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Vol. 62, Issue 3, 485-496, September 2002

Molecular Cloning and Characterization of the Human Voltage-Gated Calcium Channel alpha 2delta -4 Subunit

Ning Qin, Susan Yagel, Mary-Lou Momplaisir, Ellen E. Codd, and Michael R. D'Andrea

Johnson & Johnson Pharmaceutical Research and Development, Spring House, Pennsylvania

The voltage-gated calcium channel is composed of a pore-forming alpha 1 subunit and several regulatory subunits: alpha 2delta , beta , and gamma . We report here the identification of a novel alpha 2delta subunit, alpha 2delta -4, from the expressed sequence tag database followed by its cloning and characterization. The novel alpha 2delta -4 subunit gene contains 39 exons spanning about 130 kilobases and is co-localized with the CHCNA1C gene (alpha 1C subunit) on human chromosome 12p13.3. Alternative splicing of the alpha 2delta -4 gene gives rise to four potential variants, a through d. The open reading frame of human alpha 2delta -4a is composed of 3363 base pairs encoding a protein with 1120 residues and a calculated molecular mass of 126 kDa. The alpha 2delta -4a subunit shares 30, 32, and 61% identity with the human calcium channel alpha 2delta -1, alpha 2delta -2, and alpha 2delta -3 subunits, respectively. Primary sequence comparison suggests that alpha 2delta -4 lacks the gabapentin binding motifs characterized for alpha 2delta -1 and alpha 2delta -2; this was confirmed by a [3H]gabapentin-binding assay. In human embryonic kidney 293 cells, the alpha 2delta -4 subunit associated with CaV1.2 and beta 3 subunits and significantly increased CaV1.2/beta 3-mediated Ca2+ influx. Immunohistochemical study revealed that the alpha 2delta -4 subunit has limited distribution in special cell types of the pituitary, adrenal gland, colon, and fetal liver. Whether the alpha 2delta -4 subunit plays a distinct physiological role in select endocrine tissues remains to be demonstrated.

Copyright © 2002 by The American Society for Pharmacology and Experimental Therapeutics


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