (5): 1498–502. doi:10.1016/S0021-9258(17)34894-9. PMID 627551.
  18. ^ Marshak, DR; Neer, EJ (1980). "The site of α-chymotryptic activation of pigeon erythrocyte adenylate cyclase". J. Biol. Chem. 255 (10): 4781–5. doi:10.1016/S0021-9258(19)85565-5. PMID 7372611.
  19. ^ Salter, RS; Krinks, MH; Klee, CB; Neer, EJ (1981). "Calmodulin activates the isolated catalytic unit of brain adenylate cyclase". J. Biol. Chem. 256 (19): 9830–3. doi:10.1016/S0021-9258(19)68703-X. PMID 6268633.
  20. ^ Winslow, JW; Bradley, JD; Smith, JA; Neer, EJ (1987). "Reactive sulfhydryl groups of α39, a guanine nucleotide-binding protein from brain. Location and function". J. Biol. Chem. 262 (10): 4501–7. doi:10.1016/S0021-9258(18)61220-7. PMID 3104318.
  21. ^ Logothetis, DE; Kurachi, Y; Galper, J; Neer, EJ; Clapham, DE (1987). "The βγ subunits of GTP-binding proteins activate the muscarinic K+ channel in heart". Nature. 325 (6102): 321–6. Bibcode:1987Natur.325..321L. doi:10.1038/325321a0. PMID 2433589. S2CID 4338529.
  22. ^ Logothetis, DE; Kim, DH; Northup, JK; Neer, EJ; Clapham, DE (1988). "Specificity of action of guanine nucleotide-binding regulatory protein subunits on the cardiac muscarinic K+ channel". Proc. Natl. Acad. Sci. USA. 85 (16): 5814–8. Bibcode:1988PNAS...85.5814L. doi:10.1073/pnas.85.16.5814. PMC 281855. PMID 2457901.
  23. ^ Kim, SY; Ang, SL; Bloch, DB; Bloch, KD; Kawahara, Y; Tolman, C; Lee, R; Seidman, JG; Neer, EJ (1988). "Identification of cDNA encoding an additional α subunit of a human GTP-binding protein: expression of three αi subtypes in human tissues and cell lines". Proc. Natl. Acad. Sci. USA. 85 (12): 4153–4257. Bibcode:1988PNAS...85.4153K. doi:10.1073/pnas.85.12.4153. PMC 280384. PMID 3132707.
  24. ^ Li, Y; Mende, U; Lewis, C; Neer, EJ (1996). "Maintenance of cellular levels of G-proteins: different efficiencies of αs and αo synthesis in GH3 cells". Biochem. J. 318 (Pt 3): 1071–7. doi:10.1042/bj3181071. PMC 1217725. PMID 8836158.
  25. ^ Panchenko, MP; Saxena, K; Li, Y; Charnecki, S; Sternweis, PM; Smith, TF; Gilman, AG; Kozasa, T; Neer, EJ (23 October 1998). "Sites important for PLCβ2 activation by the G Protein βγ subunit map to the sides of the β propeller structure". J. Biol. Chem. 273 (43): 28298–304. doi:10.1074/jbc.273.43.28298. PMID 9774453.
  26. ^ Li, Y; Sternweis, PM; Charnecki, S; Smith, TF; Gilman, AG; Neer, EJ; Kozasa, T (1998). "Sites for Gα binding on the G protein β subunit overlap with sites for regulation of phospholipase Cβ and adenylyl cyclase". J. Biol. Chem. 273 (26): 16265–72. doi:10.1074/jbc.273.26.16265. PMID 9632686.
  27. ^ Neer, EJ (1990). "Structural and functional studies of the Go protein". Soc. Gen. Physiol. Series. 45: 143–51. PMID 2116036.
  28. ^ Clapham, DE; Neer, EJ (1993). "New roles for G-protein beta gamma-dimers in transmembrane signalling". Nature. 365 (6445): 403–6. Bibcode:1993Natur.365..403C. doi:10.1038/365403a0. PMID 8413584. S2CID 4245662.
  29. ^ Neer, EJ (1995). "Heterotrimeric G proteins: organizers of transmembrane signals". Cell. 80 (2): 249–57. doi:10.1016/0092-8674(95)90407-7. PMID 7834744. S2CID 10095565.
  30. ^ Neer, EJ; Clapham, DE (1988). "Roles of G protein subunits in transmembrane signalling". Nature. 333 (6169): 129–34. Bibcode:1988Natur.333..129N. doi:10.1038/333129a0. PMID 3130578. S2CID 4256130.
  31. ^ Clapham, D. E.; Neer, E. J. (1997). "G protein βγ subunits". Annu. Rev. Pharmacol. Toxicol. 37: 167–203. doi:10.1146/annurev.pharmtox.37.1.167. PMID 9131251. Archived from the original on 13 July 2020. Retrieved 1 January 2014.
  32. ^ "Damon Runyon Fellows + Grantees (by award year): '70s". Damon Runyon Cancer Research Foundation. Archived from the original on 2 January 2014. Retrieved 2 January 2014.
  33. ^ "The M.D.-Ph.D. Program at Harvard Medical School". Archived from the original on 2 February 2014. Retrieved 23 January 2014.
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