Dr. Arthur Edelman NA
Pharmacology And Toxicology
Associate Professor
521 Biomedical Research Building
102 Farber Hall (mail address)
SUNY at Buffalo, School of Medicine and Biomedical Sciences
Buffalo NY, 14214
Phone: (716) 829-3491
Fax: (716) 829-2801
Email: aedelman@buffalo.edu

View map


DESCRIPTION OF INTERESTS

Protein phosphorylation is an essential mechanism by which intercellular signals regulate specific intracellular events. Consequently protein kinases, the enzymes catalyzing protein phosphorylation reactions, represent a major superfamily of genes, collectively representing 2% of the protein coding potential of the human genome. Current projects in Dr. Edelman‘s lab are devoted to the role of protein kinases in neuronal development and in specific types of cancer. These projects utilize a wide range of techniques and involve, in the case of the latter project, a collaboration with investigators at Roswell Park Cancer Institute to develop a protein kinase-targeted therapy for prostate cancer.


SPECIALTIES

Molecular and Cellular Biology
Neurobiology
Regulation of gene expression
Signal Transduction


EDUCATION

1978 Ph.D., Neuro- and Biobehavioral- Sciences
Stanford University
1968 Bachelor of Arts, Psychology
University of California at Berkeley


EXPERTISE

Mechanisms of intracellular regulation
gene regulation, quantitative PCR, protein chemistry, immunocytochemistry, gene cloning and expression, signaling pathway analysis


PUBLICATIONS

Abbott, M.J., Edelman A.M., Turcotte, L.P.; CaMKK is an upstream signal of AMP-activated protein kinase in the regulation of substrate metabolism in contracting skeletal muscle; Am. J. Physiol.; 2009 Dec; 297; R1724-R1732
Feliciano, D.M., Edelman A.M.; Repression of Ca2 /Calmodulin-dependent protein kinase IV signaling accelerates retinoic Acid-induced differentiation of human neuroblastoma cells; J Biol Chem; 2009 Sep; 284; 26466-26481
Hawley, S.A., Pan, D.A., Mustard, K.J. Ross, L. Bain, J., Edelman, A.M., Frenguelli, B.G. and Hardie, D. G.; Calmodulin-dependent protein kinase kinase-β is an alternative upstream kinase for AMP-activated protein kinase; Cell Metabolism; 2005 Jul; 2(1); 9-19
Edelman AM, Kim WY, Higgins D, Goldstein EG, Oberdoerster M, Sigurdson W; Doublecortin kinase-2, a novel doublecortin-related protein kinase associated with terminal segments of axons and dendrites.; J Biol Chem; 2005 Mar; 280(9); 8531-8543
Qin, H., Raught, B., Sonenberg, N., Goldstein E.G. and Edelman, A.M.; Phosphorylation screening identifies translational initiation factor 4GII as an intracellular target of Ca2+/calmodulin-dependent protein kinase I; J. Biol. Chem.; 2003 Sep;
Shang L, Kwon YG, Nandy S, Lawrence DS, Edelman AM; Catalytic and regulatory domains of doublecortin kinase-1.; Biochemistry; 2003 Feb; 42(7); 2185-2194
Anderson KA, Means RL, Huang QH, Kemp BE, Goldstein EG, Selbert MA, Edelman AM, Fremeau RT, Means AR; Components of a calmodulin-dependent protein kinase cascade. Molecular cloning, functional characterization and cellular localization of Ca2+/calmodulin-dependent protein kinase kinase beta.; J Biol Chem; 1998 Nov; 273(48); 31880-31889
White RR, Kwon YG, Taing M, Lawrence DS, Edelman AM; Definition of optimal substrate recognition motifs of Ca2+-calmodulin-dependent protein kinases IV and II reveals shared and distinctive features.; J Biol Chem; 1998 Feb; 273(6); 3166-3172
Aletta JM, Selbert MA, Nairn AC, Edelman AM; Activation of a calcium-calmodulin-dependent protein kinase I cascade in PC12 cells.; J Biol Chem; 1996 Aug; 271(34); 20930-20934
Edelman AM, Mitchelhill KI, Selbert MA, Anderson KA, Hook SS, Stapleton D, Goldstein EG, Means AR, Kemp BE; Multiple Ca(2+)-calmodulin-dependent protein kinase kinases from rat brain. Purification, regulation by Ca(2+)-calmodulin, and partial amino acid sequence.; J Biol Chem; 1996 May; 271(18); 10806-10810
Hawley SA, Selbert MA, Goldstein EG, Edelman AM, Carling D, Hardie DG; 5‘-AMP activates the AMP-activated protein kinase cascade, and Ca2+/calmodulin activates the calmodulin-dependent protein kinase I cascade, via three independent mechanisms.; J Biol Chem; 1995 Nov; 270(45); 27186-27191
Haribabu B, Hook SS, Selbert MA, Goldstein EG, Tomhave ED, Edelman AM, Snyderman R, Means AR; Human calcium-calmodulin dependent protein kinase I: cDNA cloning, domain structure and activation by phosphorylation at threonine-177 by calcium-calmodulin dependent protein kinase I kinase.; EMBO J; 1995 Aug; 14(15); 3679-3686
Selbert MA, Anderson KA, Huang QH, Goldstein EG, Means AR, Edelman AM; Phosphorylation and activation of Ca(2+)-calmodulin-dependent protein kinase IV by Ca(2+)-calmodulin-dependent protein kinase Ia kinase. Phosphorylation of threonine 196 is essential for activation.; J Biol Chem; 1995 Jul; 270(29); 17616-17621
Lee JC, Edelman AM; Activation of Ca(2+)-calmodulin-dependent protein kinase Ia is due to direct phosphorylation by its activator.; Biochem Biophys Res Commun; 1995 May; 210(2); 631-637
Dale S, Wilson WA, Edelman AM, Hardie DG; Similar substrate recognition motifs for mammalian AMP-activated protein kinase, higher plant HMG-CoA reductase kinase-A, yeast SNF1, and mammalian calmodulin-dependent protein kinase I.; FEBS Lett; 1995 Mar; 361(2-3); 191-195
Arthur Edelman, Angus C. Nairn; Calcium-Calmodulin-Dependent Protein Kinase I; The Protein Kinase Factsbook; 1995 Jan;
Lee JC, Kwon YG, Lawrence DS, Edelman AM; A requirement of hydrophobic and basic amino acid residues for substrate recognition by Ca2+/calmodulin-dependent protein kinase Ia.; Proc Natl Acad Sci U S A; 1994 Jul; 91(14); 6413-6417
Lee JC, Edelman AM; A protein activator of Ca(2+)-calmodulin-dependent protein kinase Ia.; J Biol Chem; 1994 Jan; 269(3); 2158-2164
Peter J. Kennelly, Arthur Edelman; General Introduction to Protein Serine-Threonine Kinases; Design of Enzyme Inhibitors as Drugs; 1994 Jan; 2; 65-74
Rabin RA, Edelman AM, Wagner JA; Activation of protein kinase A is necessary but not sufficient for ethanol-induced desensitization of cyclic AMP production.; J Pharmacol Exp Ther; 1992 Jul; 262(1); 257-262
DeRemer MF, Saeli RJ, Edelman AM; Ca(2+)-calmodulin-dependent protein kinases Ia and Ib from rat brain I. Identification, purification, and structural comparisons.; J Biol Chem; 1992 Jul; 267(19); 13460-13465
DeRemer MF, Saeli RJ, Brautigan DL, Edelman AM; Ca(2+)-calmodulin-dependent protein kinases Ia and Ib from rat brain. II. Enzymatic characteristics and regulation of activities by phosphorylation and dephosphorylation.; J Biol Chem; 1992 Jul; 267(19); 13466-13471
Edelman AM, Higgins DM, Bowman CL, Haber SN, Rabin RA, Cho-Lee J; Myosin light chain kinase is expressed in neurons and glia: immunoblotting and immunocytochemical studies.; Brain Res Mol Brain Res; 1992; 14; 27-34
Kennelly PJ, Colburn JC, Lorenzen J, Edelman AM, Stull JT, Krebs EG; Activation mechanism of rabbit skeletal muscle myosin light chain kinase. 5‘-p-fluorosulfonylbenzoyl adenosine as a probe of the MgATP-binding site of the calmodulin-bound and calmodulin-free enzyme.; FEBS Lett; 1991 Jul; 286(1-2); 217-220
Polak KA, Edelman AM, Wasley JW, Cohan CS; A novel calmodulin antagonist, CGS 9343B, modulates calcium-dependent changes in neurite outgrowth and growth cone movements.; J Neurosci; 1991 Feb; 11(2); 534-542
Edelman AM, Lin WH, Osterhout DJ, Bennett MK, Kennedy MB, Krebs EG; Phosphorylation of smooth muscle myosin by type II Ca2+/calmodulin-dependent protein kinase.; Mol Cell Biochem; 1990 Sep; 97(1); 87-98
Kennelly PJ, Starovasnik MA, Edelman AM, Krebs EG; Modulation of the stability of rabbit skeletal muscle myosin light chain kinase through the calmodulin-binding domain.; J Biol Chem; 1990 Jan; 265(3); 1742-1749
Blumenthal DK, Charbonneau H, Edelman AM, Hinds TR, Rosenberg GB, Storm DR, Vincenzi FF, Beavo JA, Krebs EG; Synthetic peptides based on the calmodulin-binding domain of myosin light chain kinase inhibit activation of other calmodulin-dependent enzymes.; Biochem Biophys Res Commun; 1988 Oct; 156(2); 860-865
Kennelly PJ, Edelman AM, Blumenthal DK, Krebs EG; Rabbit skeletal muscle myosin light chain kinase. The calmodulin binding domain as a potential active site-directed inhibitory domain.; J Biol Chem; 1987 Sep; 262(25); 11958-11963
Kennelly, P.J., Takio, K., Blumenthal, D.K., Edelman, A.M., Glaccum, M.B., Klevit, R.E., Roush, C.L., Scott, J.D., Titani, K., Walsh, K.A. and Krebs, E.G.; Organization of myosin light chain kinase from rabbit skeletal muscle; Calcium Binding Proteins in Health and Disease; 1987;
Edelman AM, Blumenthal DK, Krebs EG; Protein serine/threonine kinases.; Annu Rev Biochem; 1987 Jan; 56; 567-613
Takio K, Blumenthal DK, Edelman AM, Walsh KA, Krebs EG, Titani K; Amino acid sequence of an active fragment of rabbit skeletal muscle myosin light chain kinase.; Biochemistry; 1985 Oct; 24(22); 6028-6037
Edelman AM, Hunter DD, Hendrickson AE, Krebs EG; Subcellular distribution of calcium- and calmodulin-dependent myosin light chain phosphorylating activity in rat cerebral cortex.; J Neurosci; 1985 Oct; 5(10); 2609-2617
Edelman AM, Takio K, Blumenthal DK, Hansen RS, Walsh KA, Titani K, Krebs EG; Characterization of the calmodulin-binding and catalytic domains in skeletal muscle myosin light chain kinase.; J Biol Chem; 1985 Sep; 260(20); 11275-11285
Blumenthal DK, Takio K, Edelman AM, Charbonneau H, Titani K, Walsh KA, Krebs EG; Identification of the calmodulin-binding domain of skeletal muscle myosin light chain kinase.; Proc Natl Acad Sci U S A; 1985 May; 82(10); 3187-3191
Krebs, E.G., Blumenthal DK, Edelman AM, Hales, C.N.; Role of cyclic AMP-dependent protein kinase in the regulation of cellular processes; Mechanisms of Receptor Regulation; 1985;
Olwin BB, Edelman AM, Krebs EG, Storm DR; Quantitation of energy coupling between Ca2+, calmodulin, skeletal muscle myosin light chain kinase, and kinase substrates.; J Biol Chem; 1984 Sep; 259(17); 10949-10955
Gallis B, Edelman AM, Casnellie JE, Krebs EG; Epidermal growth factor stimulates tyrosine phosphorylation of the myosin regulatory light chain from smooth muscle.; J Biol Chem; 1983 Nov; 258(21); 13089-13093
Edelman AM, Krebs EG; Phosphorylation of skeletal muscle myosin light chain kinase by the catalytic subunit of cAMP-dependent protein kinase.; FEBS Lett; 1982 Feb; 138(2); 293-298
Andreasen TJ, Keller CH, LaPorte DC, Edelman AM, Storm DR; Preparation of azidocalmodulin: a photoaffinity label for calmodulin-binding proteins.; Proc Natl Acad Sci U S A; 1981 May; 78(5); 2782-2785
Edelman AM, Raese JD, Lazar MA, Barchas JD; Tyrosine hydroxylase: studies on the phosphorylation of a purified preparation of the brain enzyme by the cyclic AMP-dependent protein kinase.; J Pharmacol Exp Ther; 1981 Mar; 216(3); 647-653
Raese JD, Edelman AM, Makk G, Bruckwick EA, Lovenberg W, Barchas JD; Brain striatal tyrosine hydroxylase: activation of the enzyme by cyclic AMP-independent phosphorylation.; Commun Psychopharmacol; 1979 Jan; 3(5); 295-301
Edelman AM, Raese JD, Lazar MA, Barchas JD; In vitro phosphorylation of a purified preparation of bovine corpus striatal tyrosine hydroxylase.; Commun Psychopharmacol; 1978 Jan; 2(6); 461-465
Raese, J.D, Edelman AM, Lazar, M.A., Barchas, J.D.; Tyrosine hydroxylase from brain: Phosphorylation of the enzyme by cyclic AMP-dependent protein kinase; Catecholamines:Basic and Clinical Frontiers; 1978;
Edelman AM Berger PA Renson JF; 5-Hydroxytryptamine: basic and clinical perspectives; Neuroregulators and Psychiatric Disorders; 1977;
Raese, J.D., Edelman AM, Lazar, M.A., Barchas, J.D.; Bovine striatal tyrosine hydroxylase: Multiple forms and evidence for phosphorylation by cyclic AMP-dependent protein kinase; Structure and Function of Monoamine Enzymes; 1977;
Elliott, G.R., Edelman AM, Renson, J.F., Berger, P.A.; Indoleamines and other neuroregulators; Psychopharmacology from Theory to Practice; 1977;


GRANTS

July 2009 to June 2014
Protein kinase signaling in prostate cancer
NIH
Arthur Edelman, Barbara Foster
$2,109,552
September 2004 to November 2007
Identification of In Vivo Targets of Protein Kinases
NIH
Arthur Edelman Kenneth Blumenthal
$381,514
March 2003 to February 2004
Identification of In vivo Targets of Protein Kinases by RNA Interference and Mass Spectrometry
IRCAF
Edelman, Arthur Blumenthal, Kenneth
$38,000
September 2001 to February 2006
Signal Transduction of Doublecortin Kinases
National Science Foundation
Arthur Edelman, Dennis Higgins, Robert Hard
$359,995
January 1994 to December 2001
Regulation of Calmodulin-Dependent Protein Kinases
NIH
Arthur Edelman
$1,054,239
September 1993 to December 1993
Myosin phosphorylation in the nervous system
NIH
Arthur Edelman
$7,942
September 1993 to January 1994
Regulation of calmodulin-dependent protein kinases
Burroughs Wellcome Fund
Arthur Edelman
$11,532
July 1993 to September 1993
Regulation of calmodulin-dependent protein kinases
BRSG/NIH
Arthur Edelman
$9,882
February 1988 to January 1994
Myosin Phosphorylation in the Nervous System
NIH
Arthur Edelman
$428,104
February 1988 to January 1989
Myosin phosphorylation in the nervous system
Research Development Fund-SUNY
Arthur Edelman
$6,980
May 1987 to October 1988
Myosin phosphorylation in the nervous system
NSF
Arthur Edelman
$20,000
May 1987 to June 1988
Myosin phosphorylation in the nervous system
Research Development Fund-SUNY
Arthur Edelman
$3,000
June 1986 to June 1987
Myosin phosphorylation in the nervous system
BRSG/NIH
Arthur Edelman
$7,870



 
Dr. Arthur Edelman NA
Dr. Arthur Edelman NA