Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

---

Query: EC:2.7.11.1 (protein kinase)
81,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The viscosity of membranes isolated from sarcoplasmic reticulum of rabbits with isadrine myocarditis was studied, using pyrene as a hydrophobic fluorescent probe. The increase in the viscosity of membranes from injured heart occurred at lower temperatures and was sharper than in the case of intact heart in both "free" and "bound" lipid domains. The increase in the lipid viscosity under myocarditis was associated with decreased Ca++, Mg++ -ATPase and cAMP-dependent protein kinase activities and with an elevated content of lipid peroxidation products.
...
PMID:The increase in viscosity and peroxidation of sarcoplasmic reticulum membrane lipids in isadrine myocarditis. 296 98

The incorporation of 33P into 54, 43 and 23 kDalton proteins of rabbit cardiac sarcolemma is demonstrated both in intact muscle and under isadrine myocarditis. The phosphorylation by cAMP-dependent protein kinase is shown only for the 23.5 kDalton protein. The level of this protein phosphorylation decreases under isadrine myocarditis in the presence of 10(-6) M cAMP and absence of "exogenic" protein kinase. In the preparations of the sarcolemma of the cardiac muscle under myocarditis the phosphorylation of the 23.5 kDalton protein is not stimulated by beta-agonists in the medium without "exogenic" protein kinase and cAMP. The latter being present, the phosphorylation reaches the control values.
...
PMID:[Phosphorylation of cardiac sarcolemma proteins in isadrine myocarditis]. 299 68

The content of cAMP in the rat heart under neoepinephrine myocarditis does not differ from the control values and less increases relative to the control at the adrenalin concentrations of 5 X 10(-5) and 5 X 10(-4) M in the in vitro experiments (control: myocardium of healthy animals). Under these conditions dissociation of holoenzyme of cAMP-dependent protein kinase is disturbed in the presence of endogene-developed nucleotide and the phosphorylating activity decreases, respectively. The injection of the catalytic subunit of cAMP-dependent protein kinase encapsulated into neutral liposomes increases the duration of the myocarditis action potential for animals with the metabolic myocardial insufficiency.
...
PMID:[Effect of the catalytic subunit of cAMP-dependent protein kinase on the electrical activity of the rat heart in isadrine myocarditis]. 300 39

It was demonstrated that under normal conditions calmodulin and exogenous 3':5'-AMP-dependent protein kinase considerably active Ca2+ transport by sarcoplasmic reticulum of rabbit myocardium; a combined action of these compounds produces an additive effect. The protein-inhibitor of 3':5'-AMP-dependent protein kinase and trifluoroperazine eliminate the activating effect of 3':5'-AMP-dependent protein kinase; in addition, trifluoroperazine decreases significantly the basal level of Ca2+ uptake. The 3':5'-AMP-dependent activation of Ca2+ transport becomes apparent after Ca2+-calmodulin-dependent phosphorylation of FSR membrane proteins. In toxico-allergic myocarditis calmodulin and 3':5'-AMP-dependent protein kinase do not activate the low level of Ca2+ uptake. No differences were observed between the action of calmodulin and 3':5'-AMP-dependent protein kinase isolated from normal and pathological rabbit heart. A conclusion is drawn that the decrease of Ca2+ transport is due to the impairment of Ca2+-calmodulin and 3':5'-AMP-dependent phosphorylation in sarcoplasmic reticulum membranes.
...
PMID:[Effect of calmodulin and 3':5'-AMP-dependent protein kinases on calcium transport by sarcoplasmic reticulum of normal rabbit myocardium and in toxico-allergic myocarditis]. 631 76

Changes between serial laboratory test results can be significant, even if none of the individual results exceeds the reference interval. We developed a statistical method for the calculation of reference change limits from routine patients' data for situations in which the majority of the patients can be considered suitable reference subjects. The method was applied to cardiac enzyme data [creatine kinase (CK; EC 2.7.3.2), creatine kinase isoenzyme MB (CK-2), lactate dehydrogenase (LD; EC 1.1.1.28), and lactate dehydrogenase isoenzyme 1 (LD-1)] from 2029 consecutive patients. We used hospital discharge diagnoses to exclude patients with the diagnosis of myocardial infarction or myocarditis, but we also studied the characteristics of the method on unselected patients' data. The reference change limits derived from the diagnosis-selected patient group were as follows (U/L, activity measurements in serum at 37 degrees C according to Scandinavian recommendations): CK from -39 to 27, CK-2 from -8 to 7, LD from -86 to 85, and LD-1 from -19 to 15. Similar limits were obtained by conventional statistical methods from a group of 29 hospitalized patients with no myocardial symptoms. Our results suggest that it is possible to produce clinically applicable reference change limits from routine data.
...
PMID:Method for determining reference changes from patients' serial data: example of cardiac enzymes. 822 24

The sera of patients with myocarditis and idiopathic dilated cardiomyopathy contain agonistic autoantibodies that bind to the beta 1-adrenoceptor. These antibodies recognize epitopes on either the first or second extracellular loop of this receptor and exert in cultured neonatal rat heart myocytes a positive chronotropic effect. This effect is eliminated by beta 1-adrenoceptor blockade as well as by peptides corresponding to the first or second extracellular loop of the human beta 1-adrenoceptor. The antibodies realize their effects mainly via the beta-adrenoceptor-adenylate cyclase-protein kinase A cascade.
...
PMID:The beta 1-adrenoceptor as antigen: functional aspects. 868 11

NF-kappaB is a pleiotropic transcription factor implicated in the regulation of diverse biological phenomena, including apoptosis, cell survival, cell growth, cell division, innate immunity, cellular differentiation, and the cellular responses to stress, hypoxia, stretch and ischemia. In the heart, NF-kappaB has been shown to be activated in atherosclerosis, myocarditis, in association with angina, during transplant rejection, after ischemia/reperfusion, in congestive heart failure, dilated cardiomyopathy, after ischemic and pharmacological preconditioning, heat shock, burn trauma, and in hypertrophy of isolated cardiomyocytes. Regulation of NF-kappaB is complicated; in addition to being activated by canonical cytokine-mediated pathways, NF-kappaB is activated by many of the signal transduction cascades associated with the development of cardiac hypertrophy and response to oxidative stress. Many of these signaling cascades activate NF-kappaB by activating the IkappaB kinase (IKK) complex a major component of the canonical pathway. These signaling interactions occur largely via signaling crosstalk involving the mitogen-activated protein kinase/extracellular signalregulated kinase kinases (MEKKs) that are components of mitogen activated protein kinase (MAPK) signaling pathways. Additionally, there are other signaling factors that act more directly to activate NF-kappaB via IkappaB or by direct phosphorylation of NF-kappaB subunits. Finally, there are combinatorial interactions at the level of the promoter between NF-kappaB, its coactivators, and other transcription factors, several of which are activated by MAPK and cytokine signaling pathways. Thus, in addition to being a major mediator of cytokine effects in the heart, NF-kappaB is positioned as a signaling integrator. As such, NF-kappaB functions as a key regulator of cardiac gene expression programs downstream of multiple signal transduction cascades in a variety of physiological and pathophysiological states. We show that genetic blockade of NF-kappaB reduces infarct size in the murine heart after ischemia/reperfusion (I/R), implicating NF-kappaB as a major determinant of cell death after I/R. These results support the concept that NF-kappaB may be an important therapeutic target for specific cardiovascular diseases.
...
PMID:NF-kappaB as an integrator of diverse signaling pathways: the heart of myocardial signaling? 1455 89

Coxsackievirus B3 (CVB3), a common human pathogen for viral myocarditis, induces a direct cytopathic effect (CPE) and apoptosis on infected cells. To elucidate the mechanisms that contribute to these processes, we studied the role of glycogen synthase kinase 3beta (GSK3beta). GSK3beta activity was significantly increased after CVB3 infection and addition of tyrosine kinase inhibitors blocked CVB3-triggered GSK3beta activation. Inhibition of caspase activity had no inhibitory effect on CVB3-induced CPE; however, blockage of GSK3beta activation attenuated both CVB3-induced CPE and apoptosis. We further showed that CVB3 infection resulted in reduced beta-catenin protein expression, and GSK3beta inhibition led to the accumulation and nuclear translocation of beta-catenin. Finally, we found that CVB3-induced CPE and apoptosis were significantly reduced in cells stably overexpressing beta-catenin. Taken together, our results demonstrate that CVB3 infection stimulates GSK3beta activity via a tyrosine kinase-dependent mechanism, which contributes to CVB3-induced CPE and apoptosis through dysregulation of beta-catenin.
...
PMID:Inhibition of glycogen synthase kinase 3beta suppresses coxsackievirus-induced cytopathic effect and apoptosis via stabilization of beta-catenin. 1590 81

Viral myocarditis is a major cause of sudden cardiac death in children and young adults. Among viruses, coxsackievirus B3 (CVB3) is the most common agent for myocarditis. Recently, more consideration has been given to the role of signaling pathways in pathogenesis of enteroviral myocarditis, providing new platform for identifying a new potential therapeutic target for this, so far, incurable disease. Previously, we reported on the role of the protein kinase-B/Akt in CVB3 replication and virus-induced cell injury. Here, we report on regulation of virus-induced Akt activation by the integrin-linked kinase in infected mouse cardiomyocytes and HeLa cells. This study also presents the first observation that inhibition of ILK in CVB3-infected cells significantly improves the viability of infected cells, while blocking viral replication and virus release. Complementary experiments using a constitutively active form of Akt1 revealed that the observed protective effect of ILK inhibition is dependent on the associated downregulation of virus-induced Akt activation. To our knowledge, this is the first report of such beneficial effects of ILK inhibition in a viral infection model and conveys new insights in our efforts to characterize a novel therapeutic target for treatment of enteroviral myocarditis.
...
PMID:Novel role for integrin-linked kinase in modulation of coxsackievirus B3 replication and virus-induced cardiomyocyte injury. 1691 1

The mechanisms by which autoantibodies against cardiac myosin (CM) may lead to heart dysfunction is unknown. We show that autoantibodies to CM in anti-CM sera and mAbs derived from experimental autoimmune myocarditis targeted the heart cell surface and induced Ab-mediated cAMP-dependent protein kinase A activity. Ab-mediated cell signaling of protein kinase A was blocked by CM, anti-IgG, or by specific inhibitors of the beta-adrenergic receptor (beta-AR) pathway. mAbs confirmed mimicry between CM and the beta-AR. Passive transfer of purified Ab (IgG) from CM-immunized rats resulted in IgG deposition and apoptosis in the heart, leading to a cardiomyopathic heart disease phenotype in recipients. Our novel findings link anti-CM Ab with the beta-AR and subsequent Ab-mediated cell signaling in the heart.
...
PMID:Mimicry and antibody-mediated cell signaling in autoimmune myocarditis. 1711 1


1 2 3 Next >>

---