Related Experiment Video
Updated: Dec 17, 2025

Assessment of Mitochondrial Functions and Cell Viability in Renal Cells Overexpressing Protein Kinase C Isozymes
Published on: January 7, 2013
Extracellular creatine kinase may modulate purinergic signalling
1CK Science Foundation, POB 23639, 1100, EC, Amsterdam, the Netherlands. mail@lizzybrewster.net.
Extracellular creatine kinase (CK) may influence bodily functions by interacting with ADP and ATP. This interaction could link CK to conditions like hypertension and obesity.
Area of Science:
- Biochemistry
- Physiology
- Molecular Biology
Background:
- Extracellular purine nucleotides (ADP, ATP) regulate critical physiological processes via purinergic receptors.
- Circulating cytoplasmic-type creatine kinase (CK) is linked to adverse outcomes like bleeding, hypertension, and obesity.
Purpose of the Study:
- To investigate the proposed role of extracellular CK in modulating purinergic signaling.
- To explore the potential mechanisms of CK's interaction with ADP and ATP.
Main Methods:
- The study proposes a hypothesis based on existing literature.
- Further experimental validation is required to confirm the proposed mechanisms.
Main Results:
- The abstract suggests a potential link between extracellular CK and purinergic signaling pathways.
- This interaction may involve ADP binding and ATP generation by CK.
Conclusions:
- Extracellular CK is hypothesized to modulate purinergic signaling.
- This modulation could contribute to the observed clinical associations of CK with various health conditions.
More Related Videos
08:46Implementing Patch Clamp and Live Fluorescence Microscopy to Monitor Functional Properties of Freshly Isolated PKD Epithelium
Published on: September 1, 2015
08:00Enhancing the Engraftment of Human Induced Pluripotent Stem Cell-derived Cardiomyocytes via a Transient Inhibition of Rho Kinase Activity
Published on: July 10, 2019
Related Concept Videos
cAMP-dependent Protein Kinase Pathways
GPCRs Regulate Adenylyl Cylase Activity
Amplifying Signals via Enzymatic Cascade
Calmodulin-dependent Signaling
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
GPCR Desensitization
Intracellular Signaling Cascades