DNase1, also known as deoxyribonuclease I and DNL1, is a member of the DNase family. DNaseI is a nuclease that cleaves DNA preferentially at phosphodiester linkages adjacent to a pyrimidine nucleotide, yielding 5'-phosphate-terminated polynucleotides with a free hydroxyl group on position 3', on average producing tetranucleotides. DNaseI binds to the cytoskeletal protein actin. It binds actin monomers with very high (sub-nanomolar) affinity and actin polymers with lower affinity. Mutations in DNase1 gene have been associated with systemic lupus erythematosus (SLE), an autoimmune disease. DNase1 is used to treat the one of the symptoms of cystic fibrosis by hydrolyzing the extracellular DNA in sputum and reducing its viscosity.
Dermatopontin, also known as Tyrosine-rich acidic matrix protein, TRAMP and DPT, is a secreted protein which belongs to the dermatopontin family. DPT is expressed in various tissues, such as fibroblasts, heart, skeletal muscle, brain and pancreas. It seems to mediate adhesion by cell surface integrin binding. DPT may serve as a communication link between the dermal fibroblast cell surface and its extracellular matrix environment. DPT can enhance TGFB1 activity through interaction with decorin. In addition, DPT accelerates collagen fibril formation, stabilizes collagen fibrils against low-temperature dissociation and inhibits cell proliferation.
Desmin is a cytoplasmic protein and belongs to the intermediate filament family. interacts with DST and MTM1. Desmin is only expressed in vertebrates, however homologous proteins are found in many organisms. Desmin is the main intermediate filament in mature skeletal, cardiac and smooth-muscle cells. DES founctions as homopolymers to form a stable intracytoplasmic filamentous network connecting myofibrils to each other and to the plasma membrane. .Defects in DES are cause of the myopathy myofibrillar type 1, cardiomyopathy dilated type 1I, and neurogenic scapuloperoneal syndrome Kaeser type.
DNA Fragmentation Factor Subunit Alpha (DFFA). DFFA exists as a heterodimer (DFF) with DFFB. DFF is activated once DFFA is cleaved by Caspase-3. The cleaved fragments of DFFA detach from DFFB (the active component of DFF), which in turn triggers DNA fragmentation as well as chromatin condensation during apoptosis. A reduced level of DFFA detected in ovarian endometriosis may be a part of an apoptosis-resistant mechanism enhancing the disease progression.
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