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Michael Sirover, PhDMichael Sirover, PhD

 

Professor, Pharmacology

Telephone:  215-707- 4351

Fax:  215-707-9890

Email: michael.sirover@temple.edu

 

Department of Pharmacology

 

Educational Background:

 

BS, Rensselaer Polytechnic Institute, 1968

 

PhD, SUNY at Stony Brook, 1974

 

Postdoctoral Fellowship, Fox Chase Cancer Center, 1977

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Research Interests:

 

GAPDH gradient

 

We are examining intracellular protein structure in normal human cells and as a function of aging. We examine subcellular protein: protein interactions of the multidimensional protein, glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Recent studies revealed that both eucaryotic and procaryotic GAPDH were, in reality, multidimensional proteins exhibiting a series of discrete activities independent of its classical glycolytic function. These new activities included catalysis of membrane fusion and transport, microtubule bundling, phosphate group transfer, apoptosis, nuclear tRNA export, DNA replication and DNA repair. It has also been identified as an RNA binding protein especially involved in molecular mechanisms of viral infection. Its multiple activities may have distinct subcellular localizations that may be dependent on cell proliferation. Most recently, GAPDH has been implicated in vesicular transport and in secretory pathways. The latter may involve the formation of GAPDH: tubulin protein complexes that would directly affect cytoskeletal and membrane structure/function.

 

We have begun to examine the subcellular protein structure of the b-amyloid precursor protein (b-APP). Alteration of b-APP structure is considered to be of fundamental importance in the etiology of Alzheimer’s disease. We use cells from Alzheimer’s disease patients as well as age-matched normal human cells. We have used the model system described above to identify intracellular HMW b-APP structure as a new characteristic of Alzheimer’s disease cells.

 

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PUBMED PUBLICATIONS :


Recent Medically Related Publications, Obtained from PubMed (Click on PubMed ID to view abstract)

25286305. Sirover MA, Structural analysis of glyceraldehyde-3-phosphate dehydrogenase functional diversity. Int J Biochem Cell Biol :()2014 Oct 5

22388977. Sirover MA, Subcellular dynamics of multifunctional protein regulation: mechanisms of GAPDH intracellular translocation. J Cell Biochem 113:7(2193-200)2012 Jul

21640161. Sirover MA, On the functional diversity of glyceraldehyde-3-phosphate dehydrogenase: biochemical mechanisms and regulatory control. Biochim Biophys Acta 1810:8(741-51)2011 Aug

15770658. Sirover MA, New nuclear functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells. J Cell Biochem 95:1(45-52)2005 May 1

15716040. Mazzola JL, Sirover MA, Aging of human glyceraldehyde-3-phosphate dehydrogenase is dependent on its subcellular localization. Biochim Biophys Acta 1722:2(168-74)2005 Mar 11

12829261. Mazzola JL, Sirover MA, Subcellular localization of human glyceraldehyde-3-phosphate dehydrogenase is independent of its glycolytic function. Biochim Biophys Acta 1622:1(50-6)2003 Jun 20

12503091. Mazzola JL, Sirover MA, Subcellular alteration of glyceraldehyde-3-phosphate dehydrogenase in Alzheimer's disease fibroblasts. J Neurosci Res 71:2(279-85)2003 Jan 15

12428732. Mazzola JL, Sirover MA, Alteration of intracellular structure and function of glyceraldehyde-3-phosphate dehydrogenase: a common phenotype of neurodegenerative disorders? Neurotoxicology 23:4-5(603-9)2002 Oct

12008025. Mazzola JL, Sirover MA, Alteration of nuclear glyceraldehyde-3-phosphate dehydrogenase structure in Huntington's disease fibroblasts. Brain Res Mol Brain Res 100:1-2(95-101)2002 Apr 30

11208907. Mazzola JL, Sirover MA, Reduction of glyceraldehyde-3-phosphate dehydrogenase activity in Alzheimer's disease and in Huntington's disease fibroblasts. J Neurochem 76:2(442-9)2001 Jan

10407139. Sirover MA, New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase. Biochim Biophys Acta 1432:2(159-84)1999 Jul 13

9213215. Sirover MA, Role of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in normal cell function and in cell pathology. J Cell Biochem 66:2(133-40)1997 Aug 1

8649216. Sirover MA, Minireview. Emerging new functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells. Life Sci 58:25(2271-7)1996

8169845. Wurzer JC, Tallarida RJ, Sirover MA, New mechanism of action of the cancer chemotherapeutic agent 5-fluorouracil in human cells. J Pharmacol Exp Ther 269:1(39-43)1994 Apr

8316218. Mauro DJ, De Riel JK, Tallarida RJ, Sirover MA, Mechanisms of excision of 5-fluorouracil by uracil DNA glycosylase in normal human cells. Mol Pharmacol 43:6(854-7)1993 Jun

8451199. Mansur NR, Meyer-Siegler K, Wurzer JC, Sirover MA, Cell cycle regulation of the glyceraldehyde-3-phosphate dehydrogenase/uracil DNA glycosylase gene in normal human cells. Nucleic Acids Res 21:4(993-8)1993 Feb 25

1742335. Seal G, Tallarida RJ, Sirover MA, Purification and properties of the uracil DNA glycosylase from Bloom's syndrome. Biochim Biophys Acta 1097:4(299-308)1991 Nov 21

1924305. Meyer-Siegler K, Mauro DJ, Seal G, Wurzer J, deRiel JK, Sirover MA, A human nuclear uracil DNA glycosylase is the 37-kDa subunit of glyceraldehyde-3-phosphate dehydrogenase. Proc Natl Acad Sci U S A 88:19(8460-4)1991 Oct 1

2079960. Cool BL, Sirover MA, Proliferation-dependent regulation of DNA glycosylases in progeroid cells. Mutat Res 237:5-6(211-20)1990 Sep-Nov

2155388. Seal G, Henderson EE, Sirover MA, Immunological alteration of the Bloom's syndrome uracil DNA glycosylase in Epstein-Barr virus-transformed human lymphoblastoid cells. Mutat Res 243:3(241-8)1990 Mar

2091748. Sirover MA, Vollberg TM, Seal G, DNA repair and the molecular mechanisms of Bloom's syndrome. Crit Rev Oncog 2:1(19-33)1990

2813420. Vollberg TM, Siegler KM, Cool BL, Sirover MA, Isolation and characterization of the human uracil DNA glycosylase gene. Proc Natl Acad Sci U S A 86:22(8693-7)1989 Nov

2785849. Cool BL, Sirover MA, Immunocytochemical localization of the base excision repair enzyme uracil DNA glycosylase in quiescent and proliferating normal human cells. Cancer Res 49:11(3029-36)1989 Jun 1

2720664. Lee KA, Sirover MA, Physical association of base excision repair enzymes with parental and replicating DNA in BHK-21 cells. Cancer Res 49:11(3037-44)1989 Jun 1

3353381. Seal G, Brech K, Karp SJ, Cool BL, Sirover MA, Immunological lesions in human uracil DNA glycosylase: association with Bloom syndrome. Proc Natl Acad Sci U S A 85:7(2339-43)1988 Apr

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