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}
}

cDNA Cloning and Gene Expression of Human Type Iα cGMP-Dependent Protein Kinase

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.

Characterization of the Human Gene Encoding the Type Iα and Type Iβ cGMP-Dependent Protein Kinase (PRKG1)

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.

Identification of the Amino Acid Sequences Responsible for High Affinity Activation of cGMP Kinase Iα*

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.

Molecular cloning of a tissue-specific protein kinase (C gamma) from human testis--representing a third isoform for the catalytic subunit of cAMP-dependent protein kinase.

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.

CHARACTERIZATION OF THE GENE ENCODING THE HUMAN TYPE II CGMP-DEPENDENT PROTEIN KINASE (PRKG2)

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.

Identification of a new family of human epithelial protein kinases containing two leucine/isoleucine-zipper domains.

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.

Dimerization of cGMP-dependent Protein Kinase Iβ Is Mediated by an Extensive Amino-terminal Leucine Zipper Motif, and Dimerization Modulates Enzyme Function*

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.

Effects of cyclic GMP on the secondary structure of cyclic GMP dependent protein kinase and analysis of the enzyme's amino-terminal domain by far-ultraviolet circular dichroism.

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.

Analysis of expression of cGMP-dependent protein kinase in rabbit heart cells.

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
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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.

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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.