RICHARD R. ALMON

Molecular Physiology, Endocrinology and Pharmacology

Professor Biological Sciences
Adjunct Professor Pharmaceutics

B.S 1968 MS 1970 Ph.D 1971, University of Illinois
Postdoctoral work 1971 Duke University
Research Assistant Professor 1975 University of California/San Diego
Professor Biological Sciences
Adjunct Professor Pharmaceutics, School of Pharmacy


Address Information

Richard R. Almon
Department of Biological Sciences
107 Hochstetter Hall
State University of New York at Buffalo
Buffalo, NY 14260

(716) 645-4909

To send e-mail: almon@buffalo.edu


Course Information

Dr. Almon's BIO 129 course


RESEARCH SUMMARY:

Close to one half of all protein in the body is contained in the musculature. This protein mass serves two quite different purposes. The first and most obvious function is mechanics (movement and posture). The second, perhaps less obvious function, is to support general body energy metabolism. When necessary, amino acid carbon is removed from the muscle and used for gluconeogenesis by the liver. A structurally related group of steroid hormones, glucocorticoids, express the systemic demand for amino acid carbon from the musculature. The central focus of the work in this laboratory is in understanding the mechanism by which the systemic demand for amino acid carbon is discriminately distributed amongst the various muscles of the body. In general, the quality and quantity of mechanical activity regulates protein metabolism in skeletal muscle. The character of mechanical activity also regulates many aspects of the expressed characteristics of a muscle. By manipulating the character of muscle mechanical activity, it is possible to change several expressed characteristics of a muscle. These expressed characteristics include hormonal sensitivities, isozymes of the contractile apparatus, and enzymes involved in energy metabolism. By manipulating the character of mechanical activity, it is also possible to cause a muscle to atrophy or hypertrophy. The goal of this work is to develop quantitative models that describe the integrative regulation of muscle protein mass and gene expression by mechanical activity and hormones. The general approach is to use animal manipulations to induce atrophy or hypertrophy in selected muscles within the context of controlled changes in the systemic hormonal milieu. We then analyze at the structural , cellular, and molecular levels the characteristics of the manipulated muscles. At the present time, our particular interest is in changes in the expression of protein and message for several receptors, myosin isozymes, and enzymes involved in energy metabolism. Methodologies used in the laboratory include animal surgery, cell fractionation, equilibrium binding assays, enzyme kinetics, RIAs, HPLC, light and fluorescent spectrophotometry, electrophoresis, and Northern Western hybridizations, ELISA, and quantitative rtPCR.


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