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Lactate dehydrogenase (LDH) is an enzyme(EC1.1.1.27) present in a wide variety of organisms, including plants and animals.
A tetrameric enzyme that catalyses the interconversion of pyruvateand lactate with concomitant interconversion of NADH and NAD+. At high concentrations of pyruvate, the enzyme exhibits feedback inhibition and the rate of conversion of pyruvate to lactate is decreased. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.

IFIH1 is a DEAD box protein which is upregulated in response to treatment with beta-interferon and a protein kinase C-activating compound, mezerein. Irreversible reprogramming of melanomas can be attained by therapy with both these agents; treatment with either agent alone only achieves reversible differentiation. DEAD box proteins are implicated in several cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly.

Formiminotransferase cyclodeaminase is an enzyme which catalyzes the conversion of formiminoglutamateand tetrahydrofolateinto formiminotetrahydrofolateand glutamate.
Formiminotransferase cyclodeaminase, a bifunctional enzyme of tetrahydrofolate synthesis, is the target antigen of anti-LC1 (liver cytosol antigen type 1) autoantibodies. Presence of LC1 autoantibodies is a marker for type 2 autoimmune hepatitis (for which anti-LKM 1/cytochrome P450 2D6 autoantibodies are a further marker).
Serum LC1 autoantibody concentrations appear to fluctuate in parallel with aminotransferase levels, a particularly intriguing observation that suggests a possible role of LC1 autoreactivity in the pathogenic mechanism leading to hepatocyte injury.

Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Members of the defensin family are highly similar in protein sequence. This gene encodes defensin, beta 103A, which has broad spectrum antimicrobial activity and may play an important role in innate epithelial defense.

GPD2 (Mitochondrial glycerol-3-phosphate dehydrogenase) is a Ca2+-sensitive, FAD-binding protein, which is located on the outer surface of the inner mitochondrial membrane. Two isoforms have been identified for mGPD: Isoform 1 is comprised of 727 a.a. residues, while isoform 2 lacks 126 a.a. residues of the N-terminus. GPD2 catalyses the oxidation of glycerol-3-phosphate to DHAP (dihydroxyacetone phosphate) with associated reduction of the enzyme-bound FAD. GPD2 is a testis-specific promoter of mitochondrial GPDH. GPD2 along with a cytosolic NAD-linked GPD forms the glycerol phosphate shuttle that uses the interconversion of G-3-P and DHAP to transfer reducing equivalents into mitochondria, which results in the reoxidation of NADH produced during glycolysis.
GPD2 deficiency contributes to the impairment of glucose-stimulated INS discharge in a number of animal models of non-INS dependent diabetes mellitus. GPD2 up-regulation as a result of a highly glycolytic environment contributes to the general increase in ROS generation and may lead to the progression of prostate cancer.

VEGF-D belongs to the VEGF/PDGF family of proteins. VEGF-D promotes lymphangiogesis, endothelial cell growth, and regulates vascular permeability. In addition, VEGF-D has an important part in the creation of the venous and lymphatic vascular systems and in the growth and maintenance of differentiated lymphatic endothelium Mature VEGF-D forms a noncovalently linked homodimer, and binds to and activate both VEGFR-2 (flk1) and VEGFR-3 (flt4).

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 (NDUFA5) is a member of the complex I NDUFA5 subunit family. The human NDUFA5 gene codes for the B13 subunit of complex I of the respiratory chain that transfers electrons from NADH to ubiquinone. The NDUFA5 protein localizes to the inner mitochondrial membrane as part of the seven component-containing, water soluble 'iron-sulfur protein' (IP) fraction of complex I, even though its exact role is undetermined.

SORD, also referred to as sorbitol dehydrogenase, belongs to the zinc-containing alcohol dehydrogenase family. It is widely produced. The lens of the eyeand the kidney are the protein highest production areas. Zinc-dependent interconversion of polyols, like sorbitol and xylitol, are enzymatically catalysed to their respective ketoses by SORD.

Caused by one of four closely related virus serotypes of the genus Flavivirus, family Flaviviridae, each serotype is sufficiently different that there is no cross-protection and epidemics caused by multiple serotypes (hyperendemicity) can occur. In cell culture experiments and mice Morpholino antisense oligos have shown specific activity against Dengue virus.

PDIA3 is an enzyme that belongs to the endoplasmic reticulum and interacts with lectin chaperones calreticulin and calnexin to modulate folding of newly synthesized glycoproteins. PDIA3 has protein disulfide isomerase activity. Complexes of lectins and PDIA3 mediate protein folding by promoting formation of disulfide bonds in their glycoprotein substrates. PDIA3 is expressed in the lumbar spinal cord from rats submitted to peripheral lesion during neonatal period. PDIA3 interacts with thiazide-sensitive sodium-chloride cotransporter in the kidney and is induced by glucose deprivation. PDIA3 is part of the major histocompatibility complex (MHC) class I peptide-loading complex (TAP1), which is important for formation of the final antigen conformation and export from the endoplasmic reticulum to the cell surface.

QDPR belongs to the short-chain dehydrogenases/reductase (SDR) family of enzymes. Operating as a homodimer, QDPR has an imperative role in the recycling of tetrahydrobiopterin (BH4), a vital cofactor for the hydroxylation of the aromatic amino acids (tryptophan, tyrosine and phenylalanine). More precisely, QDPR catalyzes the regeneration of BH4 from quinonoid dihydrobiopterin (qBH2), the product generated from the hydroxylation reactions. Mutations in the QDPR gene may lead to phenylketonuria II.

HPGD is the essential enzyme of prostaglandin degradation. 15-PGDH protein strongly decreases the biologic activity of these molecules by catalyzing the oxidation of the 15-hydroxyl group of prostaglandins to a keto group. GDH1 is involved in numerous physiologic and cellular processes, for instance inflammation.

The fasting-induced adipose factor (FIAF, ANGPTL4, PGAR, HFARP) was identified as an adipocytokine up-regulated by fasting, by peroxisome proliferator-activated receptor agonists, and by hypoxia. At the protein level, in human and mouse blood plasma, FIAF was found to be present both as a native protein and in a truncated form. Differentiation of mouse 3T3-L1 adipocytes was associated with the production of truncated FIAF, whereas in human white adipose tissue and SGBS adipocytes, only the native FIAF could be detected. Interestingly, the truncated FIAF was produced by human liver.
Experimental data suggest that FIAF is mainly presented in human blood plasma in a truncated form (FIAF-S2), whose level is increased by fenofibrate treatment. Levels of both truncated and native FIAF showed marked inter individual variation but were not associated with body mass index and were not influenced by prolonged semistarvation.

Delta-Like4, also known as DLL4 is implicated in the Notch signaling pathway as Notch ligand. Consequently DLL4 negatively regulates endothelial cell proliferation, migration as well as angiogenic sprouting. DLL4 is vital for retinal progenitor proliferation and also required for suppressing rod fates in late retinal progenitors and for proper generation of other retinal cell types. Furthermore, at some stage in the spinal cord neurogenesis, DLL4 inhibits V2a interneuron fate.

UBE2K belongs to the ubiquitin-conjugating enzymes family which take part in many cellular processes such as selective protein degradation, DNA repair, cell cycle control, and sporulation. In this mechanism, the ATP-coupled activation and subsequent ligation of ubiquitin are catalyzed by separate enzymes functionally linked by ubiquitin carrier protein UBC1. In addition, UBE2K is involved in Alzheimer's disease, Huntington's disease and antigen processing through its interaction with amyloid-?, huntingtin, and MHC-heavy chain proteins.

UBE2D2 belongs to the E2 ubiquitin-conjugating enzyme family. UBE2D2 takes part in the ubiquitination of the tumor-suppressor protein p53, which is induced by an E3 ubiquitin-protein ligase. UBE2D2 catalyzes ubiquitination of IkB-alpha in a SCFB-TRCP and phosphorylation dependent method.

Ketohexokinase catalyzes the phosphorylation of fructose to produce fructose-1-phosphate, resulting in the utilization of ATP and creation of AMP. Ketohexokinase commences initial step in the metabolism of dietary fructose and is a significant regulator of hepatic glucose metabolism. Ketohexokinase is found in liver, renal cortex, and small intestine. Its deficiency causes the benign hereditary metabolic disorder essential fructosuria, leading to fructose being excreted in the urine. Ketohexokinase-dependent metabolism of fructose induces proinflammatory mediators in proximal tubular cells. ketohexokinase plays an unknown physiologic function that remains intact in essential fructosuria. Ketohexokinase expression is reduceed in human clear cell type of renal cell carcinoma.

IMPDH1 is a rate limiting enzyme in the de novo synthesis of guanine nucleotides and consequently participates in the regulation of cell growth. IMPDH1 takes part in the development of malignancy and the growth progression of some tumors. IMPDH1 performs as a homotetramer to regulate cell growth. IMPDH1 catalyzes the synthesis of xanthine monophosphate (XMP) from inosine-5''-monophosphate (IMP). Defects in this gene are a cause of retinitis pigmentosa type 10 (RP10).

IMPDH2 is a member of the IMPDH/GMPR family. IMPDH2 catalyzes the NAD-dependent oxidation of inosine-5'-monophosphate into xanthine-5'-monophosphate, which is afterward converted into guanosine-5'-monophosphate. IMPDH2 is the rate-limiting enzyme in the de novo guanine nucleotide biosynthesis. IMPDH2 is consequently involved in maintaining cellular guanine deoxy- and ribonucleotide pools required for DNA and RNA synthesis. In addition, IMPDH1 and IMPDH2 are targets for the important immunosuppressive drug, MPA. Furthermore, the IMPDH2 gene is up-regulated in some neoplasms, suggesting it may have a role in malignant transformation.

Sarcoglycan Delta (SGCD) is one of the four known components of the sarcoglycan complex, which is a subcomplex of the dystrophin-glycoprotein complex (DGC) and is expressed mainly in skeletal and cardiac muscle. DGC forms a link between the F-actin cytoskeleton and the extracellular matrix. SGCD protein’s mutations have been associated with autosomal recessive limb-girdle muscular dystrophy and dilated cardiomyopathy. SGCD gene expression is regulated by MITF In melanocytic cells.

GPD1 enzyme catalyzes the reduction of dihydroxyacetone phosphate to sn-glycerol 3-phosphate. (sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH) previous names for glycerol-3-phosphate dehydrogenase include alpha glycerol-3-phosphate dehydrogenase and glycerolphosphate dehydrogenase. However, GPD1 differs from glyceraldehyde 3-phosphate dehydrogenase (GAPDH) whose substrate is an aldehyde not an alcohol.

Aldo-keto reductase family 1 member C1 or AKR1C1 is an enzyme, part of the aldo/keto reductase family that holds over 40 familiar proteins. AKR1C1 promotes the conversion of ketones & aldehydes to their alcohol forms by using cofactors such as NADH & NADPH. AKR1C1 promotes the progesterone reduction to its inactive molecule form 20-alpha-hydroxy-progesterone.

HDL is a complex of lipids and proteins in approximately equal amounts that functions as a transporter of cholesterol in the blood. HDL is the smallest of the lipoprotein particles; it’s the densest because it contains the highest proportion of protein. The liver synthesizes these lipoproteins as complexes of apolipoproteins and phospholipid, which bear a resemblance to cholesterol-free flattened spherical lipoprotein particles. They pick up cholesterol; carry it internally, from cells by interaction with the ATP Binding Cassette Transporter A1. Lecithin-cholesterol acyltransferase (plasma enzyme) converts the free cholesterol into cholesteryl ester (a more hydrophobic form of cholesterol) which is then sequestered into the core of the lipoprotein particle ultimately making the newly synthesized HDL spherical. They increase in size as they pass through the bloodstream and integrate more cholesterol and phospholipid molecules from cells and other lipoproteins, for instance by the interaction with the ABCG1 transporter and the phospholipid transport protein. HDL transports their cholesterol generally to the liver or steroidogenic organs such as adrenals, ovary and testes by direct and indirect pathways. The release of HDL cholesterol to adrenals, ovaries and testes is important for the synthesis of steroid hormones. Since the triglycerides are not stable in HDL, they’re degraded by hepatic lipase in order that finally small HDL particles are left which resume the uptake of cholesterol from cells. The cholesterol supplied to the liver is excreted into the bile and consequently intestine either directly or indirectly after conversion into bile acids. High levels of HDL are associated with a decreased risk of atherosclerosis and coronary heart disease.