cGMP effects on vascular tone: modulating the activity of myosin light chain phosphatase | Zendy

Frank V. Brozovich | Zendy

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cGMP effects on vascular tone: modulating the activity of myosin light chain phosphatase

Author(s) -

Frank V. Brozovich

Publication year - 2009

Publication title -

bmc pharmacology

Language(s) - English

Resource type - Journals

ISSN - 1471-2210

DOI - 10.1186/1471-2210-9-s1-s7

Subject(s) - myosin light chain phosphatase , protein subunit , myosin , exon , microbiology and biotechnology , phosphatase , myosin light chain kinase , protein phosphatase 1 , chemistry , nitric oxide , protein phosphatase 2 , gene isoform , biochemistry , biology , phosphorylation , organic chemistry , gene

Background During flow-mediated vasodilatation, nitric oxide activates guanylate cyclase and the resultant increase cGMP leads to an activation of PKGI. PKGI activates a number of targets in the smooth muscle cell that result in smooth muscle relaxation, including MLC phosphatase. MLC phosphatase isolated from smooth muscle is a holoenzyme consisting of three subunits; a 20 kDa subunit, a 38 kDa catalytic subunit and a myosin targeting subunit (MYPT1). MYPT1 has two isoforms that differ by the presence of a an alternatively spliced 31 bp 3' exon; exon inclusion codes for a MYPT1 that lacks a COOH-terminus leucine zipper (LZ-), while exon exclusion shifts the reading frame and codes for a LZ+ MYPT1 isoform.

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