Carol J. Deutsch, Ph.D.
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Carol J. Deutsch, Ph.D.
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Professor of Physiology
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Department: Physiology
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Graduate Group Affiliations
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Contact information
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650A Clinical Research Building
3b 415 Curie Boulevard
Philadelphia, PA 19104-6085
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3b 415 Curie Boulevard
Philadelphia, PA 19104-6085
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Office: (215) 898-8014
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Email:
cjd@pennmedicine.upenn.edu
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cjd@pennmedicine.upenn.edu
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Publications
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Links
cc Search PubMed for articles
9d Cell and Molecular Biology graduate group webpage.
85 Department of Physiology Faculty page
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cc Search PubMed for articles
9d Cell and Molecular Biology graduate group webpage.
85 Department of Physiology Faculty page
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Education:
21 9 B.A. 16 (Chemistry) c
39 Brandeis University, Waltham, MA, 1966.
21 c M. Phil 1a (Organic Chem.) c
37 Yale University, New Haven, CT, 1969.
21 a Ph.D. 18 (Phys. Chem.) c
37 Yale University, New Haven, CT, 1972.
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Permanent link21 9 B.A. 16 (Chemistry) c
39 Brandeis University, Waltham, MA, 1966.
21 c M. Phil 1a (Organic Chem.) c
37 Yale University, New Haven, CT, 1969.
21 a Ph.D. 18 (Phys. Chem.) c
37 Yale University, New Haven, CT, 1972.
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43 Function and assembly of voltage-gated potassium channels.
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ca Key words: voltage-gated K+ channels, C-type inactivation, gating kinetics, protein-protein interactions, oligomerization, channel assembly, biogenesis, ion channels, human T-lymphocytes.
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26 Description of Research
478 The research of this laboratory has focused on the physiology and biophysics of a voltage-gated potassium (Kv) channel found in human T cells, Kv1.3. Thus far, we have shown that Kv1.3 plays at least two functional roles. First, it contributes to resting T-cell membrane potential, and second, it mediates volume regulation. Both of these functions are critical in mitogen-stimulated T-cell proliferation. Therefore, it is important to understand what is responsible for the potassium channel conductance in a T lymphocyte. There are two determinants: the biophysical properties of the channel and the ability of the channel to form and be expressed on the cell surface. In the first case, we study the mechanisms of activation, inactivation, and recovery of this channel. In the second case, we study the stepwise process by which Kv1.3 acquires its secondary, tertiary, and quaternary structure. These studies involve a combined use of several diverse techniques including electrophysiological techniques, in vitro translation and transcription methods and protein assays, as well as standard cloning and molecular biological methods.
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1e Lab personnel:
44 Andrey Kosolapov, Ph.D., Senior Research Investigator
34 Jianli Lu, Ph.D., Research Specialist
3b LiWei Tu, M.D., Senior Research Investigator
2c Pengse Po, Research Specialist
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Description of Research Expertise
2a Research Interests43 Function and assembly of voltage-gated potassium channels.
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ca Key words: voltage-gated K+ channels, C-type inactivation, gating kinetics, protein-protein interactions, oligomerization, channel assembly, biogenesis, ion channels, human T-lymphocytes.
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26 Description of Research
478 The research of this laboratory has focused on the physiology and biophysics of a voltage-gated potassium (Kv) channel found in human T cells, Kv1.3. Thus far, we have shown that Kv1.3 plays at least two functional roles. First, it contributes to resting T-cell membrane potential, and second, it mediates volume regulation. Both of these functions are critical in mitogen-stimulated T-cell proliferation. Therefore, it is important to understand what is responsible for the potassium channel conductance in a T lymphocyte. There are two determinants: the biophysical properties of the channel and the ability of the channel to form and be expressed on the cell surface. In the first case, we study the mechanisms of activation, inactivation, and recovery of this channel. In the second case, we study the stepwise process by which Kv1.3 acquires its secondary, tertiary, and quaternary structure. These studies involve a combined use of several diverse techniques including electrophysiological techniques, in vitro translation and transcription methods and protein assays, as well as standard cloning and molecular biological methods.
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1e Lab personnel:
44 Andrey Kosolapov, Ph.D., Senior Research Investigator
34 Jianli Lu, Ph.D., Research Specialist
3b LiWei Tu, M.D., Senior Research Investigator
2c Pengse Po, Research Specialist
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c9 Kosolapov, A. and Deutsch, C.: Folding of the Voltage-gated K+ Channel T1 Recognition Domain. J. Biol. Chem. 278: 4305-13, 2003.
94 Deutsch, C.: Potassium channel ontology. Ann. Rev Physiol. 64: 19-46, 2002.
95 Deutsch, C.: Potassium channel ontogeny. Ann. Rev. Physiol. 64: 19-46, 2002.
10d Lu, J., Robinson, J.M., Edwards, D. and Deutsch, C: T1-T1 Interactions occur in the Endoplasmic Reticulum while nascent Kv peptides are still attached to ribosomes. Biochem. 40: 10934-10946, 2001.
d0 Lu, J. and Deutsch, C.: Pegylation: A method for assessing topological accessibilities in Kv1.3. Biochem. 40(44): 13288-301, Nov 2001.
c3 Tu L., Wang J., Helm A., Skach WR., Deutsch C.: Transmembrane biogenesis of Kv1.3. Biochemistry 39(4): 824-36, Feb 1 2000.
c5 Tu L., Deutsch C.: Evidence for dimerization of dimers in K+ channel assembly. Biophysical Journal 76(4): 2004-17, Apr 1999.
a0 Sheng Z., Deutsch C.: Assembly of ion channels. Methods in Enzymology 293: 17-32, 1998.
eb Deutsch, C: The courtship and marriage of K+ channel subunits. in Biol. Skr. Dan. Vid. Selsk. 49: 107-113, 1998 Notes: (Proceedings of The Royal Danish Academy).
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Selected Publications
94 Deutsch, C.: The Birth of a Channel. Neuron 2003 Notes: Currently in press.c9 Kosolapov, A. and Deutsch, C.: Folding of the Voltage-gated K+ Channel T1 Recognition Domain. J. Biol. Chem. 278: 4305-13, 2003.
94 Deutsch, C.: Potassium channel ontology. Ann. Rev Physiol. 64: 19-46, 2002.
95 Deutsch, C.: Potassium channel ontogeny. Ann. Rev. Physiol. 64: 19-46, 2002.
10d Lu, J., Robinson, J.M., Edwards, D. and Deutsch, C: T1-T1 Interactions occur in the Endoplasmic Reticulum while nascent Kv peptides are still attached to ribosomes. Biochem. 40: 10934-10946, 2001.
d0 Lu, J. and Deutsch, C.: Pegylation: A method for assessing topological accessibilities in Kv1.3. Biochem. 40(44): 13288-301, Nov 2001.
c3 Tu L., Wang J., Helm A., Skach WR., Deutsch C.: Transmembrane biogenesis of Kv1.3. Biochemistry 39(4): 824-36, Feb 1 2000.
c5 Tu L., Deutsch C.: Evidence for dimerization of dimers in K+ channel assembly. Biophysical Journal 76(4): 2004-17, Apr 1999.
a0 Sheng Z., Deutsch C.: Assembly of ion channels. Methods in Enzymology 293: 17-32, 1998.
eb Deutsch, C: The courtship and marriage of K+ channel subunits. in Biol. Skr. Dan. Vid. Selsk. 49: 107-113, 1998 Notes: (Proceedings of The Royal Danish Academy).
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