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A431 cells were established from an epidermoid carcinoma in the skin of an 85- year-old female patient. Epidermal growth factor (EGF) stimulation of A431 cells induces rapid tyrosine phosphorylation of intracellular signaling proteins which control cellular processes such as growth, proliferation and apoptosis.
In electrically non-excitable cells (i.e., blood cells), Ca 2+ influx is essential for regulating a host of kinetically distinct processes involving exocytosis, enzyme control, gene regulation, cell growth and proliferation, and apoptosis. Capacitative calcium entry appears to also be a major means of signal transduction.
BK channels are associated and modulated by a wide variety of intra- and extracellular factors, such as auxiliary subunits (β, γ), Slobs (slo binding protein), phosphorylation, membrane voltage, chemical ligands (Ca²⁺, Mg²⁺), PKC, The BK α-subunits assemble 1:1 with four different auxiliary types of β-subunits (β1, β2, β3 or β4).
Many different calcium-binding proteins exist, with different cellular and tissue distribution and involvement in specific functions. Calcium binding proteins also serve an important physiological role for cells. [2] The most ubiquitous Ca 2+-sensing protein, found in all eukaryotic organisms including yeasts, is calmodulin.
It is composed of 116 amino acids and is produced by parafollicular cells (C cells) of the thyroid and by the neuroendocrine cells of the lung and the intestine. The level of procalcitonin in the blood stream of healthy individuals is below the limit of detection (0.01 μg/L) of clinical assays. [3]
Calcium signaling is the use of calcium ions (Ca 2+) to communicate and drive intracellular processes often as a step in signal transduction. Ca 2+ is important for cellular signalling , for once it enters the cytosol of the cytoplasm it exerts allosteric regulatory effects on many enzymes and proteins .
When an antigen-presenting cell interacts with a T cell receptor on T cells, there is an increase in the cytoplasmic level of calcium, which activates calcineurin by binding a regulatory subunit and activating calmodulin binding. [3] Calcineurin induces transcription factors that are important in the transcription of IL-2 genes. IL-2 activates ...
Osteonectin is a 40 kDa acidic and cysteine-rich glycoprotein consisting of a single polypeptide chain that can be broken into 4 domains: 1) a Ca 2+ binding domain near the glutamic acid-rich region at the amino terminus (domain I), 2) a cysteine-rich domain (II), 3) a hydrophilic region (domain III), and 4) an EF hand motif at the carboxy terminus region (domain IV).