RUNX3, also called CBFA3, AML-2 or PEBP2-alpha C, is a member of the Runt domain family of nuclear transcriptional regulators. All of the RUNX proteins form dimers with CBF-beta. The runt domain (aa 54-186) is required for DNA binding, while a pro/ser/thr-rich region (aa 191-415) transcriptionally activates target genes. Isoform 2 has an alternate 19 aa in place of the N-terminal 5 aa of isoform 1. The 415 aa Human RUNX3 shares 91% aa identity with mouse or rat RUNX3. RUNX3 is necessary for growth control of gastric epithelium, neurogenesis of dorsal root ganglia, and T cell differentiation. RUNX3 expression is frequently mutated in tumors and appears to be silenced by methylation.
S100 proteinis a family of low molecular weight protein found in vertebrates characterized by twoEF-hand calcium-binding motifs. There are at least 21 different S100 proteins, and the name is derived from the fact that the protein is100%soluble in ammonium sulfateat neutralpH. S100 proteins have been implicated in a variety of intracellular and extracellular functions. They are involved in regulation of protein phosphorylation, transcription factors, the dynamics of cytoskeleton constituents, enzyme activities, cell growth and differentiation, and the inflammatory response. Protein S100-A10, also known as Calpactin I light chain, Cellular ligand of annexin II, ANX2LG and S100A10, is a member of the S100 family. In contrast to all other S100 proteins, S100A10 is Ca(2+) insensitive because of amino acid replacements in its Ca(2+)-binding loops that lock the protein in a permanently active state. S100A10 forms a heterotetramer with annexin IIH and promotes carcinoma invasion and metastasis by plasminogen activation. S100A10 and annexin II contribute to the aggressive characteristics of anaplastic carcinoma, while playing a constitutive role in papillary carcinoma. S100A10 induces the dimerization of ANXA2 / p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target of tyrosine-specific kinase. S100A10 functions as a linker tethering certain transmembrane proteins to annexin A2 thereby assisting their traffic to the plasma membrane and/or their firm anchorage at certain membrane sites.
S100A11 is a member of the S100 family of calcium binding proteins. Human S100A11 contains two EF hand motifs and shares 82% amino acid sequence identity with mouse and rat S100A11. It forms covalent homodimers upon transglutamination and also disulfide-linked tetramers. S100A11 is secreted by keratinocytes and can be crosslinked into the cornified envelope of the skin. Dimerization enhances its ability to signal through RAGE on keratinocytes, induce the production of EGF family proteins, and induce cell proliferation. Dimerization also enables S100A11 to bind RAGE on chondrocytes, leading to chondrocyte hypertrophy and catabolism of the cartilage matrix. S100A11 is additionally found in the cytosol where it becomes phosphorylated and translocates to the nucleus in response to DNA damage, RELM alpha exposure, or elevated extracellular calcium concentrations. Calcium also promotes S100A11 association with S100B as well as Annexins A1, A2, and A6. S100A11-Annexin A2 complexes are recruited to sites of plasma membrane damage where they facilitate membrane repair in migrating cancer cells. S100A11 is upregulated in various cancers and supports tumor cell proliferation, invasion, and migration. In addition, S100A11 is produced in the ovary, and it acts on cumulus cells to inhibit oocyte fertilization.
Facilitates the differentiation and the cornification of keratinocytes.
S100 proteinis a family of low molecular weight protein found in vertebrates characterized by twoEF-hand calcium-binding motifs. There are at least 21 different S100 proteins, and the name is derived from the fact that the protein is100%soluble in ammonium sulfateat neutralpH. Most S100 proteins are disulfide-linked homodimer, and is normally present in cells derived from theneural crest, chondrocytes, macrophages, dendritic cells, etc. S100 proteins have been implicated in a variety of intracellular and extracellular functions. They are involved in regulation of protein phosphorylation, transcription factors, the dynamics of cytoskeleton constituents, enzyme activities, cell growth and differentiation, and the inflammatory response. Protein S100-A12, also known as S100 calcium-binding protein A12, Calcium-binding protein in amniotic fluid 1, Calgranulin-C, and S100A12, is a member of the S-101 family. Like the majority of S100 proteins, S100A12 is a dimer, with the interface between the two subunits being composed mostly of hydrophobic residues. The fold of S100A12 is similar to the other known crystal and solution structures of S100 proteins, except for the linker region between the two EF-hand motifs. S100A12 plays an important role in the inflammatory response.
There are at least 21 different S100 proteins and the protein is 100% soluble in ammonium sulfate at neutral pH. S100 proteins play a role in regulation of protein phosphorylation, transcription factors, the dynamics of cytoskeleton constituents, enzyme activities, cell growth and differentiation, and the inflammatory response. S100A12 is characterized by two EF-hand calcium-binding motifs, zinc- and copper-binding protein.S100A12 is a disulfide-linked homodimer and the interface between the two subunits is composed mostly of hydrophobic residues.Its proinflammatory activity involves recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. EN-RAGE acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to receptor for advanced glycation endproducts (AGER). Binding to AGER activates the MAP-kinase and NF-kappa-B signaling pathways leading to production of proinflammatory cytokines and up-regulation of cell adhesion molecules ICAM1 and VCAM1. It also acts as a monocyte and mast cell chemoattractant. Moreover, it can stimulate mast cell degranulation and activation which generates chemokines, histamine and cytokines inducing further leukocyte recruitment to the sites of inflammation. It can inhibit the activity of matrix metalloproteinases; MMP2, MMP3 and MMP9 by chelating Zn2+ from their active sites.
Inserisci la tua e-mail e seleziona le aree di interesse per ricevere le ultime novità, approfondimenti e promozioni.
Seleziona uno o più ambiti di interesse per ricevere comunicazioni più utili e mirate.
2025 TEMA Ricerca - All Rights Reserved.
