- brush border assembly
The aggregation, arrangement and bonding together of adjacent microvilli through the formation of Ca(2+)-dependent adhesion links between them, forming a brush border.
- adenylate cyclase-activating adrenergic receptor signaling pathway involved in cardiac muscle relaxation
An adrenergic receptor signaling pathway that contributes to a reduction in cardiac muscle contraction. Beta-adrenergic receptor-induced cardiac relaxation is achieved by a GPCR-activated adenylate cyclase generating cAMP; cAMP then activates the cAMP-dependent protein kinase A (PKA), which phosphorylates the sarcoplasmic reticulum (SR) membrane protein PLB. In its non-phosphorylated state, PLB acts as an inhibitor of the ATPase Ca(2+) pump of the cardiac SR (SERCA2a); inhibition of the pump is relieved upon phosphorylation. The pump removes Ca(2+) from the cytoplasm, thereby preventing cytosolic Ca(2+)-dependent activation of contractile proteins, leading to enhanced muscle relaxation.
- intermicrovillar adhesion
The cell-cell adhesion process by which adjacent microvilli attach to each other through Ca(2+)-dependent adhesion links made of protocadherin-24 and mucin-like protocadherin.
- calcium ion transport
The directed movement of calcium (Ca) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
- calprotectin complex
A protein complex composed of S100A8 and S100A9 and capable of limiting Mn(2+) and Zn(2+) availability at sites of infection. Also binds Ca(2+). Expressed and released by neutrophils and epithelial cells, it exhibits broad-spectrum antimicrobial activity attributed to its metal-binding properties. Endogenous ligand of toll-like receptor 4 (TLR4) and of the receptor for advanced glycation end products (RAGE) initiating signal transduction through NF-kappa-B pathways.
- calcineurin-NFAT signaling cascade
Any intracellular signal transduction in which the signal is passed on within the cell by activation of a member of the NFAT protein family as a consequence of NFAT dephosphorylation by Ca(2+)-activated calcineurin. The cascade begins with calcium-dependent activation of the phosphatase calcineurin. Calcineurin dephosphorylates multiple phosphoserine residues on NFAT, resulting in the translocation of NFAT to the nucleus. The cascade ends with regulation of transcription by NFAT. The calcineurin-NFAT cascade lies downstream of many cell surface receptors, including G protein-coupled receptors (GPCRs) and receptor tyrosine kinases (RTKs) that signal to mobilize calcium ions (Ca2+).
- calcineurin-mediated signaling
Any intracellular signal transduction in which the signal is passed on within the cell by activation of a transcription factor as a consequence of dephosphorylation by Ca(2+)-activated calcineurin. The process begins with calcium-dependent activation of the phosphatase calcineurin. Calcineurin is a calcium- and calmodulin-dependent serine/threonine protein phosphatase with a conserved function in eukaryotic species from yeast to humans. In yeast and fungi, calcineurin regulates stress signaling and cell cycle, and sporulation and virulence in pathogenic fungi. In metazoans, calcineurin is involved in cell commitment, organogenesis and organ development and immune function of T-lymphocytes. By a conserved mechanism, calcineurin phosphatase activates fungal Crz1 and mammalian NFATc by dephosphorylation and translocation of these transcription factors to the nucleus to regulate gene expression.