SerpinC1, also known as antithrombin III (AT III), is a member of the serpin superfamily of serine protease inhibitors, and has been found to be a marker for disseminated intravascular coagulation (DIC) and to be of prognostic significance in septic patients. SerpinC1 synthesized in the liver is the principal plasma serpin of blood coagulation proteases and inhibits thrombin and other factors such as Xa by the formation of covalently linked complexes. Thus it is one of the most important coagulation inhibitors and the fundamental enzyme for the therapeutical action of heparin. In common with SerpinA5 and D1, the inhibitory activity of SerpinC1 undergoes a dramatic increase in the presence of heparin and other glycosaminoglycans. ATIII mediates the promotion of prostaglandin release, an inhibitor of leucocyte activation and downregulator of many proinflammatory cytokines. Antithrombin III exerts anti-inflammatory properties in addition to its anti-coagulative mechanisms. In animal models of sepsis, ATIII affected cytokine plasma concentrations with a decrease of pro-inflammatory cytokines. The deficiency or functional abnormality of ATIII may result in an increased risk of thromboembolic disease, such as deep vein thrombosis and pulmonary embolism. In addition, it has been reported that SerpinC1 can alter or influence inflammatory processes via inhibition of NF-&kappa,B activation or actin polymerization.
Annexin V predicts a molecular mass of 36.8 kDa. 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. Annexin V forms a shield around negatively charged phospholipid molecules. The formation of an annexin V shield blocks the entry of phospholipids into coagulation reactions.
Amyloid β A4 Precursor Protein-Binding Family A Member 3 (APBA3) is an adapter protein that belongs to the X11 family. APBA3 contains 2 PDZ (DHR) domains and 1 PID domain and interacts with the Alzheimer's disease amyloid precursor protein.. APBA3 is believed to be involved in signal transduction processes. Unlike X11-α and -β which are generally neuronal proteins, APBA3 is widely expressed in all tissues examined with lower levels in brain and testis. It binds to the cytoplasmic domain of amyloid protein (APP) in vivo and may modulate processing of the β-amyloid precursor protein (APP) and hence formation of β-APP.
APC is a ubiquitous, tumor-suppressor protein that is mutated in most colon cancers, generally resulting in a gene product that is truncated in the carboxy terminal region. APC contains several binding domains. The region used as an immunogen overlaps the EB1, DLG (PDZ sequence), and PSD-93 domains. These domains bind microtubules, mitotic spindles, and F-actin and are involved in cell cycle, division, and migration. The immunogen does not include the beta-catenin-binding region, which antagonizes Wnt signaling. The human APC amino acid sequence used as immunogen is 83% and 86% identical to mouse and rat APC, respectively.
Serum Amyoid P Component (SAP) is a monomeric 25 kDa secreted serum glycoprotein that belongs to the pentraxins family. The members of pentaxin superfamily be characterised by calcium dependent ligand binding and distinctive flattened β-jellyroll structure similar to that of the legume lectins. SAP is a non-fibrillar component; it can interact with DNA and histones. It regulates the solubility of amyloid fibrils and protects them from degradation by proteolytic enzymes and phagocytic cells. SAP scavenge nuclear material released from damaged circulating cells. It has been proposed that SAP may function as an opsonin for a variety of ligands including autoantigens; apoptotic cells; chromatin and micro-organisms.
Apurinic-Apyrimidinic Endonuclease 1 (APE1) is required for efficient DNA base excision repair. When the DNA glycosylase remove the damaged bases; APE1 cleaves the AP site to allow resynthesis and ligation to complete repair. APE1 stimulates the DNA binding activity of many transcription factors; which participate in cancer promotion and progression. APE1 regulates the redox state of multiple transcription factors; such as c-Jun; c-Fos; NF-kB; p53. APEN is also involved in calcium-dependent down-regulation of PTH expression.
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