The Role of Tyrosine Phosphorylation of Protein Kinase C Delta in Infection and Inflammation.


Journal

International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791

Informations de publication

Date de publication:
26 Mar 2019
Historique:
received: 07 03 2019
revised: 15 03 2019
accepted: 22 03 2019
entrez: 29 3 2019
pubmed: 29 3 2019
medline: 10 7 2019
Statut: epublish

Résumé

Protein Kinase C (PKC) is a family composed of phospholipid-dependent serine/threonine kinases that are master regulators of inflammatory signaling. The activity of different PKCs is context-sensitive and these kinases can be positive or negative regulators of signaling pathways. The delta isoform (PKCδ) is a critical regulator of the inflammatory response in cancer, diabetes, ischemic heart disease, and neurodegenerative diseases. Recent studies implicate PKCδ as an important regulator of the inflammatory response in sepsis. PKCδ, unlike other members of the PKC family, is unique in its regulation by tyrosine phosphorylation, activation mechanisms, and multiple subcellular targets. Inhibition of PKCδ may offer a unique therapeutic approach in sepsis by targeting neutrophil-endothelial cell interactions. In this review, we will describe the overall structure and function of PKCs, with a focus on the specific phosphorylation sites of PKCδ that determine its critical role in cell signaling in inflammatory diseases such as sepsis. Current genetic and pharmacological tools, as well as in vivo models, that are used to examine the role of PKCδ in inflammation and sepsis are presented and the current state of emerging tools such as microfluidic assays in these studies is described.

Identifiants

pubmed: 30917487
pii: ijms20061498
doi: 10.3390/ijms20061498
pmc: PMC6471617
pii:
doi:

Substances chimiques

Protein Kinase C-delta EC 2.7.11.13

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : NIGMS NIH HHS
ID : R01 GM114359
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM134701
Pays : United States
Organisme : National Institute of Health
ID : GM114359
Organisme : American Heart Association
ID : 16GRNT29980001

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Auteurs

Qingliang Yang (Q)

Department of Mechanical Engineering, College of Engineering, Temple University, Philadelphia, PA 19122, USA. tug44932@temple.edu.

Jordan C Langston (JC)

Department of Bioengineering, College of Engineering, Temple University, Philadelphia, PA 19122, USA. tuj27061@temple.edu.

Yuan Tang (Y)

Department of Mechanical Engineering, College of Engineering, Temple University, Philadelphia, PA 19122, USA. tud19329@temple.edu.

Mohammad F Kiani (MF)

Department of Mechanical Engineering, College of Engineering, Temple University, Philadelphia, PA 19122, USA. mkiani@temple.edu.
Department of Radiation Oncology, Lewis Katz School of Medicine, Temple University, Philadelphia, PA 19140, USA. mkiani@temple.edu.

Laurie E Kilpatrick (LE)

Center for Inflammation, Clinical and Translational Lung Research, Department of Thoracic Medicine and Surgery, Lewis Katz School of Medicine, Temple University, Philadelphia, PA 19140, USA. laurie.kilpatrick@temple.edu.

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