Rajendra Kumar Sharma

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Rajendra Kumar Sharma

Photo of Rajendra Kumar Sharma.jpg
Born (1942-01-02) January 2, 1942 (age 81)
EducationD.Sc. in pathology, Ph.D. in biochemistry
Alma mater
Occupation(s)Professor, research scientist
Years activeSince 1970
Employer University of Saskatchewan
Known forCalmodulin regulated systems and myristoylation of cellular proteins
Awards

Rajendra Kumar Sharma SOM FRSA (born January 2, 1942) is a professor at the Department of Pathology and Laboratory Medicine, University of Saskatchewan College of Medicine. [1] He holds an earned Doctor of Science from the University of Saskatchewan, [2] and was elected a Fellow of the Royal Society of the Arts (FRSA) in 2014. [3] His contributions to research have been documented in the Encyclopedia of Saskatchewan – A Living Legacy. [4] Sharma has made several discoveries in the areas of colorectal cancer and the cardiovascular system.

Contents

Biography

Rajendra Sharma, the son of Venkateswar Sharma and Durga Devi Sharma, was born on January 2, 1942, in Hathras, Uttar Pradesh, India. He spent his childhood in Hathras where he studied primary education at Mohan Gunj Primary Municipality School and higher secondary education at Saraswati Inter College. Sharma completed his B.Sc. in Chemistry, Botany and Zoology in 1963 and M.Sc. in Biochemistry in 1965 from Aligarh Muslim University. He served as a chemistry lecturer at Saraswati Inter College due to the shortage of chemistry teachers during 1965. He was awarded a research fellowship from the Council of Scientific and Industrial Research (CSIR) to pursue a Ph.D. degree in Biochemistry at the All India Institute of Medical Sciences (AIIMS), New Delhi, where he worked in the area of protein chemistry and enzymology. His Ph.D. research work was published in the Journal of Biological Chemistry. [5] After completing his Ph.D., Sharma worked as a lecturer at the Department of Biochemistry, Lady Hardinge Medical College & Hospital, New Delhi.

Sharma married Manjul Saraswat in 1970; they have three daughters, Priya, Puja and Poonam.

Scientific career

Sharma pursued his postdoctoral research in the field of cancer biology in 1972 in the Department of Biochemistry & Pharmacology, Tufts University School of Medicine, Boston, Massachusetts, US. [6] [7] In 1975, he joined the College of Medicine, University of South Alabama, as a research associate in the Department of Biochemistry. In 1976 he joined the Department of Biochemistry, Faculty of Medicine, University of Manitoba, in Winnipeg to pursue his further research career. [8] [9] Later he moved to the Department of Medical Biochemistry, University of Calgary, Alberta and made several discoveries in the areas of signal transduction. [10] [11] [12] [13] In 1991, Sharma joined as an associate professor at the Department of Pathology & Laboratory Medicine, College of Medicine, University of Saskatchewan, Saskatoon. In the year 2012, Sharma was awarded the title of a Distinguished Professor at the University of Saskatchewan [14] [15] and he continues to serve at the same position to date. [16]

Sharma's research was primarily focused in the areas of calmodulin-regulated systems [17] and myristoylation of cellular proteins. [18] He was the first to report the role of N-myrstoyltransferase in colorectal cancer, [19] which was highlighted in the Journal of the National Cancer Institute. [20] His extensive research studies led to the identification of N-myrstoyltransferase as a potential biomarker in colorectal cancer patients. [21] This discovery was licensed for the development of a diagnostic tool to detect colorectal cancer. [22] Sharma's research has resulted in the identification and characterization of several proteins from various species related to colorectal cancer and cardiovascular system that has led to 265 full-length publications in reputed journals to his credit. [23] Sharma has also co-edited a book on signal transduction mechanisms. [24] He is also currently serving as the Editor-In-Chief of a peer-reviewed international scientific journal entitled "Journal of Molecular Biology & Therapeutics". [25] Recently an article on his decades of dedication to research was published in OCN (ON CAMPUS NEWS) at the University of Saskatchewan. [26]

Recognitions

The City of Saskatoon, Saskatchewan, named four streets in Aspen Ridge in recognition of Sharma's scholarly contributions to science and research. [31]

Related Research Articles

<span class="mw-page-title-main">Phosphodiesterase</span> Class of enzymes

A phosphodiesterase (PDE) is an enzyme that breaks a phosphodiester bond. Usually, phosphodiesterase refers to cyclic nucleotide phosphodiesterases, which have great clinical significance and are described below. However, there are many other families of phosphodiesterases, including phospholipases C and D, autotaxin, sphingomyelin phosphodiesterase, DNases, RNases, and restriction endonucleases, as well as numerous less-well-characterized small-molecule phosphodiesterases.

<span class="mw-page-title-main">Transducin</span>

Transducin (Gt) is a protein naturally expressed in vertebrate retina rods and cones and it is very important in vertebrate phototransduction. It is a type of heterotrimeric G-protein with different α subunits in rod and cone photoreceptors.

<span class="mw-page-title-main">Alfred G. Gilman</span> American pharmacologist

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<span class="mw-page-title-main">Glycogen phosphorylase</span> Class of enzymes

Glycogen phosphorylase is one of the phosphorylase enzymes. Glycogen phosphorylase catalyzes the rate-limiting step in glycogenolysis in animals by releasing glucose-1-phosphate from the terminal alpha-1,4-glycosidic bond. Glycogen phosphorylase is also studied as a model protein regulated by both reversible phosphorylation and allosteric effects.

<span class="mw-page-title-main">PRKACA</span> Protein-coding gene in the species Homo sapiens

The catalytic subunit α of protein kinase A is a key regulatory enzyme that in humans is encoded by the PRKACA gene. This enzyme is responsible for phosphorylating other proteins and substrates, changing their activity. Protein kinase A catalytic subunit is a member of the AGC kinase family, and contributes to the control of cellular processes that include glucose metabolism, cell division, and contextual memory. PKA Cα is part of a larger protein complex that is responsible for controlling when and where proteins are phosphorylated. Defective regulation of PKA holoenzyme activity has been linked to the progression of cardiovascular disease, certain endocrine disorders and cancers.

<span class="mw-page-title-main">Calcium/calmodulin-dependent protein kinase type II subunit alpha</span> Protein-coding gene in the species Homo sapiens

Calcium/calmodulin-dependent protein kinase type II subunit alpha (CAMKIIα), a.k.a.Ca2+/calmodulin-dependent protein kinase II alpha, is one subunit of CamKII, a protein kinase (i.e., an enzyme which phosphorylates proteins) that in humans is encoded by the CAMK2A gene.

<span class="mw-page-title-main">CALM3</span> Protein-coding gene in the species Homo sapiens

Calmodulin 3 is a protein that in humans is encoded by the CALM3 gene.

<span class="mw-page-title-main">CALM2</span> Protein-coding gene in the species Homo sapiens

Calmodulin 2 is a protein that in humans is encoded by the CALM2 gene. A member of the calmodulin family of signaling molecules, it is an intermediary between calcium ions, which act as a second messenger, and many intracellular processes, such as the contraction of cardiac muscle.

<span class="mw-page-title-main">PRKAR2A</span> Protein-coding gene in the species Homo sapiens

cAMP-dependent protein kinase type II-alpha regulatory subunit is an enzyme that in humans is encoded by the PRKAR2A gene.

<span class="mw-page-title-main">AKR1B1</span> Protein-coding gene in the species Homo sapiens

Aldo-keto reductase family 1, member B1 (AKR1B1), also known as aldose reductase, is an enzyme that is encoded by the AKR1B1 gene in humans. It is a reduced nicotinamide-adenine dinucleotide phosphate (NADPH)-dependent enzyme catalyzing the reduction of various aldehydes and ketones to the corresponding alcohol. The involvement of AKR1B1 in oxidative stress diseases, cell signal transduction, and cell proliferation process endows AKR1B1 with potential as a therapeutic target.

<span class="mw-page-title-main">ATP2B4</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">MARCKS</span> Protein-coding gene in the species Homo sapiens

Myristoylated alanine-rich C-kinase substrate is a protein that in humans is encoded by the MARCKS gene. It plays important roles in cell shape, cell motility, secretion, transmembrane transport, regulation of the cell cycle, and neural development. Recently, MARCKS has been implicated in the exocytosis of a number of vesicles and granules such as mucin and chromaffin. It is also the name of a protein family, of which MARCKS is the most studied member. They are intrinsically disordered proteins, with an acidic pH, with high proportions of alanine, glycine, proline, and glutamic acid. They are membrane-bound through a lipid anchor at the N-terminus, and a polybasic domain in the middle. They are regulated by Ca2+/calmodulin and protein kinase C. In their unphosphorylated form, they bind to actin filaments, causing them to crosslink, and sequester acidic membrane phospholipids such as PIP2.

<span class="mw-page-title-main">LAMP1</span> Protein-coding gene in the species Homo sapiens

Lysosomal-associated membrane protein 1 (LAMP-1) also known as lysosome-associated membrane glycoprotein 1 and CD107a, is a protein that in humans is encoded by the LAMP1 gene. The human LAMP1 gene is located on the long arm (q) of chromosome 13 at region 3, band 4 (13q34).

<span class="mw-page-title-main">ATP2B1</span> Protein-coding gene in the species Homo sapiens

Plasma membrane calcium-transporting ATPase 1 also known as Plasma membrane calcium pump isoform 1 is a plasma membrane Ca2+
ATPase
, an enzyme that in humans is encoded by the ATP2B1 gene. It's a transport protein, a translocase, a calcium pump EC 7.2.2.10.

<span class="mw-page-title-main">PDE4B</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">ADCY8</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">PDE1B</span> Protein-coding gene in the species Homo sapiens

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References

  1. "Rajendra Sharma - College of Medicine, University of Saskatchewan". medicine.usask.ca. Retrieved January 15, 2018.
  2. "Past recipients of earned degrees - College of Graduate and Postdoctoral Studies, University of Saskatchewan". www.usask.ca. Retrieved January 15, 2018.
  3. RSA. "Find a Fellow - RSA". www.thersa.org. Retrieved January 15, 2018.
  4. THE ENCYCLOPEDIA OF SASKATCHEWAN a Living Legacy. Regina: Canadian Plains Research Center. 2005.
  5. Mazumder, Rajarshi; Sharma, Rajendra K. (1970). "Purification, Properties, and Feedback Control of l-Threonine Dehydratase from Spinach". Journal of Biological Chemistry. 245 (11): 3008–3014. doi: 10.1016/S0021-9258(18)63089-3 . PMID   5423384.
  6. Sharma, Rajendra K.; Kisliuk, Roy L.; Verma, Surendra P.; Wallach, Donald F.H. (1975). "Study of thymidylate synthetase-function by laser Raman spectroscopy". Biochimica et Biophysica Acta (BBA) - Enzymology. 391 (1): 19–27. doi:10.1016/0005-2744(75)90148-5. ISSN   0005-2744. PMID   806300.
  7. Sharma, R.K.; Kisliuk, R.L. (1975). "Quenching of thymidylate synthetases fluorescence by substrate analogs". Biochem Biophys Res Commun. 64 (2): 648–655. doi:10.1016/0006-291X(75)90370-8. PMID   125086.
  8. Sharma, RK; Wirch, E; Wang, JH (May 25, 1978). "Inhibition of Ca2+-activated cyclic nucleotide phosphodiesterase reaction by a heat-stable inhibitor protein from bovine brain". The Journal of Biological Chemistry. 253 (10): 3575–80. doi: 10.1016/S0021-9258(17)34840-8 . PMID   206547.
  9. Sharma, RK; Tam, SW; Waisman, DM; Wang, JH (December 10, 1980). "Differential interaction of rabbit skeletal muscle phosphorylase kinase isozymes with calmodulin". The Journal of Biological Chemistry. 255 (23): 11102–3. doi: 10.1016/S0021-9258(19)70260-9 . PMID   6777374.
  10. Huang, C. Y.; Chau, V.; Chock, P. B.; Wang, J. H.; Sharma, R. K. (1982). "Mechanism of activation of cyclic nucleotide phosphodiesterase: requirement of the binding of four Ca2+ to calmodulin for activation". Proc Natl Acad Sci USA. 78 (2): 874–876. doi: 10.1073/pnas.78.2.871 . PMC   319905 . PMID   6262778.
  11. Sharma, R. K.; Adachi, A. M.; Adachi, K.; Wang, J. H. (1984). "Demonstration of bovine brain calmodulin dependent cyclic nucleotide phosphodiesterase isozymes by monoclonal antibodies". J Biol Chem. 259 (14): 9248–9254. doi: 10.1016/S0021-9258(17)47292-9 . PMID   6086630.
  12. Sharma, R. K.; Wang, J. H. (1985). "Differential regulation of bovine brain calmodulin dependent cyclic nucleotide phosphodiesterase isozyme by cyclic AMP-dependent protein kinase and calmodulin-dependent phosphatase". Proc Natl Acad Sci USA. 82 (9): 2603–2607. Bibcode:1985PNAS...82.2603S. doi: 10.1073/pnas.82.9.2603 . PMC   397612 . PMID   2986124.
  13. Sharma, R. K. (1990). "Purification and characterization of novel calmodulin binding protein from cardiac muscle". J Biol Chem. 265 (2): 1152–7. doi: 10.1016/S0021-9258(19)40171-3 . PMID   2295605.
  14. "Distinguished Professorship Program".
  15. "Distinguished Professorship Recipients" (PDF).
  16. "Distinguished Professor".
  17. Parameswaran, S; Sharma, RK (August 2012). "High molecular weight calmodulin-binding protein: 20 years onwards-a potential therapeutic calpain inhibitor". Cardiovascular Drugs and Therapy. 26 (4): 321–30. doi:10.1007/s10557-012-6399-8. PMID   22588788. S2CID   22528531.
  18. Selvakumar, P; Lakshmikuttyamma, A; Shrivastav, A; Das, SB; Dimmock, JR; Sharma, RK (January 2007). "Potential role of N-myristoyltransferase in cancer". Progress in Lipid Research. 46 (1): 1–36. doi:10.1016/j.plipres.2006.05.002. PMID   16846646.
  19. Magnuson, B. A.; Raju, R. V. S.; Moyana, T. N.; Sharma, R. K. (1995). "Increased N -Myristoyltransferase Activity Observed in Rat and Human Colonic Tumors". J. Natl. Cancer Inst. 87 (21): 1630–1635. doi:10.1093/jnci/87.21.1630. PMID   7563206.
  20. Felsted, R. L.; Glover, C. J.; Hartman, K. (1995). "Protein N-Myristoylation as a Chemotherapeutic Target for Cancer". J. Natl. Cancer Inst. 87 (21): 1571–1573. doi: 10.1093/jnci/87.21.1571 . PMID   7563194.
  21. Shrivastav, Anuraag; Varma, Shailly; Saxena, Anurag; Decoteau, John; Sharma, Rajendra K. (2007). "N-myristoyltransferase: A potential novel diagnostic marker for colon cancer". J. Transl. Med. 5: 58. doi: 10.1186/1479-5876-5-58 . PMC   2203986 . PMID   18021392.
  22. Sharma, R.K. and Shrivastav, A. "Use of N-myristoyltransferase on non-tumor tissue for cancer diagnosis" . Retrieved May 15, 2018.{{cite web}}: CS1 maint: multiple names: authors list (link)
  23. "Rajenda K. Sharma - Google Scholar Citations". scholar.google.ca.
  24. Barnes, Junor A; Coore, Haldane G; Mohammed, Abdul H; Sharma, Rajendra K, eds. (1995). Signal Transduction Mechanisms. Developments in Molecular and Cellular Biochemistry. Springer. doi:10.1007/978-1-4615-2015-3. ISBN   9780792336631. S2CID   26525644 . Retrieved May 15, 2018.
  25. "Journal of Molecular Biology & Therapeutics | Innova Publications". innovapublications.com. Retrieved August 20, 2019.
  26. "Celebrating Sharma's record of research". News. Retrieved August 20, 2019.
  27. "Saskatchewan Order of Merit | Saskatchewan Heritage, Honours, and Awards | Government of Saskatchewan". Government of Saskatchewan. Retrieved January 15, 2018.
  28. "On Campus News". news.usask.ca. Retrieved January 15, 2018.
  29. "Rajendra Sharma, S.O.M., Ph.D., D.Sc. | The Governor General of Canada". Office of the Governor General of Canada. Retrieved November 15, 2018.
  30. RSA. "Find a Fellow - RSA". www.thersa.org. Retrieved January 15, 2018.
  31. "ASPEN RIDGE NEIGHBOURHOOD CONCEPT PLAN".