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.
Human Deoxyhypusine Synthase (DHS) is vital for the first step of hypusine biosynthesis. DHS catalyzes the NAD-dependent oxidative cleavage of spermidine, the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.
Amiloride-sensitive amine oxidase (AOC1) belongs to the copper/topaquinone oxidase family. The protein exists as homodimer by disulfide and mainly located in placenta and kidney. AOC1 catalyzes the degradation of compounds such as putrescine, histamine, spermine, and spermidine, substances involved in allergic and immune responses, cell proliferation, tissue differentiation, tumor formation, and possibly apoptosis. Placental DAO is thought to play a role in the regulation of the female reproductive function. The activity of this protein can be inhibited by amiloride in a competitive manner. It is inhibited by amiloride, a diuretic that acts by closing epithelial sodium ion channels.
Dickkopf-related protein 1(DKK-1), is a member of the dickkopf family. DKK1 secreted proteins with two cysteine-rich domains separated by a linker region. It antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease.
Dihydropteridine reductase, also known as HDHPR and Quinoid dihydropteridine reductase, QDPR and DHPR, belongs to the short-chain dehydrogenases/reductases (SDR) family. QDPR exists as a homodimer. QDPR is part of the pathway that recycles a substance called tetrahydrobiopterin, also known as BH4 and tryptophan hydroxylases. The regeneration of this substance is critical for the proper processing of several other amino acids in the body. Tetrahydrobiopterin also helps produce certain chemicals in the brain called neurotransmitters, which transmit signals between nerve cells. Defects in QDPR are the cause of BH4-deficient hyperphenylalaninemia type C (HPABH4C) which is a rare autosomal recessive disorder and is lethal.
DIM1, also known as TXNL4A, is a member of the Dim protein family. The Dim protein family is composed of two classes, DIM1and Dim2, which share a common thioredoxin-like fold. They were originally identified for their role in cell cycle progression and have been found to interact with Prp6, an essential component of the spliceosome, which forms the bridge of U4/U6.U5-tri-snRNP. In spite of their biological and structural similarities, DIM1 and Dim2 proteins differ in many aspects. DIM1 bears distinctive structural motifs responsible for its interaction with other spliceosome components. Dim2 forms homodimers and contains specific domains required for its interactions with partners. This originality suggests that although both proteins are involved in pre-mRNA splicing, they are likely to be involved in different biological pathways. DIM1 interacts with HNRPF, HNRPH2, NEDD9/HEF1 and PQBP1/NPW38. It plays an essential role in pre-mRNA splicing.
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