Biomaterial Database

Enhancement of the phosphorylation of membrane bound myosin light chain by antigen stimulation in rat basophilic leukemia cells. 1989

R Teshima, and K Suzuki, and H Ikebuchi, and T Terao

Division of Radiochemistry, National Institute of Hygienic Sciences, Tokyo, Japan.

We have found that phosphorylation of the 18,000 mol. wt protein in rat basophilic leukemia cells (RBL-2H3 cells) is enhanced by stimulation by an antigen. This phenomenon was also observed when cells were treated with phorbol myristate (TPA) and a calcium ionophor, A23187. The phosphorylated 18,000 mol. wt protein was mainly located in the membrane fraction. It was identified as one of the myosin light chains as follows: (1) the mol. wt of one of the major myosin light chains of RBL-2H3 cells was 18,000; (2) more than half of the phosphorylated 18,000 mol. wt protein was recovered in an actomyosin fraction; (3) this phosphorylated 18,000 mol. wt protein was immunoprecipitated with anti-myosin antibody. Since the presence of Ca2+ in the cell culture medium was essential for the phosphorylation of the 18,000 mol. wt protein and, since trifluoperazine (a potent inhibitor of calmodulin as well as of the degranulation process of RBL-2H3 cells) inhibited the reaction, the phosphorylation may be catalyzed by a Ca2+-calmodulin-dependent process, most likely by myosin light chain kinase. These results, together with our previous observation [Teshima et al. Molec Immun. 23, 279-284 (1986)], suggest that simultaneous phosphorylation of the 18,000 mol. wt myosin light chain and a 36,000 mol. wt membranous protein is a prerequisite for the degranulation of RBL-2H3 cells.

UI	MeSH Term	Description	Entries
D008970	Molecular Weight	The sum of the weight of all the atoms in a molecule.	Molecular Weights,Weight, Molecular,Weights, Molecular
D009218	Myosins	A diverse superfamily of proteins that function as translocating proteins. They share the common characteristics of being able to bind ACTINS and hydrolyze MgATP. Myosins generally consist of heavy chains which are involved in locomotion, and light chains which are involved in regulation. Within the structure of myosin heavy chain are three domains: the head, the neck and the tail. The head region of the heavy chain contains the actin binding domain and MgATPase domain which provides energy for locomotion. The neck region is involved in binding the light-chains. The tail region provides the anchoring point that maintains the position of the heavy chain. The superfamily of myosins is organized into structural classes based upon the type and arrangement of the subunits they contain.	Myosin ATPase,ATPase, Actin-Activated,ATPase, Actomyosin,ATPase, Myosin,Actin-Activated ATPase,Actomyosin ATPase,Actomyosin Adenosinetriphosphatase,Adenosine Triphosphatase, Myosin,Adenosinetriphosphatase, Actomyosin,Adenosinetriphosphatase, Myosin,Myosin,Myosin Adenosinetriphosphatase,ATPase, Actin Activated,Actin Activated ATPase,Myosin Adenosine Triphosphatase
D009363	Neoplasm Proteins	Proteins whose abnormal expression (gain or loss) are associated with the development, growth, or progression of NEOPLASMS. Some neoplasm proteins are tumor antigens (ANTIGENS, NEOPLASM), i.e. they induce an immune reaction to their tumor. Many neoplasm proteins have been characterized and are used as tumor markers (BIOMARKERS, TUMOR) when they are detectable in cells and body fluids as monitors for the presence or growth of tumors. Abnormal expression of ONCOGENE PROTEINS is involved in neoplastic transformation, whereas the loss of expression of TUMOR SUPPRESSOR PROTEINS is involved with the loss of growth control and progression of the neoplasm.	Proteins, Neoplasm
D010446	Peptide Fragments	Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.	Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D010766	Phosphorylation	The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.	Phosphorylations
D002462	Cell Membrane	The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.	Plasma Membrane,Cytoplasmic Membrane,Cell Membranes,Cytoplasmic Membranes,Membrane, Cell,Membrane, Cytoplasmic,Membrane, Plasma,Membranes, Cell,Membranes, Cytoplasmic,Membranes, Plasma,Plasma Membranes
D002478	Cells, Cultured	Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.	Cultured Cells,Cell, Cultured,Cultured Cell
D004591	Electrophoresis, Polyacrylamide Gel	Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.	Polyacrylamide Gel Electrophoresis,SDS-PAGE,Sodium Dodecyl Sulfate-PAGE,Gel Electrophoresis, Polyacrylamide,SDS PAGE,Sodium Dodecyl Sulfate PAGE,Sodium Dodecyl Sulfate-PAGEs
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D000941	Antigens	Substances that are recognized by the immune system and induce an immune reaction.	Antigen