Rajendra Kumar Sharma | |
---|---|
![]() | |
Born | |
Education | D.Sc. in pathology, Ph.D. in biochemistry |
Alma mater | |
Occupation(s) | Professor, research scientist |
Years active | Since 1970 |
Employer | University of Saskatchewan |
Known for | Calmodulin regulated systems and myristoylation of cellular proteins |
Awards |
Rajendra Kumar Sharma SOM FRSA (born 2 January 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.
Rajendra Sharma, the son of Venkateswar Sharma and Durga Devi Sharma, was born on 2 January 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.[ citation needed ]
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]
The City of Saskatoon, Saskatchewan, named four streets in Aspen Ridge in recognition of Sharma's scholarly contributions to science and research. [31]
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.
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.
Alfred Goodman Gilman was an American pharmacologist and biochemist. He and Martin Rodbell shared the 1994 Nobel Prize in Physiology or Medicine "for their discovery of G-proteins and the role of these proteins in signal transduction in cells."
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.
Phosphodiesterase 1, PDE1, EC 3.1.4.1, systematic name oligonucleotide 5′-nucleotidohydrolase) is a phosphodiesterase enzyme also known as calcium- and calmodulin-dependent phosphodiesterase. It is one of the 11 families of phosphodiesterase (PDE1-PDE11). Phosphodiesterase 1 has three subtypes, PDE1A, PDE1B and PDE1C which divide further into various isoforms. The various isoforms exhibit different affinities for cAMP and cGMP.
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.
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.
Calmodulin 3 is a protein that in humans is encoded by the CALM3 gene.
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.
cAMP-dependent protein kinase type II-alpha regulatory subunit is an enzyme that in humans is encoded by the PRKAR2A gene.
Sphingomyelin phosphodiesterase 1 (SMPD1), also known as acid sphingomyelinase (ASM), is an enzyme that in humans is encoded by the SMPD1 gene.
Plasma membrane calcium-transporting ATPase 4 is an enzyme that in humans is encoded by the ATP2B4 gene.
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.
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.
cAMP-specific 3',5'-cyclic phosphodiesterase 4B is an enzyme that in humans is encoded by the PDE4B gene.
Adenylyl cyclase type 8 is an enzyme that in humans is encoded by the ADCY8 gene.
Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B is an enzyme that in humans is encoded by the PDE1B gene.
2′,3′-Cyclic-nucleotide 3'-phosphodiesterase is an enzyme that in humans is encoded by the CNP gene.
Benjamin Weiss is an American neuropharmacologist, Emeritus Professor of Pharmacology and Physiology at Drexel University College of Medicine. He is best known for his work with cyclic nucleotide phosphodiesterases. He was the first to propose, based on his experimental work, that selective inhibition of phosphodiesterases which are expressed differentially in all tissues, could be used as a target for drug development. His work is the basis for many marketed and developmental human drugs that selectively inhibit cyclic nucleotide phosphodiesterases.
George Stark is an American chemist and biochemist. His research interests include protein and enzyme function and modification, interferons and cytokines, signal transduction, and gene expression.
{{cite web}}
: CS1 maint: multiple names: authors list (link)