Activators & Inhibitors

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.

Cytochrome b5 (CYB5A) is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases. CYB5A contains one cytochrome b5 heme-binding domain and has two isoforms produced by alternative splicing. Isoform 1 is a sngle-pass membrane protein. Isoform 2 is located in cytoplasm. The defects in CYB5A can result in type IV hereditary methemoglobinemia.

L-Lactate Dehydrogenase A Chain (LDHA) is an enzyme that catalyzes the conversion of L-lactate and NAD+ to pyruvate and NADH in the final step of anaerobic glycolysis. LDHA contains an N-terminal coenzyme binding region, a central catalytic site, and at least nine utilized Lys acetylation and two Tyr phosphorylation sites. LDHA belongs to the lactate dehydrogenase family, expressed predominantly in muscle tissue. LDHA mutations have been linked to exertional myoglobinuria.

Hypoxanthine-Guanine Phosphoribosyltransferase (HGPRT) has an important role in the generation of purine nucleotides through the purine salvage pathway. HPRT1 functions to salvage purines from degraded DNA to renewed purine synthesis, it acts as a catalyst in the reaction between guanine and phosphoribosyl pyrophosphate to form GMP.

Aminoglycoside 3'-phosphotransferase (APH(3')), also known as aminoglycoside kinase, is an aminoglycoside-modifying enzyme and widely presented in resistant bacteria. These ATP-dependent enzymes phosphorylate the 3'-hydroxyl of a variety of aminoglycosides including kanamycins, neomycins, paromomycins, neamine, ribostamycin, geneticin, and paromamine. These phosphorylated aminoglycosides fail to bind to their respective ribosomal binding sites with high affinity; hence resistance is conferred to the drugs that are phosphorylated. APH(3') is primarily found in certain species of gram-positive bacteria.

Phosphoglycerate kinase 1(PGK1) is an enzyme. It is mainly expressed in spermatogonia and Localized on the principle piece in the sperm. Its expression significantly decreased in the testis of elderly men. PGK1 involved in a critical energy-producing process known as glycolysis. It helps carry out a chemical reaction that converts a molecule called 1,3-diphosphoglycerate, which is produced during the breakdown of glucose, to another molecule called 3-phosphoglycerate during glycolysis. PGK1 may also act as a cofactor for polymerase alpha. The protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions.

Haptoglobin(HP) is a secreted protein which is a member of the peptidase S1 family of serine proteases. As a result of hemolysis, hemoglobin is found to accumulate in the kidney and is secreted in the urine. Haptoglobin captures, and combines with free plasma hemoglobin to allow hepatic recycling of heme iron and to prevent kidney damage. Haptoglobin also acts as an Antimicrobial; Antioxidant has antibacterial activity and plays a role in modulating many aspects of the acute phase response. Hemoglobin/haptoglobin complexes are rapidely cleared by the macrophage CD163 scavenger receptor expressed on the surface of liver Kupfer cells through an endocytic lysosomal degradation pathway. Uncleaved haptoglogin, also known as zonulin, plays a role in intestinal permeability, allowing intercellular tight junction disassembly, and controlling the equilibrium between tolerance and immunity to non-self antigens.

Serine Protease Inhibitor Kazal-Type 1 (SPINK1) is a trypsin inhibitor that prevent the trypsin-catalyzed premature activation of zymogens within the pancreas. Defects in SPINK1 are a cause of pancreatitis (PCTT). A disease characterized by the presence of calculi in pancreatic ducts. It causes severe abdominal pain attacks. Defects in SPINK1 are the cause of susceptibility to tropical calcific pancreatitis (TCP). Recombinant SPINK1 protein (rSPINK1) stimulated cell proliferation in benign RWPE as well as cancerous prostate cells. The research result indicated that the potential of SPINK1 as an extracellular therapeutic target in prostate cancer. In contrast, knockdown of SPINK1 in 22RV1 cells inhibited cell proliferation, cell invasion, and tumor growth in xenograft assays.

Kininogen-1 is a secreted protein which contains three cystatin domains. There are two alternatively spliced forms, designated as the high molecular weight (HMW) and low MW (LMW) forms. Kininogen-1 plays a critical role in blood coagulation and inflammatory response. Kininogens are inhibitors of thiol proteases. Kininogen-1 participates in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII, also inhibits the thrombin- and plasmin-induced aggregation of thrombocytes. The active peptide bradykinin that is released from Kininogen-1 shows a variety of physiological effects: influence in smooth muscle contraction, induction of hypotension, natriuresis and diuresis, decrease in blood glucose level. It is a mediator of inflammation and causes increase in vascular permeability, stimulation of nociceptors release of other mediators of inflammation. It has a cardioprotective effect. LMW-kininogen inhibits the aggregation of thrombocytes and doesn’t