scholarly journals Cyclin-Dependent Kinase 5 Promotes Pancreatic  -Cell Survival via Fak-Akt Signaling Pathways

Diabetes ◽  
2011 ◽  
Vol 60 (4) ◽  
pp. 1186-1197 ◽  
Author(s):  
M. Daval ◽  
T. Gurlo ◽  
S. Costes ◽  
C.-j. Huang ◽  
P. C. Butler
Keyword(s):  
Cell Survival ◽  
Signaling Pathways ◽  
Akt Signaling ◽  
Cyclin Dependent Kinase ◽  
Pancreatic Cell ◽  
Cyclin Dependent Kinase 5

scholarly journals SP6616 as a new Kv2.1 channel inhibitor efficiently promotes β-cell survival involving both PKC/Erk1/2 and CaM/PI3K/Akt signaling pathways

2016 ◽  
Vol 7 (5) ◽  
pp. e2216-e2216 ◽  
Author(s):  
T T Zhou ◽  
L L Quan ◽  
L P Chen ◽  
T Du ◽  
K X Sun ◽  
...  
Keyword(s):  
Cell Survival ◽  
Signaling Pathways ◽  
Akt Signaling ◽  
Β Cell

scholarly journals CDK5: Key Regulator of Apoptosis and Cell Survival

Biomedicines ◽  
2019 ◽  
Vol 7 (4) ◽  
pp. 88 ◽  
Author(s):  
Rabih Roufayel ◽  
Nimer Murshid
Keyword(s):  
Cell Survival ◽  
Tertiary Structure ◽  
Cyclin D ◽  
Cyclin Dependent Kinase ◽  
Cellular Functions ◽  
Cellular Processes ◽  
Apoptotic Protein ◽  
Protein Functions ◽  
Induced Apoptosis ◽  
Cyclin Dependent Kinase 5

The atypical cyclin-dependent kinase 5 (CDK5) is considered as a neuron-specific kinase that plays important roles in many cellular functions including cell motility and survival. The activation of CDK5 is dependent on interaction with its activator p35, p39, or p25. These activators share a CDK5-binding domain and form a tertiary structure similar to that of cyclins. Upon activation, CDK5/p35 complexes localize primarily in the plasma membrane, cytosol, and perinuclear region. Although other CDKs are activated by cyclins, binding of cyclin D and E showed no effect on CDK5 activation. However, it has been shown that CDK5 can be activated by cyclin I, which results in anti-apoptotic functions due to the increased expression of Bcl-2 family proteins. Treatment with the CDK5 inhibitor roscovitine sensitizes cells to heat-induced apoptosis and its phosphorylation, which results in prevention of the apoptotic protein functions. Here, we highlight the regulatory mechanisms of CDK5 and its roles in cellular processes such as gene regulation, cell survival, and apoptosis.

scholarly journals Proinsulin C-Peptide Enhances Cell Survival and Protects against Simvastatin-Induced Myotoxicity in L6 Rat Myoblasts

2019 ◽  
Vol 20 (7) ◽  
pp. 1654
Author(s):  
Sumia Essid ◽  
Alan Bevington ◽  
Nigel Brunskill
Keyword(s):  
Skeletal Muscle ◽  
Cell Survival ◽  
Signaling Pathways ◽  
Intracellular Signaling ◽  
Akt Signaling ◽  
Skeletal Muscle Function ◽  
Repair Capacity ◽  
C Peptide ◽  
Myoblast Cell ◽  
Induced Apoptosis

The repair capacity of progenitor skeletal muscle satellite cells (SC) in Type 1 diabetes mellitus (T1DM) is decreased. This is associated with the loss of skeletal muscle function. In T1DM, the deficiency of C-peptide along with insulin is associated with an impairment of skeletal muscle functions such as growth, and repair, and is thought to be an important contributor to increased morbidity and mortality. Recently, cholesterol-lowering drugs (statins) have also been reported to increase the risk of skeletal muscle dysfunction. We hypothesised that C-peptide activates key signaling pathways in myoblasts, thus promoting cell survival and protecting against simvastatin-induced myotoxicity. This was tested by investigating the effects of C-peptide on the L6 rat myoblast cell line under serum-starved conditions. Results: C-peptide at concentrations as low as 0.03 nM exerted stimulatory effects on intracellular signaling pathways—MAP kinase (ERK1/2) and Akt. When apoptosis was induced by simvastatin, 3 nM C-peptide potently suppressed the apoptotic effect through a pertussis toxin-sensitive pathway. Simvastatin strongly impaired Akt signaling and stimulated the reactive oxygen species (ROS) production; suggesting that Akt signaling and oxidative stress are important factors in statin-induced apoptosis in L6 myoblasts. The findings indicate that C-peptide exerts an important protective effect against death signaling in myoblasts. Therefore, in T1DM, the deficiency of C-peptide may contribute to myopathy by rendering myoblast-like progenitor cells (involved in muscle regeneration) more susceptible to the toxic effects of insults such as simvastatin.

Hypoxic preconditioning reduces expression of the cyclin dependent kinase 5 in the post-ischemic neurons

2005 ◽  
Vol 25 (1_suppl) ◽  
pp. S309-S309
Author(s):  
Svetlana Pundik ◽  
W David Lust ◽  
Jose Valerio ◽  
Michael Buczek ◽  
Randall D York ◽  
...  
Keyword(s):  
Hypoxic Preconditioning ◽  
Cyclin Dependent Kinase ◽  
Cyclin Dependent Kinase 5

Homology Modeling of Mus Musculus CDK5 and Molecular Docking Studies with Flavonoids

2017 ◽  
Vol 9 (6) ◽  
Author(s):  
Sowmya Suri ◽  
Rumana Waseem ◽  
Seshagiri Bandi ◽  
Sania Shaik
Keyword(s):  
Molecular Docking ◽  
3D Model ◽  
Structural Features ◽  
Docking Studies ◽  
Amino Acid Residues ◽  
Cyclin Dependent Kinase ◽  
Ligand Complex ◽  
Ligand Interaction ◽  
Molecular Docking Studies ◽  
Cyclin Dependent Kinase 5

A 3D model of Cyclin-dependent kinase 5 (CDK5) (Accession Number: Q543f6) is generated based on crystal structure of P. falciparum PFPK5-indirubin-5-sulphonate ligand complex (PDB ID: 1V0O) at 2.30 Å resolution was used as template. Protein-ligand interaction studies were performed with flavonoids to explore structural features and binding mechanism of flavonoids as CDK5 (Cyclin-dependent kinase 5) inhibitors. The modelled structure was selected on the basis of least modeler objective function. The model was validated by PROCHECK. The predicted 3D model is reliable with 93.0% of amino acid residues in core region of the Ramachandran plot. Molecular docking studies with flavonoids viz., Diosmetin, Eriodictyol, Fortuneletin, Apigenin, Ayanin, Baicalein, Chrysoeriol and Chrysosplenol-D with modelled protein indicate that Diosmetin is the best inhibitor containing docking score of -8.23 kcal/mol. Cys83, Lys89, Asp84. The compound Diosmetin shows interactions with Cys83, Lys89, and Asp84.

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