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S100A7
S100 calcium-binding protein A7 (S100A7), also known as psoriasin, is a protein that in humans is encoded by the ''S100A7'' gene. Function S100A7 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. This protein differs from the other S100 proteins of known structure in its lack of calcium binding ability in one EF-hand at the N-terminus. The protein functions as a prominent antimicrobial peptide mainly against '' E. coli''. S100A7 also displays antimicrobial properties. It is secreted by epithelial cells of the skin and is a key antimicrobial protein against ''Escherichia coli'' by disrupting their cell membranes. This is the reason that in countries w ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
S100A15
S100 calcium-binding protein A15 (S100A15), also known as koebnerisin and S100 calcium-binding protein A7A (S100A7A), is a protein that in humans is encoded by the ''S100A7A'' (alias:''S100A15'') gene. S100 proteins are a diverse calcium-binding family that regulate fundamental cellular and extracellular processes including cell proliferation and differentiation, cell migration, and the antimicrobial host defense as antimicrobial peptides. Koebnerisin (S100A15) was first identified upregulated in inflammation-prone psoriatic skin, suggesting involvement in the lesional phenotype of the disease, Koebner phenomenon. Today, the protein is of further interest because of its role in antimicrobial defence, innate immunity, epidermal cell maturation and epithelial tumorigenesis. Function Epithelial homeostasis and antimicrobial host defense ''Skin'': In normal epidermis, koebnerisin (S100A15) is expressed by epidermal basal and differentiated keratinocytes, melanocytes, and Lang ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Koebnerisin
S100 calcium-binding protein A15 (S100A15), also known as koebnerisin and S100 calcium-binding protein A7A (S100A7A), is a protein that in humans is encoded by the ''S100A7A'' (alias:''S100A15'') gene. S100 proteins are a diverse calcium-binding family that regulate fundamental cellular and extracellular processes including cell proliferation and differentiation, cell migration, and the antimicrobial host defense as antimicrobial peptides. Koebnerisin (S100A15) was first identified upregulated in inflammation-prone psoriatic skin, suggesting involvement in the lesional phenotype of the disease, Koebner phenomenon. Today, the protein is of further interest because of its role in antimicrobial defence, innate immunity, epidermal cell maturation and epithelial tumorigenesis. Function Epithelial homeostasis and antimicrobial host defense ''Skin'': In normal epidermis, koebnerisin (S100A15) is expressed by epidermal basal and differentiated keratinocytes, melanocytes, and Lange ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
S100 Protein
The S100 proteins are a family of low molecular-weight proteins found in vertebrates characterized by two calcium-binding sites that have helix-loop-helix (" EF-hand-type") conformation. At least 21 different S100 proteins are known. They are encoded by a family of genes whose symbols use the ''S100'' prefix, for example, ''S100A1'', ''S100A2'', ''S100A3''. They are also considered as damage-associated molecular pattern molecules (DAMPs), and knockdown of aryl hydrocarbon receptor downregulates the expression of S100 proteins in THP-1 cells. Structure Most S100 proteins consist of two identical polypeptides (homodimeric), which are held together by noncovalent bonds. They are structurally similar to calmodulin. They differ from calmodulin, though, on the other features. For instance, their expression pattern is cell-specific, i.e. they are expressed in particular cell types. Their expression depends on environmental factors. In contrast, calmodulin is a ubiquitous and univer ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
FABP5
Fatty acid-binding protein, epidermal is a protein that in humans is encoded by the ''FABP5'' gene. Function This gene encodes the fatty acid binding protein found in epidermal cells, and was first identified as being upregulated in psoriasis tissue. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. It is thought that FABPs roles include fatty acid uptake, transport, and metabolism. The phytocannabinoids (THC and CBD) inhibit endocannabinoid anandamide (AEA) uptake by targeting FABP5, and competition for FABPs may in part or wholly explain the increased circulating levels of endocannabinoids reported after consumption of cannabinoids. Results show that cannabinoids inhibit keratinocyte proliferation, and therefore support a potential role for cannabinoids in the treatment of psoriasis. Interactions FABP5 has been shown to interact with S100A7 S100 calcium-binding pr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
COP9 Constitutive Photomorphogenic Homolog Subunit 5
COP9 constitutive photomorphogenic homolog subunit 5 (Arabidopsis), also known as COPS5 or Csn5, is a gene conserved from humans to Saccharomyces cerevisiae. Function The protein encoded by this gene is one of the eight subunits of COP9 signalosome, a highly conserved protein complex that functions as an important regulator in multiple signaling pathways. The structure and function of COP9 signalosome is similar to that of the 19S regulatory particle of 26S proteasome. COP9 signalosome has been shown to interact with SCF-type E3 ubiquitin ligases and act as a positive regulator of E3 ubiquitin ligases. This protein is reported to be involved in the degradation of cyclin-dependent kinase inhibitor CDKN1B/p27Kip1. It is also known to be a coactivator that increases the specificity of JUN/AP1 transcription factors. Interactions COP9 constitutive photomorphogenic homolog subunit 5 has been shown to interact with Macrophage migration inhibitory factor, GFER, BCL3, Ubiquitin c ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
RANBP9
Ran-binding protein 9 is a protein that in humans is encoded by the ''RANBP9'' gene. Function This gene encodes a protein that binds RAN, a small GTP binding protein belonging to the RAS superfamily that is essential for the translocation of RNA and proteins through the nuclear pore complex. The protein encoded by this gene has also been shown to interact with several other proteins, including met proto-oncogene, homeodomain interacting protein kinase 2, androgen receptor, and cyclin-dependent kinase 11. Interactions RANBP9 has been shown to interact with: * Androgen receptor, * C-Met, * DISC1, * DYRK1B, * Glucocorticoid receptor, * HIPK2 * MKLN1, * S100A7 S100 calcium-binding protein A7 (S100A7), also known as psoriasin, is a protein that in humans is encoded by the ''S100A7'' gene. Function S100A7 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 pro ..., and * USP11. References Further reading * * * ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
RAGE (receptor)
RAGE ( receptor for advanced glycation endproducts), also called AGER, is a 35 kilodalton transmembrane receptor of the immunoglobulin super family which was first characterized in 1992 by Neeper ''et al.'' Its name comes from its ability to bind advanced glycation endproducts ( AGE), which include chiefly glycoproteins, the glycans of which have been modified non-enzymatically through the Maillard reaction. In view of its inflammatory function in innate immunity and its ability to detect a class of ligands through a common structural motif, RAGE is often referred to as a pattern recognition receptor. RAGE also has at least one other agonistic ligand: high mobility group protein B1 ( HMGB1). HMGB1 is an intracellular DNA-binding protein important in chromatin remodeling which can be released by necrotic cells passively, and by active secretion from macrophages, natural killer cells, and dendritic cells. The interaction between RAGE and its ligands is thought to result in p ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
EF Hand
The EF hand is a helix–loop–helix structural domain or ''motif'' found in a large family of calcium-binding proteins. The EF-hand motif contains a helix–loop–helix topology, much like the spread thumb and forefinger of the human hand, in which the Ca2+ ions are coordinated by ligands within the loop. The motif takes its name from traditional nomenclature used in describing the protein parvalbumin, which contains three such motifs and is probably involved in muscle relaxation via its calcium-binding activity. The EF-hand consists of two alpha helices linked by a short loop region (usually about 12 amino acids) that usually binds calcium ions. EF-hands also appear in each structural domain of the signaling protein calmodulin and in the muscle protein troponin-C. Calcium ion binding site The calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cytoplasm
In cell biology, the cytoplasm is all of the material within a eukaryotic cell, enclosed by the cell membrane, except for the cell nucleus. The material inside the nucleus and contained within the nuclear membrane is termed the nucleoplasm. The main components of the cytoplasm are cytosol (a gel-like substance), the organelles (the cell's internal sub-structures), and various cytoplasmic inclusions. The cytoplasm is about 80% water and is usually colorless. The submicroscopic ground cell substance or cytoplasmic matrix which remains after exclusion of the cell organelles and particles is groundplasm. It is the hyaloplasm of light microscopy, a highly complex, polyphasic system in which all resolvable cytoplasmic elements are suspended, including the larger organelles such as the ribosomes, mitochondria, the plant plastids, lipid droplets, and vacuoles. Most cellular activities take place within the cytoplasm, such as many metabolic pathways including glycolysis, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cell Nucleus
The cell nucleus (pl. nuclei; from Latin or , meaning ''kernel'' or ''seed'') is a membrane-bound organelle found in eukaryotic cells. Eukaryotic cells usually have a single nucleus, but a few cell types, such as mammalian red blood cells, have no nuclei, and a few others including osteoclasts have many. The main structures making up the nucleus are the nuclear envelope, a double membrane that encloses the entire organelle and isolates its contents from the cellular cytoplasm; and the nuclear matrix, a network within the nucleus that adds mechanical support. The cell nucleus contains nearly all of the cell's genome. Nuclear DNA is often organized into multiple chromosomes – long stands of DNA dotted with various proteins, such as histones, that protect and organize the DNA. The genes within these chromosomes are structured in such a way to promote cell function. The nucleus maintains the integrity of genes and controls the activities of the cell by regulating gene ex ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cell Cycle
The cell cycle, or cell-division cycle, is the series of events that take place in a cell that cause it to divide into two daughter cells. These events include the duplication of its DNA (DNA replication) and some of its organelles, and subsequently the partitioning of its cytoplasm, chromosomes and other components into two daughter cells in a process called cell division. In cells with nuclei ( eukaryotes, i.e., animal, plant, fungal, and protist cells), the cell cycle is divided into two main stages: interphase and the mitotic (M) phase (including mitosis and cytokinesis). During interphase, the cell grows, accumulating nutrients needed for mitosis, and replicates its DNA and some of its organelles. During the mitotic phase, the replicated chromosomes, organelles, and cytoplasm separate into two new daughter cells. To ensure the proper replication of cellular components and division, there are control mechanisms known as cell cycle checkpoints after each of the key s ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cellular Differentiation
Cellular differentiation is the process in which a stem cell alters from one type to a differentiated one. Usually, the cell changes to a more specialized type. Differentiation happens multiple times during the development of a multicellular organism as it changes from a simple zygote to a complex system of tissues and cell types. Differentiation continues in adulthood as adult stem cells divide and create fully differentiated daughter cells during tissue repair and during normal cell turnover. Some differentiation occurs in response to antigen exposure. Differentiation dramatically changes a cell's size, shape, membrane potential, metabolic activity, and responsiveness to signals. These changes are largely due to highly controlled modifications in gene expression and are the study of epigenetics. With a few exceptions, cellular differentiation almost never involves a change in the DNA sequence itself. Although metabolic composition does get altered quite dramatical ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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