IkappaBgamma is expressed in mast cells

Michael G Haase1, Anke Klawitter, Gustavo B Baretton

  • 1Department of Pathology, Dresden University of Technology, Fetscherstrasse 74, 01307 Dresden, Germany. michael.haase@mailbox.tu-dresden.de

IkappaBgamma (IkappaBgamma) is a 70-kDa protein that is encoded by the C-terminal part of the NF-kappaB p105 gene and acts as an inhibitor of the transcription factor NF-kappaB. Until now, IkappaBgamma expression has only been described in cell-culture models of B-lymphocytes and enterocytes but not in tissues. In a model of radiation-induced pulmonary damage, we found that mast cells accumulating after irradiation are the only cells in the rat lung that are positive for IkappaBgamma. The mast cells were characterised by their metachromatic staining with toluidine blue and by double immunofluorescence labelling with mast-cell tryptase. Western blotting revealed that the lung mast cells expressed the 70-kDa form of IkappaBgamma cytoplasmatically and that no alternative splicing variants were expressed. In addition, we studied 11 cases of systemic mastocytosis, as well as 5 cases of mast-cell hyperplasia. In all cases, the mast cells stained strongly with IkappaBgamma. Rat peritoneal mast cells also contained high levels of IkappaBgamma. Since NF-kappaB is an important regulator of mast-cell functions, IkappaBgamma is likely to play a central role in the maintenance of the mast-cell phenotype and possibly in the modification of mast-cell-dependent immune responses.

Related Concept Videos

Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Transcytosis of IgG01:15

Transcytosis of IgG

Transcytosis is the process in which molecules are internalized by endocytosis, transported across the cell, and released through exocytosis from the opposite end of the cell. Molecules such as insulin, immunoglobulins, and certain nutrients are transferred through the recycling endosomes by recycling and transcytosis.
IgG molecules from a mother undergo transcytosis starting around 13 weeks of gestation. The amount of IgG transferred and entering the fetal blood circulation increases with...
IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and produces two-second...
Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal01:22

Role 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.
Rab Proteins01:14

Rab Proteins

Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...