scholarly journals STE20 ‐Type Protein Kinase MST4 Controls NAFLD Progression by Regulating Lipid Droplet Dynamics and Metabolic Stress in Hepatocytes

2021 ◽  
Author(s):  
Mara Caputo ◽  
Emmelie Cansby ◽  
Sima Kumari ◽  
Yeshwant Kurhe ◽  
Syam Nair ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Lipid Droplet ◽  
Metabolic Stress ◽  
Droplet Dynamics ◽  
Type Protein

Tracking lipid droplet dynamics for the discrimination of cancer cells by a solvatochromic fluorescent probe

2021 ◽  
Vol 333 ◽  
pp. 129541
Author(s):  
Linlin Yang ◽  
Jianping Wang ◽  
Bianhua Liu ◽  
Guangmei Han ◽  
Hong Wang ◽  
...  
Keyword(s):  
Cancer Cells ◽  
Fluorescent Probe ◽  
Lipid Droplet ◽  
Droplet Dynamics

Identification and characterization of a novel sucrose-non-fermenting protein kinase/AMP-activated protein kinase-related protein kinase, SNARK

2001 ◽  
Vol 355 (2) ◽  
pp. 297-305 ◽  
Author(s):  
Diana L. LEFEBVRE ◽  
Yahong BAI ◽  
Nazanin SHAHMOLKY ◽  
Monika SHARMA ◽  
Raymond POON ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Cellular Response ◽  
Catalytic Domain ◽  
Metabolic Stress ◽  
Glucose Deprivation ◽  
Protein Band ◽  
Northern Blotting ◽  
Significant Similarity ◽  
Amp Activated Protein Kinase

Subtraction hybridization after the exposure of keratinocytes to ultraviolet radiation identified a differentially expressed cDNA that encodes a protein of 630 amino acid residues possessing significant similarity to the catalytic domain of the sucrose-non-fermenting protein kinase (SNF1)/AMP-activated protein kinase (AMPK) family of serine/threonine protein kinases. Northern blotting and reverse-transcriptase-mediated PCR demonstrated that mRNA transcripts for the SNF1/AMPK-related kinase (SNARK) were widely expressed in rodent tissues. The SNARK gene was localized to human chromosome 1q32 by fluorescent in situ hybridization. SNARK was translated in vitro to yield a single protein band of approx. 76kDa; Western analysis of transfected baby hamster kidney (BHK) cells detected two SNARK-immunoreactive bands of approx. 76-80kDa. SNARK was capable of autophosphorylation in vitro; immunoprecipitated SNARK exhibited phosphotransferase activity with the synthetic peptide substrate HMRSAMSGLHLVKRR (SAMS) as a kinase substrate. SNARK activity was significantly increased by AMP and 5-amino-4-imidazolecarboxamide riboside (AICAriboside) in rat keratinocyte cells, implying that SNARK might be activated by an AMPK kinase-dependent pathway. Furthermore, glucose deprivation increased SNARK activity 3-fold in BHK fibroblasts. These findings identify SNARK as a glucose- and AICAriboside-regulated member of the AMPK-related gene family that represents a new candidate mediator of the cellular response to metabolic stress.

Evaluation of fertilization and flower abscission following over-expression of an apple NAK-type protein kinase in tomato

2011 ◽  
Vol 130 (4) ◽  
pp. 487-491 ◽  
Author(s):  
In-Jung Kim ◽  
Joon-Seon Yoon ◽  
Young-Koung Lee
Keyword(s):  
Protein Kinase ◽  
Over Expression ◽  
Type Protein ◽  
Flower Abscission

AMP-Activated Protein Kinase: A Metabolic Stress Sensor in the Heart

2015 ◽  
pp. 187-225
Author(s):  
Martin Pelosse ◽  
Malgorzata Tokarska-Schlattner ◽  
Uwe Schlattner
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Metabolic Stress ◽  
Stress Sensor ◽  
Amp Activated Protein Kinase ◽  
Kinase A

scholarly journals CIDE Proteins in Human Health and Disease

Cells ◽  
2019 ◽  
Vol 8 (3) ◽  
pp. 238 ◽  
Author(s):  
Mark Slayton ◽  
Abhishek Gupta ◽  
Bijinu Balakrishnan ◽  
Vishwajeet Puri
Keyword(s):  
Human Health ◽  
Dna Fragmentation ◽  
Lipid Droplet ◽  
Fat Metabolism ◽  
Physiological Role ◽  
Specific Protein ◽  
Metabolic Phenotype ◽  
Droplet Dynamics ◽  
Health And Disease ◽  
Cide Proteins

Cell death-Inducing DNA Fragmentation Factor Alpha (DFFA)-like Effector (CIDE) proteins have emerged as lipid droplet-associated proteins that regulate fat metabolism. There are three members in the CIDE protein family—CIDEA, CIDEB, and CIDEC (also known as fat-specific protein 27 (FSP27)). CIDEA and FSP27 are primarily expressed in adipose tissue, while CIDEB is expressed in the liver. Originally, based upon their homology with DNA fragmentation factors, these proteins were identified as apoptotic proteins. However, recent studies have changed the perception of these proteins, redefining them as regulators of lipid droplet dynamics and fat metabolism, which contribute to a healthy metabolic phenotype in humans. Despite various studies in humans and gene-targeting studies in mice, the physiological roles of CIDE proteins remains elusive. This review will summarize the known physiological role and metabolic pathways regulated by the CIDE proteins in human health and disease.

Novel and Efficient Access to Phenylamino-pyrimidine Type Protein Kinase C Inhibitors Utilizing a Negishi Cross-Coupling Strategy†

2005 ◽  
Vol 70 (13) ◽  
pp. 5215-5220 ◽  
Author(s):  
Peter Stanetty ◽  
Gregor Hattinger ◽  
Michael Schnürch ◽  
Marko D. Mihovilovic
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cross Coupling ◽  
Protein Kinase C Inhibitors ◽  
Kinase C ◽  
Type Protein ◽  
Efficient Access ◽  
Coupling Strategy

scholarly journals TRESK (K2P18.1) Background Potassium Channel Is Activated by Novel-Type Protein Kinase C via Dephosphorylation

2019 ◽  
Vol 95 (6) ◽  
pp. 661-672 ◽  
Author(s):  
Enikő Pergel ◽  
Miklós Lengyel ◽  
Péter Enyedi ◽  
Gábor Czirják
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Potassium Channel ◽  
Kinase C ◽  
Type Protein
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