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(Circulation Research. 2003;93:891.)
© 2003 American Heart Association, Inc.

Editorials

Neuropeptide Y Modulates L-Type Ca²⁺ Current During Heart Development

Alan E.G. Lomax, Keith A. Sharkey, Wayne R. Giles

From the Department of Physiology and Biophysics (A.E.G.L., K.A.S., W.R.G.), University of Calgary, Calgary, Alberta, Canada; Department of Bioengineering (W.R.G.), Whitaker Institute of Biomedical Engineering University of California San Diego, Calif.

Correspondence to Dr Wayne R. Giles, Department of Bioengineering, Whitaker Institute of Biomedical Engineering, PFBG 384, University of California San Diego, 9500 Gilman Dr, La Jolla, CA 92093-0412. E-mail wgiles@bioeng.ucsd.edu

Key Words: neuropeptide Y • development • Ca²⁺ channel • innervation • ventricle

An extract of the first 250 words of the full text is provided, because this article has no abstract.

An interesting and potentially very important study¹ in this issue of Circulation Research reports that during development of the mammalian heart, neuropeptide Y can significantly increase L-type Ca²⁺ current, thereby enhancing heart rate and strength of contraction. In this study, a combination of targeted deletion of the NPY gene, electrophysiological recordings, and immunoblot analysis of Ca²⁺ channel _1C expression is used in an experimental design that involves study of hearts from pre- and postnatal animals at predetermined stages.¹ These findings can perhaps be put in context by the following brief review of NPY physiology and pharmacology in mammalian tissue.

Neuropeptide Y (NPY) was identified by Tatemoto and Mutt in 1982 through use of a novel chemical assay that detected the amidated C-terminal tyrosine residue of this 36-amino acid peptide.^2,3 Isolated first from brain, it was soon discovered to be widely distributed throughout the body, primarily in postganglionic sympathetic nerves and often colocalized with norepinephrine.⁴ Indeed, NPY is the most widely distributed and abundant neuropeptide in the nervous system. NPY shares structural and functional homology with two other 36-amino acid peptides, pancreatic polypeptide (PP) and peptide YY (PYY).⁴ All three have a characteristic U-shaped tertiary structure termed the PP-fold.⁵ Four G protein–coupled receptors for the PP-fold peptides have been cloned; these are termed the Y₁, Y₂, Y₄, and Y₅ receptors. The Y₃ receptor has not been cloned, although a y₆ receptor has been identified by molecular methods. It is designated with a lowercase "y" as, at present, it appears . . . [Full Text of this Article]