Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization. May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity.
S100-B; is an acidic protein with a molecular weight of 21 kDa belonging to the S100 family. S100-B contains two EF-hand-type calcium-binding motifs separated by a hinge region with a hydrophobic cleft. S100-B plays an important role in neurodevelopment; differentiation; and brain construction. S100-B has neuroprotective effects; but at high concentrations S100-B is neurotoxic. Extracellular concentration of S100-B increases following brain damage; which easily penetrates into cerebrospinal fluid in brain damage and then into the blood. S100-B is expressed and produced by astrocytes in vertebrate brains and in the CNS; and the astrocytes are the major cells producing S100-B protein in gray matter; as well as oligodendrocytes are the predominant S100-B in protein producing cells in white matter. The major advantage of using S100-B is that elevations in serum or CSF levels provide a sensitive measure for determining CNS injury at the molecular level before gross changes develop; enabling timely delivery of crucial medical intervention before irreversible damage occurs. In addition; S100-B; which is also present in human melanocytes; is a reliable marker for melanoma malignancy both in bioptic tissue and in serum.
S100B is a member of the S100 family of proteins containing two EF-hand-type calcium-binding motifs. S100B exerts both intracellular and extracellular functions. Intracellular S100B acts as a stimulator of cell proliferation and migration and an inhibitor of apoptosis and differentiation, which might have important implications during brain, cartilage and skeletal muscle development and repair, activation of astrocytes in the course of brain damage and neurodegenerative processes, and of cardiomyocyte remodeling after infarction, as well as in melanomagenesis and gliomagenesis. As an extracellular factor, S100B engages RAGE (receptor for advanced glycation end products) in a variety of cell types with different outcomes depending on the concentration attained by the protein, the cell type and the microenvironment. This calcium binding astrocyte-specific cytokine, presents a marker of astrocytic activation and reflects CNS injury. The excellent sensitivity of S100B has enabled it to confirm the existence of subtle brain injury in patients with mild head trauma, strokes, and after successful resuscitation from cardiopulmonary arrest. Recent findings provide evidence, that S100B may decrease neuronal injury and/or contribute to repair following traumatic brain injury (TBI). Hence, S100B, far from being a negative determinant of outcome, as suggested previously in the human TBI and ischemia literature, is of potential therapeutic value that could improve outcome in patients who sustain various forms of acute brain damage.
Protein S100-P; also known as Protein S100-E; S100 calcium-binding protein P; S100P and S100E; is a nucleus and cytoplasm protein which belongs to theS-100 family. S100P / S100E contains twoEF-hand domains. S100P protein regulates calcium signal transduction and mediates cytoskeletal interaction; protein phosphorylation and transcriptional control. S100P / S100E overexpression can upregulate androgen receptor expression and thereby promote prostate cancer progression by increasing cell growth. S100P / S100E may directly confer resistance to chemotherapy. S100P / S100E induction may be considered an important step in the initial stage of lung adenocarcinomas; whereas its downregulation in advanced stages seems to be important for tumour progression in which DNA methylation and/or feedback transcription processes play a critical role. S100P / S100E plays a major role in the aggressiveness of pancreatic cancer that is likely mediated by its ability to activate RAGE. Interference with S100P / S100E may provide a novel approach for treatment of pancreatic cancer. S100P / S100E could be considered a potential drug target or a chemosensitization target; and could also serve as a biomarker for aggressive; hormone-refractory and metastatic prostate cancer.
Protein S100-P (S100P) belongs to the S100 family of Calcium-Binding Proteins. S100P is 95 amino acids in length and it contains 2 EF-Hand Calcium-Binding Motifs. The EF-Hand Motif binds calcium; which likely alters molecular conformation. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells and it is involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. In addition to binding Ca; S100P also binds Zn and Mg; and may play a role in the etiology of prostate cancer.
Serum amyloid A-2 protein (SAA2) belongs to the SAA family. It expressed by the liver and secreted in plasma. SAA2 functions as major acute phase reactant and could works as apolipoprotein of the HDL complex. Increased levels of A-SAA in serum are indicative of inflammatory disease. When highly expressed, SAA can displace ApoA1 as the major apolipoprotein in HDL complexes, weakening the function of HDL as a reverse (lipid clearing) cholesterol transporter. A highly charged region of SAA2 and SAA1 (aa 36-68) contains putative fibronectin- and laminin-binding motifs. This region also binds heparin sulfate proteoglycans at mildly acidic pH and promotes aggregation of A-SAA.
Has transcriptional repressor activity. Overexpression inhibits the transcriptional activities of AP-1, p53/TP53 and CDKN1A.
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