scholarly journals A rare case of pseudohypoparathyroidism

2019 ◽  
Vol 45 (1) ◽  
pp. 38-39
Author(s):  
V. A. Gubkina ◽  
T. S. Kamynina ◽  
E. V. Kornilova ◽  
A. V. Dreval
Keyword(s):  
Rare Case ◽  
Rna Synthesis ◽  
Specific Effect ◽  
Receptor Complex ◽  
Dependent Protein Kinase ◽  
Dominant Type ◽  
Related Disease ◽  
Dependent Protein ◽  
Kinase Substrates ◽  
Gh Receptors

Pseudohypoparathyroidism (PGPT) - Albright's hereditary osteodystrophy is a sex-related disease rarely seen in medical practice. Inherited by the dominant type. It is caused by insensitivity of the kidneys and bones to parathyroid hormone (PG), which is secreted in normal or slightly elevated amounts [6, 10]. GH may not have a specific effect on cells due to pathology of GH receptors, impaired expression of information RNA synthesis by an unchanged hormone-receptor complex, the presence of pathological components of adenylate cyclase, pathological AMP-dependent protein kinase, or a defect in the synthesis of kinase substrates in the presence of circulating GH antagonists [5, 10 ].

Constitutive RNA synthesis for the yeast activator ADR1 and identification of the ADR1-5c mutation: implications in posttranslational control of ADR1

1986 ◽  
Vol 6 (11) ◽  
pp. 4026-4030
Author(s):  
C L Denis ◽  
C Gallo
Keyword(s):  
Rna Synthesis ◽  
Potential Role ◽  
Glucose Repression ◽  
Posttranslational Regulation ◽  
Mrna Levels ◽  
Recognition Sequence ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
Kinase Phosphorylation

The regulation of mRNA production for the yeast positive activator ADR1, a gene required for the expression of the glucose-repressible alcohol dehydrogenase (ADH II), was studied. ADR1 mRNA levels did not vary when yeasts were switched from glucose- to ethanol-containing medium, while ADH II expression increased 100-fold. The mRNA for the ADR1-5c allele, which augments ADH II expression 60-fold during glucose repression, was not present in greater abundance than ADR1 mRNA. Additionally, the ccr1-1 allele, which blocks ADH2 mRNA formation and partially suppresses the ADR1-5c phenotype, did not alter the levels of ADR1 mRNA. These results indicate that ADR1 is not transcriptionally controlled. To determine the character of the ADR1-5c mutation, the region containing the mutation was identified and sequenced. At base pair +683 a G-to-A transition was detected in the ADR1 coding sequence which would result in the substitution of a lysine residue for an arginine at amino acid 228. The location of the ADR1-5c mutation in the interior of the ADR1 coding sequences suggests that it enhances the activity of an extant but inactive ADR1 protein rather than increases the abundance of ADR1 by altered translation of its mRNA. The ADR1-5c mutation occurs in a region of the polypeptide corresponding to a cyclic AMP-dependent protein kinase phosphorylation recognition sequence. The potential role of reversible phosphorylation in the posttranslational regulation of ADR1 is discussed.

scholarly journals Constitutive RNA synthesis for the yeast activator ADR1 and identification of the ADR1-5c mutation: implications in posttranslational control of ADR1.

1986 ◽  
Vol 6 (11) ◽  
pp. 4026-4030 ◽  
Author(s):  
C L Denis ◽  
C Gallo
Keyword(s):  
Rna Synthesis ◽  
Potential Role ◽  
Glucose Repression ◽  
Posttranslational Regulation ◽  
Mrna Levels ◽  
Recognition Sequence ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
Kinase Phosphorylation

The regulation of mRNA production for the yeast positive activator ADR1, a gene required for the expression of the glucose-repressible alcohol dehydrogenase (ADH II), was studied. ADR1 mRNA levels did not vary when yeasts were switched from glucose- to ethanol-containing medium, while ADH II expression increased 100-fold. The mRNA for the ADR1-5c allele, which augments ADH II expression 60-fold during glucose repression, was not present in greater abundance than ADR1 mRNA. Additionally, the ccr1-1 allele, which blocks ADH2 mRNA formation and partially suppresses the ADR1-5c phenotype, did not alter the levels of ADR1 mRNA. These results indicate that ADR1 is not transcriptionally controlled. To determine the character of the ADR1-5c mutation, the region containing the mutation was identified and sequenced. At base pair +683 a G-to-A transition was detected in the ADR1 coding sequence which would result in the substitution of a lysine residue for an arginine at amino acid 228. The location of the ADR1-5c mutation in the interior of the ADR1 coding sequences suggests that it enhances the activity of an extant but inactive ADR1 protein rather than increases the abundance of ADR1 by altered translation of its mRNA. The ADR1-5c mutation occurs in a region of the polypeptide corresponding to a cyclic AMP-dependent protein kinase phosphorylation recognition sequence. The potential role of reversible phosphorylation in the posttranslational regulation of ADR1 is discussed.

scholarly journals Interphase-specific Phosphorylation-mediated Regulation of Tubulin Dimer Partitioning in Human Cells

2007 ◽  
Vol 18 (5) ◽  
pp. 1909-1917 ◽  
Author(s):  
Per Holmfeldt ◽  
Sonja Stenmark ◽  
Martin Gullberg
Keyword(s):  
Receptor Complex ◽  
Cell Models ◽  
Dependent Protein Kinase ◽  
Tubulin Dimer ◽  
Microtubule Polymerization ◽  
Protein Map ◽  
Dependent Protein ◽  
Necessary And Sufficient ◽  
Stimulation Of ◽  
Inducible Gene

The microtubule cytoskeleton is differentially regulated by a diverse array of proteins during interphase and mitosis. Op18/stathmin (Op18) and microtubule-associated protein (MAP)4 have been ascribed opposite general microtubule-directed activities, namely, microtubule destabilization and stabilization, respectively, both of which can be inhibited by phosphorylation. Here, using three human cell models, we depleted cells of Op18 and/or MAP4 by expression of interfering hairpin RNAs and we analyzed the resulting phenotypes. We found that the endogenous levels of Op18 and MAP4 have opposite and counteractive activities that largely govern the partitioning of tubulin dimers in the microtubule array at interphase. Op18 and MAP4 were also found to be the downstream targets of Ca2+- and calmodulin-dependent protein kinase IV and PAR-1/MARK2 kinase, respectively, that control the demonstrated counteractive phosphorylation-mediated regulation of tubulin dimer partitioning. Furthermore, to address mechanisms regulating microtubule polymerization in response to cell signals, we developed a system for inducible gene product replacement. This approach revealed that site-specific phosphorylation of Op18 is both necessary and sufficient for polymerization of microtubules in response to the multifaceted signaling event of stimulation of the T cell antigen receptor complex, which activates several signal transduction pathways.

Aza-β3-amino acid containing peptidomimetics as cAMP-dependent protein kinase substrates

2010 ◽  
Vol 38 (5) ◽  
pp. 229-233 ◽  
Author(s):  
Ksenija Kisseljova ◽  
Aleksei Kuznetsov ◽  
Michèle Baudy-Floc’h ◽  
Jaak Järv
Keyword(s):  
Amino Acid ◽  
Protein Kinase ◽  
Dependent Protein Kinase ◽  
Camp Dependent Protein Kinase ◽  
Dependent Protein ◽  
Kinase Substrates

scholarly journals Phosphorylation of Ser-241 is essential for the activity of 3-phosphoinositide-dependent protein kinase-1: identification of five sites of phosphorylation in vivo

1999 ◽  
Vol 342 (2) ◽  
pp. 287-292 ◽  
Author(s):  
Antonio CASAMAYOR ◽  
Nick A. MORRICE ◽  
Dario R. ALESSI
Keyword(s):  
Protein Kinase ◽  
Kinase Domain ◽  
The Other ◽  
Phosphorylation Sites ◽  
Dependent Protein Kinase ◽  
Equivalent Position ◽  
293 Cells ◽  
Dependent Protein ◽  
Kinase Substrates

3-Phosphoinositide-dependent protein kinase-1 (PDK1) expressed in unstimulated 293 cells was phosphorylated at Ser-25, Ser-241, Ser-393, Ser-396 and Ser-410 and the level of phosphorylation of each site was unaffected by stimulation with insulin-like growth factor-1. Mutation of Ser-241 to Ala abolished PDK1 activity, whereas mutation of the other phosphorylation sites individually to Ala did not affect PDK1 activity. Ser-241, unlike the other phosphorylation sites on PDK1, was resistant to dephosphorylation by protein phosphatase 2A1. Ser-241 lies in the activation loop of the PDK1 kinase domain between subdomains VII and VIII in the equivalent position to the site that PDK1 phosphorylates on its protein kinase substrates. PDK1 expressed in bacteria was active and phosphorylated at Ser-241, suggesting that PDK1 can phosphorylate itself at this site, leading to its own activation.

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