Plasma Levels of Receptor Interacting Protein Kinase-3 Correlated with Coronary Artery Disease.

08:00 EDT 30th March 2019 | BioPortfolio

Summary of "Plasma Levels of Receptor Interacting Protein Kinase-3 Correlated with Coronary Artery Disease."

Necroptosis plays an important role in human atherosclerosis and atheroma development. Since receptor interacting protein kinase-3 (RIP3) acts as a key mediator of necroptosis, this study aimed to explore its relationship between plasma RIP3 levels and coronary artery disease (CAD) and discover a potential new biomarker for screening CAD subtypes and severity.


Journal Details

This article was published in the following journal.

Name: Chinese medical journal
ISSN: 2542-5641


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Medical and Biotech [MESH] Definitions

A ubiquitously expressed G-protein-coupled receptor kinase subtype that has specificity for the agonist-occupied form of BETA-ADRENERGIC RECEPTORS and a variety of other G-PROTEIN-COUPLED RECEPTORS. Although it is highly homologous to G-PROTEIN-COUPLED RECEPTOR KINASE 2, it is not considered to play an essential role in regulating myocardial contractile response.

Receptors for PROTEIN KINASE C that consist of seven WD40 REPEATS. They function in a wide variety of cellular and physiologic processes including the assembly of signaling complexes, protein translation, cell growth and proliferation, APOPTOSIS, and MUSCARINIC RECEPTOR transport. RACK1 depends on protein kinase C activity to translocate from the perinuclear region to the cell periphery and associates with the plasma membrane through interactions with KERATIN-1 and INTEGRIN BETA-1.

A RIP serine-theonine kinase that contains a C-terminal caspase activation and recruitment domain. It can signal by associating with other CARD-signaling adaptor proteins and INITIATOR CASPASES that contain CARD domains within their N-terminal pro-domain region.

A family of serine-threonine kinases that plays a role in intracellular signal transduction by interacting with a variety of signaling adaptor proteins such as CRADD SIGNALING ADAPTOR PROTEIN; TNF RECEPTOR-ASSOCIATED FACTOR 2; and TNF RECEPTOR-ASSOCIATED DEATH DOMAIN PROTEIN. Although they were initially described as death domain-binding adaptor proteins, members of this family may contain other protein-binding domains such as those involving caspase activation and recruitment.

A protein-tyrosine kinase receptor that is closely related in structure to the INSULIN RECEPTOR. Although commonly referred to as the IGF-I receptor, it binds both IGF-I and IGF-II with high affinity. It is comprised of a tetramer of two alpha and two beta subunits which are derived from cleavage of a single precusor protein. The beta subunit contains an intrinsic tyrosine kinase domain.

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