Research Faculty

630 West 168th Street
PH15 West 1574-I
New York, NY 10032

Phone: 212-305-3795
Anatomy & Cell Biology
Philip W. Brandt, Ph.D.
Professor Emeritus, Anatomy and Cell Biology
Research Summary

Muscle regulation and contraction

The research in my laboratory explores how cooperation between the proteins of the thin and thick filaments regulates muscle contraction. We use "skinned muscle fibers" made by placing small bundles of fresh rabbit psoas muscle in solutions designed to break down the cell surface membranes. Selected regulatory proteins are extracted and replaced with those made by genetic engineering or by modification of purified natural proteins. Fluorescent labels are often attached to the proteins before they are inserted into the filaments to follow changes in protein and filament conformation by fluorescence spectrometry and microscopy. Most experiments are done on computer controlled apparatus. For example, in a typical experiment a single fiber is dissected, modified then exposed to a series of increasing calcium concentrations while tension and fluorescence ratios are recorded. Our aim is to define the rapid restructuring of groups of molecules in the filaments that precede and accompany muscle contraction.

Selected Publications

Brandt, PW and Poggesi, C. 2014. Clusters of Bound Ca2+ Initiate Contraction in Fast Skeletal Muscle. Archives of Biochemistry and Biophysics. In Press.

Schachat F. & Brandt, P. W. 2013. The troponin I inhibitory peptide uncouples force generation and the cooperativity of contractile activation in mammalian skeletal muscle. J. Muscle Research & Cell Motility. 34(2): 83-92.

Brandt P.W.,, Colomo F, Piroddi N, Poggesi C & Tesi C. 1998. Force regulation by Ca2+ in skinned single cardiac myocytes of frog. Biophysical Journal, 74(4):1994-2004.

Brandt P,W.,, & Schachat FH. 1997. Troponin C modulates the activation of the thin filament by rigor cross-bridges. Biophysical Journal. 72:2262-2267.

Brandt, P.W., Diamond, M.S., Rutchik, J.S. and Schachat, F.H., 1987. Cooperative interactions between troponin-tropomyosin units extend the length of the thin filament in skeletal muscle. J. Molecular Biol. 195:885-896.

Brandt, P.W., Diamond, M.S., and Schachat, F.H., l984. The thin filament of vertebrate skeletal muscle co-operatively activates as a unit. Journal of Molecular Biology. l80:379-l67.

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