Related Experiment Video
Updated: Jul 19, 2026
03:23
Three-Dimensional Cell Culture Models to Investigate the Epithelial Barrier in Eosinophilic Esophagitis
Published on: May 10, 2024
Role of protein kinase C in eosinophil function
Takafumi Yamaguchi1, Masato Suzuki, Hirokazu Kimura
1Gunma Prefectural Institute of Public Health and Environmental Sciences, Gunma, Japan.
Summary
Protein kinase C (PKC) isoforms are crucial for eosinophil functions. This review summarizes current knowledge on how different PKC isoforms impact eosinophil cell dynamics and inflammatory responses.
Area of Science:
- Immunology
- Cell Biology
- Biochemistry
Background:
- Protein kinase C (PKC) comprises a diverse family of enzymes crucial for cell signaling.
- Eleven PKC isoforms are classified into conventional, novel, and atypical groups based on structure and activation.
- Eosinophils play key roles in allergic diseases and parasitic infections.
Purpose of the Study:
- To review and summarize the current understanding of Protein Kinase C (PKC) isoform involvement in eosinophil functions.
- To highlight the significance of PKC in eosinophil dynamics, including cell motility and inflammatory responses.
Main Methods:
- This review synthesizes findings from recent studies utilizing selective activators and inhibitors of individual PKC isoforms.
- Literature search and critical analysis of existing research on PKC and eosinophils.
Main Results:
- PKC isoforms are implicated in regulating various eosinophil functions.
- Specific PKC isoforms influence eosinophil motility and other critical cellular processes.
- The precise roles of all PKC isoforms in eosinophil biology require further elucidation.
Conclusions:
- Protein Kinase C (PKC) signaling pathways are integral to eosinophil function.
- Understanding specific PKC isoform roles is essential for developing targeted therapies for allergic and inflammatory conditions.
- Further research is needed to fully delineate the complex interplay between PKC isoforms and eosinophils.
Related Concept Videos
01:25cAMP-dependent Protein Kinase Pathways
Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
01:22Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal
Erythropoietin-producing hepatocellular carcinoma receptor (Eph) and its ligand, Eph receptor-interacting protein (Ephrin) were first discovered in the human carcinoma cell line, hence the name. Ephrin-Eph interaction guides cells to reach their appropriate location in adult tissues. They also play an essential role in the immune system by helping in immune cell migration, adhesion, and activation. Based on their structure and function, Eph is divided into two classes — EphA and EphB.
02:54Protein Kinases and Phosphatases
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
02:54Protein Kinases and Phosphatases
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
01:22Amplifying Signals via Enzymatic Cascade
When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...
01:16Calmodulin-dependent Signaling
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...