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J. Biol. Chem., Vol. 265, Issue 28, 16841-16845, 10, 1990
M Nakane, K Arai, S Saheki, T Kuno, W Buechler and F Murad
Complementary DNA clones corresponding to the 70- and 82-kDa subunits of
soluble guanylate cyclase of rat lung have been isolated. Blot
hybridization of total poly(A)+ RNA from rat tissues detected mRNA of about
3.4 kilobases for the 70-kDa subunit and about 5.5 kilobases for the 82-kDa
subunit. Messenger RNA levels of both subunits were abundant in lung and
cerebrum, moderate in cerebellum, heart, and kidney, and low in liver and
muscle, consistent with previously described enzyme activities in these
tissues. Southern blot analysis of high molecular weight genomic DNA from
rat liver indicated that the genes for the 70- and 82-kDa subunits are
different. The carboxyl-terminal region of the 70- and 82-kDa subunits
showed a high degree of homology and also had a partial homology with the
putative catalytic domain of particulate guanylate cyclase and adenylate
cyclase, indicating that both the 70- and 82-kDa subunits have catalytic
domains. The cDNAs were subcloned to an expression vector and transfected
to L cells. The cells transfected with cDNA of the 70-kDa subunit or the
82-kDa subunit showed no guanylate cyclase activity, whereas the cells
transfected with both the 70- and 82-kDa subunit cDNAs showed significant
guanylate cyclase activity that was activated markedly by sodium
nitroprusside. These data suggest that both subunits are required for both
the basal catalytic and regulatory activity of soluble guanylate cyclase.
Presumably both catalytic subunits must be present and interactive to
permit synthesis of cyclic GMP and nitrovasodilator activation.
Molecular cloning and expression of cDNAs coding for soluble guanylate cyclase from rat lung
Tokyo Metropolitan Institute for Neurosciences, Japan.
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