Michael Sirover, PhD
- Contact Information
- About Me
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.
- Education, Training & Credentials
- Postdoctoral Fellowship, Fox Chase Cancer Center, 1977
- PhD, SUNY at Stony Brook, 1974
- BS, Rensselaer Polytechnic Institute, 1968