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J Biol Chem, Vol. 274, Issue 21, 14838-14849, May 21, 1999

hSK4/hIK1, a Calmodulin-binding K_Ca Channel in Human T Lymphocytes
ROLES IN PROLIFERATION AND VOLUME REGULATION

Rajesh Khanna, Martin C. Chang, William J. Joiner^§, Leonard K. Kaczmarek^§¶, and Lyanne C. Schlichter

From the  Playfair Neuroscience Unit, Toronto Western Hospital, University Health Network, and Department of Physiology, University of Toronto, Toronto, Ontario M5T 2S8, Canada and the ^§ Departments of Cellular and Molecular Physiology and ^¶ Pharmacology, Yale University School of Medicine, New Haven, Connecticut 06520

Human T lymphocytes express a Ca²⁺-activated K⁺ current (IK), whose roles and regulation are poorly understood. We amplified hSK4 cDNA from human T lymphoblasts, and we showed that its biophysical and pharmacological properties when stably expressed in Chinese hamster ovary cells were essentially identical to the native IK current. In activated lymphoblasts, hSK4 mRNA increased 14.6-fold (Kv1.3 mRNA increased 1.3-fold), with functional consequences. Proliferation was inhibited when Kv1.3 and IK were blocked in naive T cells, but IK block alone inhibited re-stimulated lymphoblasts. IK and Kv1.3 were involved in volume regulation, but IK was more important, particularly in lymphoblasts. hSK4 lacks known Ca²⁺-binding sites; however, we mapped a Ca²⁺-dependent calmodulin (CaM)-binding site to the proximal C terminus (Ct1) of hSK4. Full-length hSK4 produced a highly negative membrane potential (V_m) in Chinese hamster ovary cells, whereas the channels did not function when either Ct1 or the distal C terminus was deleted (V_m ~0 mV). Native IK (but not expressed hSK4) current was inhibited by CaM and CaM kinase antagonists at physiological V_m values, suggesting modulation by an accessory molecule in native cells. Our results provide evidence for increased roles for IK/hSK4 in activated T cell functions; thus hSK4 may be a promising therapeutic target for disorders involving the secondary immune response.

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