# Molecular cloning and predicted full‐length amino acid sequence of the type Iβ isozyme of cGMP‐dependent protein kinase from human placenta

@article{Sandberg1989MolecularCA,
title={Molecular cloning and predicted full‐length amino acid sequence of the type I$\beta$ isozyme of cGMP‐dependent protein kinase from human placenta},
author={M{\aa}rten Sandberg and Vasanti Natarajan and Inger Ronander and Daniel Kalderon and Ulrich Walter and Suzanne M. Lohmann and Tore Jahnsen},
journal={FEBS Letters},
year={1989},
volume={255}
}
• Published 25 September 1989
• Biology
• FEBS Letters
• Biology, Chemistry
• 1996
In cultured vascular smooth muscle cells, the type I cGK mRNA concentration was reduced to 10% of the basal level by 4×10 −10 mol/L platelet-derived growth factor, and this suggests a pathophysiological implication of thetype I cK in cardiovascular diseases, including hypertension and atherosclerosis.
• Biology
• 1997
The cloning of the gene PRKG1 is described, a single-copy gene consisting of 19 exons encompassing at least 220 kb that was shown to encode the type Iα- and type Iβ-specific parts of the cGK.
• Biology
The Journal of Biological Chemistry
• 1997
Based on the activation constants of all chimeras constructed, empirical weighting factors have been calculated that quantitatively describe the contribution of the individual amino-terminal domains S1–S6 to the high affinity cGK Iα phenotype.
• Biology
Molecular endocrinology
• 1990
The molecular cloning of a third isoform of C, from a human testis cDNA library, as well as the isolation of human cDNAs for C alpha and C beta are reported, suggesting that C gamma may be distinct in its protein substrate specificity or its interaction with the different regulatory subunits.
• Biology
• 1998
The isolation and characterization of bacterial artificial chromosome (BAC)- and P1-derived artificial chromosomes (PAC)-clones containing the gene encoding the human type II cGK showed the presence of a non-translated exon and 5′-rapid amplification of cDNA-ends established the presence.
• Biology
European journal of biochemistry
• 1993
Using the polymerase chain reaction to study mRNA expressed in human epithelial tumor cells, a member of a new family of protein kinases was identified that has amino-acid-sequence similarity to both the Tyr-specific and the Ser/Thr-specific kinase classes.
• Biology
Journal of Biological Chemistry
• 2003
Deletion and site-directed mutagenesis have been used to systematically delete and substitute individual Leu/Ile heptad repeats in PKG Iβ, and results indicate that dimerization increases sensitivity for cGMP activation of the enzyme.
• Biology, Chemistry
Biochemistry
• 1990
Far-UV circular dichroism spectra of bovine lung cyclic GMP dependent protein kinase (G-kinase) show that the enzyme contains alpha-helical and beta-pleated sheet elements and it is proposed that this sequence may be the important part of the dimerization domain of the enzyme.
• Biology, Medicine
The Journal of pharmacology and experimental therapeutics
• 1999
We previously showed that stimulation of cGMP-dependent protein kinase (PKG) stimulates L-type calcium current in newborn but not in adult rabbit ventricular myocytes. We have now isolated rabbit PKG
• Biology
Journal of neurochemistry
• 1995
The effects of guanylyl cyclase activators, such as nitric oxide and the atriopeptides, in various regions of the CNS may be mediated through cGK II, with highest expression in the thalamus.

## References

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• Biology
Biochemistry
• 1984
Data suggest that ancestral gene splicing events may have been involved in the fusion of two families of proteins to generate the allosteric character of this chimeric enzyme.
• Biology
The Journal of biological chemistry
• 1989
The results indicated that the catalytic domain, cGMP binding domain(s), and inhibitory domain of cGK interact primarily within the same subunit rather than between subunits of the dimer as previously hypothesized for dimeric c GK.
• Biology
Proceedings of the National Academy of Sciences of the United States of America
• 1976
CGMP-dependent protein kinase holoenzyme has an apparent molecular weight of 150,000 as determined by glycerol density gradient sedimentation, and a single protein band of 71,000 molecular weight was observed that suggested the holoen enzyme is a dimer composed of subunits of identical molecular weight.