| S100A11 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Aliases | S100A11 , HEL-S-43, MLN70, S100C, S100 calcium binding protein A11 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 603114 MGI: 3645720 HomoloGene: 55916 GeneCards: S100A11 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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| Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
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S100 calcium-binding protein A11 (S100A11) is a protein that in humans is encoded by the S100A11 gene. [4] [5]
The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100A11, also known as calgizzarin or 100C, is a small acidic protein. Along with all 13 members of the S100 family, are located as a cluster on chromosome 1q21. [6] It was first found in 1989, and later isolated from chicken gizzard muscles. [7]
The protein may function in motility, invasion, and tubulin polymerization. Chromosomal rearrangements and altered expression of this gene have been implicated in tumor metastasis. [5]
Its high expression has been found in many tissues including lung, pancreas, heart, placenta, kidney, and low levels in skeletal muscle, liver, and brain tissue. [8]
S100A11 is implicated in membrane and cytoskeletal dynamics, vesicular transportation and processes of endo and exocytosis. It has been shown that S100A11 interacts with many cytoskeletal structures as tubulin, actin, intermediate filaments also with annexin I and annexin II. [9] [10] S100A11 is able to control reorganization of actin and it is important in forming protrusion by metastatic cells. [11]
It lacks enzymatic activity, it functions by binding to other proteins, it regulates activity of other enzymes. [12] It is associated with cell cycle, growth, survival and apoptosis. It has been identified as dual growth mediator. [13] [6] Suppression of S100A11 by small interfering RNA caused cells to apoptosis, and overexpression of S100A11 has been found to inhibit apoptosis in tumor cells. [6] Furthermore, the knock-down of S100A11 via siRNA reduces the sister-chromatid exchange and the viability of cells.
IL-8 and TNF-alpha induce the expression and release of S100A11 in chondrocytes in culture and exogenous S100A11 causes chondrocyte hypertrophy. [14] S100A11 could play a role in maintaining low-grade inflammation in osteoarthritis and in its progression. [15]
Its cellular localization is associated with the regulation of cell growth and proliferation. This protein is normally found strictly in the nucleus, but appears in the cytoplasm in cancer cells. S100A11 was localized in the cytoplasm of resting human keratinocytes in vitro. [9]
It has been shown to interact with the RAGE receptor, which is also a receptor for other S100 proteins. [14]
It is associated with low or high production in many different types of cancers. Its overproduction has been found, for example, in breast, pancreas or colectal carcinoma and its levels can be used as clinical marker in these diseases. [7]
It has been shown that S100A11 enhances the recombination activity of human RAD51 in vitro. A knock-down leads to diffuse distribution of RAD54B. [16] These finding suggest a potential role of S100A11 in the process of homologous recombination repair of double-strand breaks. [17]
Usually, S100A11 makes homodimeres, but it has been shown that S100A11 heterodimerizes with S100B [18] and it also interacts with Nucleolin, [19] and RAD54B. [16]
Keratinocytes are the primary type of cell found in the epidermis, the outermost layer of the skin. In humans, they constitute 90% of epidermal skin cells. Basal cells in the basal layer of the skin are sometimes referred to as basal keratinocytes. Keratinocytes form a barrier against environmental damage by heat, UV radiation, water loss, pathogenic bacteria, fungi, parasites, and viruses. A number of structural proteins, enzymes, lipids, and antimicrobial peptides contribute to maintain the important barrier function of the skin. Keratinocytes differentiate from epidermal stem cells in the lower part of the epidermis and migrate towards the surface, finally becoming corneocytes and eventually be shed off, which happens every 40 to 56 days in humans.
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.
Annexin A2 also known as annexin II is a protein founded by Dr. Baogang Xu, that in humans is encoded by the ANXA2 gene.
Annexin A5 is a cellular protein in the annexin group. In flow cytometry, annexin V is commonly used to detect apoptotic cells by its ability to bind to phosphatidylserine, a marker of apoptosis when it is on the outer leaflet of the plasma membrane. The function of the protein is unknown; however, annexin A5 has been proposed to play a role in the inhibition of blood coagulation by competing for phosphatidylserine binding sites with prothrombin and also to inhibit the activity of phospholipase A1. These properties have been found by in vitro experiments.
S100 calcium-binding protein A7 (S100A7), also known as psoriasin, is a protein that in humans is encoded by the S100A7 gene.
S100 calcium-binding protein A2 (S100A2) is a protein that in humans is encoded by the S100A2 gene and it is located on chromosome 1q21 with other S100 proteins.
Annexin A6 is a protein that in humans is encoded by the ANXA6 gene.
S100 calcium-binding protein A8 (S100A8) is a protein that in humans is encoded by the S100A8 gene. It is also known as calgranulin A.
Protein S100-A1, also known as S100 calcium-binding protein A1 is a protein which in humans is encoded by the S100A1 gene. S100A1 is highly expressed in cardiac and skeletal muscle, and localizes to Z-discs and sarcoplasmic reticulum. S100A1 has shown promise as an effective candidate for gene therapy to treat post-myocardially infarcted cardiac tissue.
S100 calcium-binding protein A10 (S100A10), also known as p11, is a protein that is encoded by the S100A10 gene in humans and the S100a10 gene in other species. S100A10 is a member of the S100 family of proteins containing two EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells. They regulate a number of cellular processes such as cell cycle progression and differentiation. The S100 protein is implicated in exocytosis and endocytosis by reorganization of F-actin.
Involucrin is a protein component of human skin and in humans is encoded by the IVL gene. In binding the protein loricrin, involucrin contributes to the formation of a cell envelope that protects corneocytes in the skin.
S100 calcium-binding protein A6 (S100A6) is a protein that in humans is encoded by the S100A6 gene.
S100 calcium-binding protein P (S100P) is a protein that in humans is encoded by the S100P gene.
Sorcin is a protein that in humans is encoded by the SRI gene.
Fatty acid-binding protein, epidermal is a protein that in humans is encoded by the FABP5 gene.
S100 calcium-binding protein A13 (S100A13) is a protein that in humans is encoded by the S100A13 gene.
S100 calcium-binding protein A3 (S100A3) is a protein that in humans is encoded by the S100A3 gene.
Envoplakin is a protein that in humans is encoded by the EVPL gene.
Annexin A9 is a protein that in humans is encoded by the ANXA9 gene.
The S100 calcium-binding protein mS100a7a15 is the murine ortholog of human S100A7 (Psoriasin) and human S100A15 (Koebnerisin). mS100a7a15 is also known as S100a15, mS100a7 and mS100a7a and is encoded by the mS100a7a gene
