Premium
Expression of soluble guanylyl cyclase
Author(s) -
Harteneck Christian,
Koesling Doris,
Söling Ariane,
Schultz Günter,
Böhme Eycke
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80489-6
Subject(s) - soluble guanylyl cyclase , complementary dna , transfection , protein subunit , gucy2d , guanylate cyclase 2c , gucy1a3 , enzyme , biochemistry , cyclase , gucy1b3 , microbiology and biotechnology , coding region , chemistry , messenger rna , biology , guanylate cyclase , gene
Purified soluble guanylyl cyclase consists of two subunits (70 and 73 kDa) whose primary structures were recently determined. The availability of cDNA clones coding for either subunit allowed to study the question of the functional roles of the two subunits in expression experiments. Enzyme subunits were expressed in COS‐7 cells by transfection with expression vectors containing the coding region for the 70 of 73 kDa subunit of the enzyme. No significant elevation in the activity of soluble guanylyl cyclase was observed in cells transfected with cDNA coding for one of the subunits. In contrast, transfection of cells with cDNAs coding for both subunits resulted in a marked increase in activity of soluble guanylyl cyclase. Enzyme activity was stimulated about 50‐fold by sodium nitroprusside. The results indicate that formation of cyclic GMP by soluble guanylyl cyclase requires'both 70 and 73 kDa subunits.