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Dr. Martin Snider
Associate Professor
- Biochemistry Trainer: YES
- Phone: 216-368-5572
- Fax: 216-368-3419
- Office: W433
- Lab: RT400
- Mail Address:
Department of Biochemistry
10900 Euclid Avenue
Cleveland, OH 44106-4935
Dr. Martin Snider
Dr. Snider's research is focused on the synthesis and intracellular traffic of glycoproteins in eukaryotic cells. Three current projects are concerned with the function of the Golgi complex, an important organelle of the secretory pathway.
Molecular genetics of glycoprotein synthesis in yeast. Sugars are added to most secreted proteins as they are transported through the endoplasmic reticulum and Golgi. To gain a better understanding of this process, glycosylation- defective mutants have been isolated in the yeast, S. pombe. Two of these mutants are defective in the late stages of glycoprotein synthesis in the Golgi. The defective genes are currently being cloned. Cloned genes will provide important tools for studying the enzymology of glycosylation in the Golgi and the signals that cause enzymes to become localized in this complex organelle. Retrograde traffic from the plasma membrane to the Golgi. The Snider lab has shown that some membrane proteins can return from the cell surface to the Golgi in mammalian cells. This pathway allows cells to rescue missorted proteins, repair covalent modifications of cell surface proteins, and reuse membranes of secretory vesicles. Current studies are aimed at elucidating the route of retrograde traffic, identifying proteins that follow the pathway, and evaluating the functions. Mechanisms of altered plasma protein glycosylation in human disease. Inflammation in humans affects the sugar structures of glycoproteins in the bloodstream. In many diseases, these changes alter proteins' functional properties. To understand the cellular and molecular basis of these changes the glycosylation of immunoglobulins in rheumatoid arthritis is being studied. Immunoglobulin- secreting cells are being investigated to learn how this disease affects Golgi enzymes of glycoprotein synthesis. These studies will provide important insights into the regulation of the glycosylation machinery by hormones and cytokines in normal and disease states.
Selected References
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