Beta-defensin 3 is a member of the defensin family. Defensin family is comprised by microbicidal and cytotoxic peptides made by neutrophils. Members of the beta-defensin 3 family are highly similar in protein sequence. Beta-defensin 3 shows antimicrobial activity against Gram-positive bacteria S.aureus and S.pyogenes, Gram-negative bacteria P.aeruginosa and E.coli and the yeast C.albicans. Beta-defensin 3 is abundantly expressed in skin and tonsils, and to a lesser extent in trachea, uterus, kidney, thymus, adenoid, pharynx and tongue. It is also expressed in salivary gland, bone marrow, colon, stomach, polyp and larynx. However, in small intestine, it cannot be detected. Defensin has broad spectrum antimicrobial activity and may play an important role in innate epithelial defense. Beta-defensin 3 kills multiresistant S.aureus and vancomycin-resistent E.faecium. It has no significant hemolytic activity.
Exhibits antimicrobial activity against Gram-negative bacteria and Gram-positive bacteria. May act as a ligand for C-C chemokine receptor CCR6. Can bind to both human and mouse CCR6 and induce chemotactic activity of CCR6-expressing cells.
Delta-like protein 1 (DLL1) is a type I transmembrane protein that belongs to the Delta/Serrate/Lag2 (DSL) family of Notch ligands. Mature human DLL1 consists of a 528 amino acid (aa) extracellular domain (ECD) with one DSL domain and eight EGF-like repeats, a 23 aa transmembrane segment, and a 155 aa cytoplasmic domain. Within the ECD, human DLL1 shares 91% aa sequence identity with mouse and rat DLL1. The residual membranebound portion of DLL1 can be cleave by presenilin-dependent γ-secretase, enabling the cytoplasmic domain to migrate to the nucleus. DLL1 localizes to adherens junctions on neuronal processes through its association with the scaffolding protein MAGI1. DLL1 is widely expressed, and it plays an important role in embryonic somite formation, cochlear hair cell differentiation, plus B and T lymphocyte differentiation. The upregulation of DLL1 in arterial endothelial cells following injury or angiogenic stimulation is central to postnatal arteriogenesis. DLL1 is also overexpressed in cervical carcinoma and glioma and contributes to tumor progression.
Delta-like protein 4 (DLL4) is a type I membrane protein belonging to the Delta/Serrate/Lag2 (DSL) family of Notch ligands. In mammals, four Notch homologs (Notch 1 to4) and five ligands (DLL 1, 3 and 4, Jagged 1 and 2) have been identified. DLL4 is expressed highly and selectively within the arterial endothelium and has been shown to function as a ligand for Notch 1 and Notch 4. Human and mouse DLL4 shares 86% amino acid sequence identity. Notch ligands are transmembrane proteins with a DSL motif necessary for Notch binding, tandem EGF repeats, a transmembrane region and a short intracellular domain (ICD). Notch ligands are categorized into two subfamilies based on the presence of an extracellular cysteinerich domain and insertions that interrupt some EGF repeats in the Jagged but not the Delta ligand family. Interactions of Notch receptors with their ligands result in reciprocal regulated intramembrane proteolysis (RIP). RIP is a mechanism for transmembrane signal transduction that involves the sequential processing by a disintegrin metalloprotease (ADAM) and then by presenilin/ γ secretase, resulting in shedding of the extracellular domains and the generation of the soluble ICD signaling fragments, respectively.
Deoxycytidine Kinase (DCK) is a member of the DCK/DGK family. DCK exists as a homodimer and is localized to the nucleus. DCK is required for the phosphorylation of the deoxyribonucleosides deoxycytidine (dC), deoxyguanosine (dG), and deoxyadenosine (dA). DCK has broad substrate specificity, and does not display selectivity based on the chirality of the substrate. In addition, DCK is also an essential enzyme for the phosphorylation of numerous nucleoside analogs widely employed as antiviral and chemotherapeutic agents. DCK is clinically important because of its relationship to drug resistance and sensitivity.
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.
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