A - Z
MARCO COLOMBINI 
Professor, Associate Chair, and Director of Graduate Studies
email:colombini@umd.edu
phone:
301.405.6925 (office)
301.405.2599 (lab)
fax:301.314.9358
office:3276
Bio-Psych
graduate programs: Biology,
CHEM & BCHM,
BIOE,
Biophysics,
CBMG,
MOCB
visit lab page
most recent publications
RESEARCH INTERESTS
Research Focus: biophysics and cell physiology of membrane channels, especially those located in the mitochondrial outer membrane. These channels are involved in mitochondria-mediated apoptosis. I believe they are involved in the decision-making process, the release of proteins from mitochondria that activate the execution phase of apoptosis. These channels are: 1) VDAC, a 30kDa channel that controls the flow of metabolites across the outer membrane; 2) ceramide channels, large, protein permeable, channels formed by the self-assembly of a lipid, ceramide. The research is mechanistic in nature and we use a variety of techniques from electrophysiological recordings to electron microscopy.
Recent Publications
Siskind, L. J., Fluss, S., Bui, M., and Colombini, M. 2005. Sphingosine forms channels in membranes that differ greatly from those formed by ceramide. Journal of Bioenergetics and Biomembranes. 37: 227-236.
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Rostovtseva, T.K., Tan, W., and Colombini, M. 2005. On the role of VDAC in apoptosis: fact and fiction. Journal of Bioenergetics and Biomembranes. 37: 129-142.
Siskind, Leah J. 2005. Mitochondrial Ceramide and the Induction of Apoptosis. Journal of Bioenergetics and Biomembranes. 37: 143-153.
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Stiban, J., Fistere Jr., D., and Colombini, M. 2006. Dihydroceramide hinders ceramide channel formation: implications on apoptosis. Apoptosis 11:773-80.
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Elrick, M.J., Fluss, S., and Colombini, M. 2006. Sphingosine, a product of ceramide hydrolysis by ceramidase, influences the formation of ceramide channels. Biophys. J. 91: 1749-1756.
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Siskind, L. J., Kolesnick, R.N. and Colombini, M. 2006. Ceramide forms channels in mitochondrial outer membranes at physiologically relevant concentrations. Mitochondrion 6:118-25.
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Lai, J.C., Tan, W., Benimetskaya, L., Miller, P., Colombini, M., and Stein, C.A. 2006. A pharmacologic target of G3139 in melanoma cells may be the mitochondrial VDAC. Proceedings of the National Academy of Sciences U.S.A., 103:7494-7499.
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Anishkin, A., Sukharev, S., and Colombini, M. 2006. Searching for the molecular arrangement of transmembrane ceramide channels. Biophysical Journal, 90:2414-2426.
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Lai, J.C., Brown, B.D., Voskresenskiy, A.M., Vonhoff, S., Klussman, S., Tan, W., Colombini, M., Weeratna, R., Miller, P., Benimetskaya, L., and Stein, C.A. 2007. Comparison of D-G3139 and Its Enantiomer L-G3139 in Melanoma Cells Demonstrates Minimal In Vitro but Dramatic In Vivo Chiral Dependency. Molecular Therapy, 15: 270-280.
Tan, W., Lai, J.C., Miller. P., Stein, C.A., and Colombini, M. 2007. Phosphorothioate Oligonucleotides Reduce Mitochondrial Outer Membrane Permeability to ADP. American Journal of Physiology 292: C1388-C1397.
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Tan W., Loke Y.H., Stein C.A., Miller P. and Colombini M. 2007. Phosphorothioate Oligonucleotides Block the VDAC Channel. Biophysical Journal 93: 1184-1191.
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