Tyrosine kinases phosphorylation

Tyrosine kinases phosphorylate protein tyrosine residues using ATP. Phospholipase C cleaves PIP2 into IP3 and PAG. 

Store it while it s here. Insulin binds to a specific receptor on the cell surface and exerts its metabolic effect by a signaling pathway that involves a receptor tyrosine kinase phosphorylation cascade. Note that insulin stimulates storage processes and at the same time inhibits degradative pathways. 

Type II interferon. Type I interferon binds to receptor, which in turn activates tyrosine kinase phosphorylation and the subsequent transcription pathway that induces viral resistance. Similarly, Type II interferon binds to another receptor and activates the immune response. 

Emerging Concepts of Platelet Activation Tyrosine Kinase Phosphorylation. 247... 

We have proposed a mechanism by which lL-1 exerts its deleterious effects on islet function and viability (Fig. 11 Corbett et al., 1992). In this proposed mechanism, lL-1 is released by macrophages during the initial stages of islet infiltration. IL-1 binds to a specific IL-1 receptors on the /3 cell activating a tyrosine kinase. Tyrosine kinase phosphorylation stimulates second messengers to induce the expression of c-/os, c-jun, the activation of NF-xB, and possibly other early transcriptional regulators. These early-immediate transcriptional response elements may activate or stimulate the expression of inducible nitric oxide... 

Receptor tyrosine kinase phosphorylates other proteins, for example, insulin receptor substrates (IRSs). 

Fig. 6-24 Schematic representation of the epidermal growth factor (EGF) receptor. The receptor is an integral membrane protein with a single transmembrane domain. The ligand binding site is in the extracellular domain and there is a tyrosine kinase domain near the C terminus in the cytoplasm, (a) At rest the receptor exists as single subunits. (b) Upon binding EGF, the receptor forms dimers stabilized by noncovalent associations. After dimerization the activated tyrosine kinase phosphorylates tyrosine residues in the cytoplasmic domain prior to the recruitment of further proteins to bind to the receptor. The formation of a protein assembly on the cytoplasmic domain is necessary for activation of enzymes that regulate cell metabolism and gene transcription.

Interferons There are two types of interferons Type I, which includes IFN-a and IFN- 3 and Type II consisting of IFN-y. IFN-a and (3 have about 30% homology in amino acid sequence. There are two more recently discovered Type I interferons they are called IFN-cu and IFN-x. IFN-a and IFN- 3 each have 166 amino acids, and IFN-y has 143. Both IFN-a and IFN- 3 are of single chain structure and bind to the same type of cell surface receptors, whereas IFN-y is a dimer of two identical chains and interacts with another type of receptors. All our cells can produce Type I interferons when infected by viruses, bacteria and fungi. Flowever, only T cells and natural killer cells can produce Type II interferon. Type I interferon binds to receptor, which in turn activates tyrosine kinase phosphorylation and the subsequent transcription pathway that induces viral resistance. Similarly, Type II interferon binds to another receptor and activates the immune response. 

Hanks, S.K. Calab, M.B. Harper, M.C. Patel, S.K. Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronec-tin. Proc. Natl. Acad. Sci. USA, 89, 8487-8491 (1992)... 

B. Effects Insulin has extremely important effects in almost every tissue of the body. The insulin receptor, a transmembrane tyrosine kinase, phosphorylates itself and a variety of mtracel-lular proteins when activated by the hormone. The major target organs for insulin action include the following ... 

SH2 domain array can be used for profiling general tyrosine phosphorylation with the antibody against phosphotyrosine and detecting specific tyrosine kinase phosphorylation with the antibody against specific active kinase. 

Despite a few claims that growth factor receptors are associated with caveolae, and the fact that tyrosine kinase phosphorylation of receptor in caveolae is rapidly induced upon PDGF or EGF stimulation of cells [16, 17], growth factor receptors are absent or barely detectable in GSL microdomain. A major question therefore remains How do GSLs affect growth factor receptor function We have no information as to whether ... 

Yano S, Herbst RS, Shinohara H, et al. Treatment for malignant pleural eflusion of human lung adenocarcinoma by inhibition of vascular endothelial growth factor receptor tyrosine kinase phosphorylation. Clin Cancer Res 2000 6 957-965. 

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