A family of enzymes accepting a wide range of substrates, including phenols, alcohols, amines, and fatty acids. They function as drug-metabolizing enzymes that catalyze the conjugation of UDPglucuronic acid to a variety of endogenous and exogenous compounds. EC 2.4.1.17.
A nucleoside diphosphate sugar which serves as a source of glucuronic acid for polysaccharide biosynthesis. It may also be epimerized to UDP iduronic acid, which donates iduronic acid to polysaccharides. In animals, UDP glucuronic acid is used for formation of many glucosiduronides with various aglycones.
Glycosides of GLUCURONIC ACID formed by the reaction of URIDINE DIPHOSPHATE GLUCURONIC ACID with certain endogenous and exogenous substances. Their formation is important for the detoxification of drugs, steroid excretion and BILIRUBIN metabolism to a more water-soluble compound that can be eliminated in the URINE and BILE.
A familial form of congenital hyperbilirubinemia transmitted as an autosomal recessive trait. It is characterized by icterus and brain damage caused by a glucuronyl transferase deficiency in the liver and faulty bilirubin conjugation.
Derivatives of GLUCURONIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that include the 6-carboxy glucose structure.
Mutant strain of Rattus norvegicus which is used as a disease model of kernicterus.
A benign familial disorder, transmitted as an autosomal dominant trait. It is characterized by low-grade chronic hyperbilirubinemia with considerable daily fluctuations of the bilirubin level.
Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough.
A bile pigment that is a degradation product of HEME.
A condition characterized by an abnormal increase of BILIRUBIN in the blood, which may result in JAUNDICE. Bilirubin, a breakdown product of HEME, is normally excreted in the BILE or further catabolized before excretion in the urine.
Uridine Diphosphate (UDP) sugars are nucleotide sugars that serve as essential glycosyl donors in the biosynthesis of various glycoconjugates, including proteoglycans and glycoproteins.
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
The chemical alteration of an exogenous substance by or in a biological system. The alteration may inactivate the compound or it may result in the production of an active metabolite of an inactive parent compound. The alterations may be divided into METABOLIC DETOXICATION, PHASE I and METABOLIC DETOXICATION, PHASE II.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
An alkaloid isolated from the stem wood of the Chinese tree, Camptotheca acuminata. This compound selectively inhibits the nuclear enzyme DNA TOPOISOMERASES, TYPE I. Several semisynthetic analogs of camptothecin have demonstrated antitumor activity.
Proteins prepared by recombinant DNA technology.
The rate dynamics in chemical or physical systems.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
The regular and simultaneous occurrence in a single interbreeding population of two or more discontinuous genotypes. The concept includes differences in genotypes ranging in size from a single nucleotide site (POLYMORPHISM, SINGLE NUCLEOTIDE) to large nucleotide sequences visible at a chromosomal level.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
The study of natural phenomena by observation, measurement, and experimentation.
The deposit of SEMEN or SPERMATOZOA into the VAGINA to facilitate FERTILIZATION.
A plant genus of the family ASCLEPIADACEAE.

Regulation and function of family 1 and family 2 UDP-glucuronosyltransferase genes (UGT1A, UGT2B) in human oesophagus. (1/1925)

Human UDP-glucuronosyltransferases (UGTs) are expressed in a tissue-specific fashion in hepatic and extrahepatic tissues [Strassburg, Manns and Tukey (1998) J. Biol. Chem. 273, 8719-8726]. Previous work suggests that these enzymes play a protective role in chemical carcinogenesis [Strassburg, Manns and Tukey (1997) Cancer Res. 57, 2979-2985]. In this study, UGT1 and UGT2 gene expression was investigated in human oesophageal epithelium and squamous-cell carcinoma in addition to the characterization of individual UGT isoforms using recombinant protein. UGT mRNA expression was characterized by duplex reverse transcriptase-PCR analysis and revealed the expression of UGT1A7, UGT1A8, UGT1A9 and UGT1A10 mRNAs. UGT1A1, UGT1A3, UGT1A4, UGT1A5 and UGT1A6 transcripts were not detected. UGT2 expression included UGT2B7, UGT2B10 and UGT2B15, but UGT2B4 mRNA was absent. UGT2 mRNA was present at significantly lower levels than UGT1 transcripts. This observation was in agreement with the analysis of catalytic activities in oesophageal microsomal protein, which was characterized by high glucuronidation rates for phenolic xenobiotics, all of which are classical UGT1 substrates. Whereas UGT1A9 was not regulated, differential regulation of UGT1A7 and UGT1A10 mRNA was observed between normal oesophageal epithelium and squamous-cell carcinoma. Expression and analysis in vitro of recombinant UGT1A7, UGT1A9, UGT1A10, UGT2B7 and UGT2B15 demonstrated that UGT1A7, UGT1A9 and UGT1A10 catalysed the glucuronidation of 7-hydroxybenzo(alpha)pyrene, as well as other environmental carcinogens, such as 2-hydroxyamino-1-methyl-6-phenylimidazo-(4, 5-beta)-pyridine. Although UGT1A9 was not regulated in the carcinoma tissue, the five-fold reduction in 7-hydroxybenzo(alpha)pyrene glucuronidation could be attributed to regulation of UGT1A7 and UGT1A10. These data elucidate an individual regulation of human UGT1A and UGT2B genes in human oesophagus and provide evidence for specific catalytic activities of individual human UGT isoforms towards environmental carcinogens that have been implicated in cellular carcinogenesis.  (+info)

Hyaluronan synthase expression in bovine eyes. (2/1925)

PURPOSE: Hyaluronan (HA), a high-molecular-weight linear glycosaminoglycan, is a component of the extracellular matrix (ECM). It is expressed in eyes and plays important roles in many biologic processes, including cell migration, proliferation, and differentiation. Hyaluronan is produced by HA synthase (HAS), which has three isoforms: HAS1, HAS2, and HAS3. In this study, the HAS expression in the anterior segment of bovine eyes was investigated to determine the significance of HA in eyes. METHODS: To obtain bovine HAS probes, degenerate oligonucleotide primers, based on well-conserved amino acid sequences including the catalytic region of each HAS isoform, were used for reverse transcription-polymerase chain reaction to amplify mRNA from bovine corneal endothelial cells (BCECs). Hyaluronan synthase-1 expression in the anterior segment of bovine eyes at the protein level was investigated by immunohistochemistry. RESULTS: All three HAS isoforms were expressed in BCECs at the mRNA level. Amplified cDNA fragments of HAS1, HAS2, and HAS3 from BCECs can be aligned to human counterparts, showing similarities of 100%, 97.3%, and 100%, respectively, at the amino acid level. Hyaluronan synthase 1 was expressed at the protein level in corneal epithelium, keratocyte, corneal endothelium, conjunctival epithelium, ciliary epithelium, capillary endothelium, and trabecular meshwork. CONCLUSIONS: Hyaluronan synthase isoforms were expressed in the ocular anterior segment and are speculated to be involved in HA production in situ.  (+info)

Overproduction of hyaluronan by expression of the hyaluronan synthase Has2 enhances anchorage-independent growth and tumorigenicity. (3/1925)

Hyaluronan (HA) has long been implicated in malignant transformation and tumor progression. However, due to the lack of molecular tools to directly manipulate production of HA, which does not require a core protein for its synthesis, our understanding of the role of HA in tumor cells has been largely circumstantial. In this study, we genetically manipulated the production of HA by transfection of a mammalian HA synthase Has2 into human HT1080 cells and examined the malignant phenotype of transfected cells. We found that increased production of HA promotes anchorage-independent growth and tumorigenicity of the cells. Has2-transfected cells formed greater numbers of colonies in semisolid medium. Tumors in nude mice derived from Has2-transfected cells grew more rapidly and were 2-4 times larger than those derived from control cells at termination of experiments. Histological and biochemical analyses of tumors revealed no significant differences in cell density and tissue structures between them, indicating that the larger size of the tumors was due to enhanced cell proliferation, not to increased accumulation of tumor stroma or increased angiogenesis. These results demonstrate that HA production by tumor cells per se promotes proliferation of these cells in tissues and provides direct evidence for the role of HA in tumorigenicity.  (+info)

Formation of HNK-1 determinants and the glycosaminoglycan tetrasaccharide linkage region by UDP-GlcUA:Galactose beta1, 3-glucuronosyltransferases. (4/1925)

While expression-cloning enzymes involved in heparan sulfate biosynthesis, we isolated a cDNA that encodes a protein 65% identical to the UDP-GlcUA:glycoprotein beta1, 3-glucuronosyltransferase (GlcUAT-P) involved in forming HNK-1 carbohydrate epitopes (3OSO3GlcUAbeta1,3Gal-) on glycoproteins. The cDNA contains an open reading frame coding for a protein of 335 amino acids with a predicted type II transmembrane protein orientation. Cotransfection of the cDNA with HNK-1 3-O-sulfotransferase produced HNK-1 carbohydrate epitopes in Chinese hamster ovary (CHO) cells and COS-7 cells. In vitro, a soluble recombinant form of the enzyme transferred GlcUA in beta-linkage to Galbeta1,3/4GlcNAcbeta-O-naphthalenemethanol, which resembles the core oligosaccharide on which the HNK-1 epitope is assembled. However, the enzyme greatly preferred Galbeta1, 3Galbeta-O-naphthalenemethanol, a disaccharide component found in the linkage region tetrasaccharide in chondroitin sulfate and heparan sulfate. During the course of this study, a human cDNA clone was described that was thought to encode UDP-GlcUA:Galbeta1,3Gal-R glucuronosyltransferase (GlcUAT-I), involved in the formation of the linkage region of glycosaminoglycans (Kitagawa, H., Tone, Y., Tamura, J., Neumann, K. W., Ogawa, T., Oka, S., Kawasaki, T., and Sugahara, K. (1998) J. Biol. Chem. 273, 6615-6618). The deduced amino acid sequences of the CHO and human cDNAs are 95% identical, suggesting that they are in fact homologues of the same gene. Transfection of a CHO cell mutant defective in GlcUAT-I with the hamster cDNA restored glycosaminoglycan assembly in vivo, confirming its identity. Interestingly, transfection of the mutant with GlcUAT-P also restored glycosaminoglycan synthesis. Thus, both GlcUAT-P and GlcUAT-I have overlapping substrate specificities. However, the expression of the two genes was entirely different, with GlcUAT-I expressed in all tissues tested and GlcUAT-P expressed only in brain. These findings suggest that, in neural tissues, GlcUAT-P may participate in both HNK-1 and glycosaminoglycan production.  (+info)

(TA)8 allele in the UGT1A1 gene promoter of a Caucasian with Gilbert's syndrome. (5/1925)

BACKGROUND AND OBJECTIVE: Gilbert's syndrome, a chronic non-hemolytic unconjugated hyperbilirubinemia, is caused by a reduction in the activity of hepatic bilirubin UDP-glucuronosyltransferase (UGT1A1). This reduction has been shown to be due to a polymorphism in the promoter region of the UGT1A1 gene. The presence of seven thymine adenine (TA) repeats reduces the efficiency of transcription of the UGT1A1 gene. To elucidate the genetic background of a patient affected by Gilbert's syndrome, we collected blood samples from family members for the analysis of the A(TA)nTAA motif in the promoter region of the UGT1A1 gene. DESIGN AND METHODS: Analysis of the A(TA)nTAA motif in the promoter region of the UGT1A1 gene was performed by PCR. Estimation of UGT1A1 promoter containing the variable (TA) repeats was performed by using a luciferase reporter system. RESULTS: Three different genotypes were identified due to the presence of (TA)6, (TA)7 and (TA)8 repeats. The production of luciferase decreases in inverse relation to the number of repeats. INTERPRETATION AND CONCLUSIONS: The (TA)7 polymorphism, associated with Gilbert syndrome, is the only allele found up to now in white populations, while two other variants (TA)5 and (TA)8 have been identified in black populations. We describe here the first case of a subject affected by Gilbert's syndrome who is heterozygous for the (TA)8 allele in the promoter region of the UGT1A1 gene. This polymorphism, as well as the (TA)7 one, is associated with an increased level of bilirubin and a significant reduction of transcription activity of the UGT1A1 gene.  (+info)

Molecular cloning, expression and characterization of a monkey steroid UDP-glucuronosyltransferase, UGT2B19, that conjugates testosterone. (6/1925)

Although enzymatic processes involved in the formation of active steroids are well known, less information is available about the enzymes responsible for the metabolism of these hormones. Moreover, the expression of these catabolic enzymes, which include UDP-glucuronosyltransferases, may play a role in the regulation of the level and action of steroid hormones in steroid target tissues. Previous studies have shown that the cynomolgus monkey contains high levels of circulating androgen glucuronides, indicating that it represents the best animal model to study the glucuronidation of steroids in extrahepatic tissues. Two cDNA libraries were constructed from monkey liver and prostate mRNA, and a novel UDP-glucuronosyltransferase UGT2B cDNA, UGT2B19, was isolated from both libraries. The UGT2B19 cDNA is 2108 bp in length and contains an open reading frame of 1584 bp encoding a protein of 528 residues. The UGT2B19 cDNA clone was transfected into HK293 cells and a stable cell line expressing UGT2B19 protein was established. The activity of UGT2B19 on 3alpha-hydroxy and 17beta-hydroxy positions of steroids was demonstrated. The enzyme also conjugates xenobiotics including eugenol, 1-naphthol and p-nitrophenol. Kinetic analysis revealed that UGT2B19 glucuronidates steroids with Km values of 1.6, 2.6 and 4.3 microm for testosterone, etiocholanolone and 5beta-androstane-3alpha,17beta-diol, respectively. UGT2B19 transcript was detected, by specific reverse transcriptase-PCR analysis in the liver, ovary, prostate, colon, spleen, kidney, pancreas, brain, cerebellum, mammary gland and epididymis. The molecular characterization of simian UGT2B19 demonstrates relevance of using monkey as an animal model to study and understand steroid glucuronidation in extrahepatic target tissue.  (+info)

Substrate specificity and properties of uridine diphosphate glucuronyltransferase purified to apparent homogeneity from phenobarbital-treated rat liver. (7/1925)

1. The purification to homogeneity of stable highly active preparations of UDP-glucuronyltransferase from liver of phenobarbital-treated rats is briefly described. 2. A single polypeptide was visible after sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, of mol.wt.57000. 3. Antiserum raised against the pure enzyme produces a single sharp precipitin line after Ouchterlony double-diffusion analysis. 4. The pure UDP-glucuronyltransferase isolated from livers of untreated and phenobarbital-pretreated rats appears to be the same enzyme. 5. The Km (UDP-glucuronic acid) of the pure enzyme is 5.4 mM. 6. The activity of the pure enzyme towards 2-aminophenol can still be activated 2-3-fold by diethylnitrosamine. 7. UDP-glucose and UDP-galacturonic acid are not substrates for the purified enzyme. 8. The final preparation catalysed the glucuronidation of 4-nitrophenol, 1-naphthol, 2-aminophenol, morphine and 2-aminobenzoate. 9. Activities towards 4-nitrophenol, 1-naphthol and 2-aminophenol were all copurified. The proposed heterogeneity of UDP-glucuronyltransferase is discussed.  (+info)

Functional heterogeneity of UDP-glucuronosyltransferase as indicated by its differential development and inducibility by glucocorticoids. Demonstration of two groups within the enzyme's activity towards twelve substrates. (8/1925)

1. UDP-glucuronosyltransferase activity towards 12 substrates has been assessed in rat liver during the perinatal period. 2. Between days 16 and 20 of gestation, enzyme activities towards the substrates 2-aminophenol, 2-aminobenzoate, 4-nitrophenol, 1-naphthol, 4-methylumbelliferone and 5-hydroxytryptamine (the 'late foetal' group) surge to reach adult values, while activities towards bilirubin, testosterone, beta-oestradiol, morphine, phenolphthalein, and chloramphenicol (the 'neonatal' group) remain negligible or at less than 10% of adult values. 3. By the second postnatal day, enzyme activities towards the neonatal group have attained, or approached adult values. 4. Dexamethasone precociously stimulates in 17-day foetal liver in utero transferase activities in the late foetal, but not the neonatal group. A similar inductive pattern is found for 15-day foetal liver in organ culture. 5. It is suggested that foetal glucocorticoids, whose synthesis markedly increases between days 16 and 20 of gestation, are responsibile for triggering the simultaneous surge of all the hepatic UDP-glucuronosyltransferase activities in the late foetal group. The neonatal group of activities apparently require a different or additional stimulus for their appearance. 6. The relationship of these two groups of transferase activities to other similar groups observed during induction by xenobiotics and enzyme purification is discussed.  (+info)

Glucuronosyltransferase (UDP-glucuronosyltransferase) is an enzyme belonging to the family of glycosyltransferases. It plays a crucial role in the process of biotransformation and detoxification of various endogenous and exogenous substances, including drugs, hormones, and environmental toxins, in the liver and other organs.

The enzyme functions by transferring a glucuronic acid moiety from a donor molecule, uridine diphosphate glucuronic acid (UDP-GlcUA), to an acceptor molecule, which can be a variety of hydrophobic compounds. This reaction results in the formation of a more water-soluble glucuronide conjugate, facilitating the excretion of the substrate through urine or bile.

There are multiple isoforms of glucuronosyltransferase, classified into two main families: UGT1 and UGT2. These isoforms exhibit different substrate specificities and tissue distributions, allowing for a wide range of compounds to be metabolized through the glucuronidation pathway.

In summary, Glucuronosyltransferase is an essential enzyme in the detoxification process, facilitating the elimination of various substances from the body by conjugating them with a glucuronic acid moiety.

Uridine Diphosphate Glucuronic Acid (UDP-Glucuronic Acid) is not a medical term per se, but rather a biochemical term. It is a compound that plays an essential role in the detoxification process in the liver. UDP-Glucuronic Acid is a nucleotide sugar derivative that combines with toxins, drugs, and other substances to form glucuronides, which are then excreted through urine or bile. This process is known as glucuronidation, and it helps make the substances more water-soluble and easier for the body to eliminate.

Glucuronides are conjugated compounds formed in the liver by the attachment of glucuronic acid to a variety of molecules, including drugs, hormones, and environmental toxins. This process, known as glucuronidation, is catalyzed by enzymes called UDP-glucuronosyltransferases (UGTs) and increases the water solubility of these compounds, allowing them to be more easily excreted from the body through urine or bile.

Glucuronidation plays a crucial role in the detoxification and elimination of many substances, including drugs and toxins. However, in some cases, glucuronides can also be hydrolyzed back into their original forms by enzymes called β-glucuronidases, which can lead to reabsorption of the parent compound and prolong its effects or toxicity.

Overall, understanding the metabolism and disposition of glucuronides is important for predicting drug interactions, pharmacokinetics, and potential adverse effects.

Crigler-Najjar Syndrome is a rare inherited genetic disorder that affects the metabolism of bilirubin, a yellow pigment produced when hemoglobin breaks down. This condition is characterized by high levels of unconjugated bilirubin in the blood, which can lead to jaundice, kernicterus, and neurological damage if left untreated.

There are two types of Crigler-Najjar Syndrome: Type I and Type II.

Type I is the more severe form, and it is caused by a mutation in the UGT1A1 gene, which encodes for an enzyme responsible for conjugating bilirubin. People with this type of Crigler-Najjar Syndrome have little to no functional enzyme activity, leading to very high levels of unconjugated bilirubin in the blood. This form is usually diagnosed in infancy and requires regular phototherapy or a liver transplant to prevent neurological damage.

Type II is a milder form of the disorder, caused by a mutation that results in reduced enzyme activity but not complete loss of function. People with this type of Crigler-Najjar Syndrome usually have milder symptoms and may not require regular phototherapy or a liver transplant, although they may still be at risk for neurological damage if their bilirubin levels become too high.

Both types of Crigler-Najjar Syndrome are inherited in an autosomal recessive manner, meaning that an individual must inherit two copies of the mutated gene (one from each parent) to develop the condition.

Glucuronates are not a medical term per se, but they refer to salts or esters of glucuronic acid, a organic compound that is a derivative of glucose. In the context of medical and biological sciences, glucuronidation is a common detoxification process in which glucuronic acid is conjugated to a wide variety of molecules, including drugs, hormones, and environmental toxins, to make them more water-soluble and facilitate their excretion from the body through urine or bile.

The process of glucuronidation is catalyzed by enzymes called UDP-glucuronosyltransferases (UGTs), which are found in various tissues, including the liver, intestines, and kidneys. The resulting glucuronides can be excreted directly or further metabolized before excretion.

Therefore, "glucuronates" can refer to the chemical compounds that result from this process of conjugation with glucuronic acid, as well as the therapeutic potential of enhancing or inhibiting glucuronidation for various clinical applications.

I'm sorry for any confusion, but "Rats, Gunn" is not a recognized medical term or phrase. It appears to be a nonsensical expression without specific meaning in the context of medicine or healthcare. If you have any questions about medical terminology or concepts, I would be happy to try and help answer those for you!

Gilbert's disease, also known as Gilbert's syndrome, is a common and mild condition characterized by **intermittent** elevations in bilirubin levels in the bloodstream without any evidence of liver damage or disease. Bilirubin is a yellowish pigment that forms when hemoglobin breaks down. Normally, it gets processed in the liver and excreted through bile.

In Gilbert's disease, there is an impaired ability to conjugate bilirubin due to a deficiency or dysfunction of the enzyme UDP-glucuronosyltransferase 1A1 (UGT1A1), which is responsible for the glucuronidation process. This results in mild unconjugated hyperbilirubinemia, where bilirubin levels may rise and cause mild jaundice, particularly during times of fasting, illness, stress, or dehydration.

Gilbert's disease is typically an incidental finding, as it usually does not cause any significant symptoms or complications. It is often discovered during routine blood tests when bilirubin levels are found to be slightly elevated. The condition is usually harmless and does not require specific treatment, but avoiding triggers like fasting or dehydration may help minimize the occurrence of jaundice.

Microsomes, liver refers to a subcellular fraction of liver cells (hepatocytes) that are obtained during tissue homogenization and subsequent centrifugation. These microsomal fractions are rich in membranous structures known as the endoplasmic reticulum (ER), particularly the rough ER. They are involved in various important cellular processes, most notably the metabolism of xenobiotics (foreign substances) including drugs, toxins, and carcinogens.

The liver microsomes contain a variety of enzymes, such as cytochrome P450 monooxygenases, that are crucial for phase I drug metabolism. These enzymes help in the oxidation, reduction, or hydrolysis of xenobiotics, making them more water-soluble and facilitating their excretion from the body. Additionally, liver microsomes also host other enzymes involved in phase II conjugation reactions, where the metabolites from phase I are further modified by adding polar molecules like glucuronic acid, sulfate, or acetyl groups.

In summary, liver microsomes are a subcellular fraction of liver cells that play a significant role in the metabolism and detoxification of xenobiotics, contributing to the overall protection and maintenance of cellular homeostasis within the body.

Bilirubin is a yellowish pigment that is produced by the liver when it breaks down old red blood cells. It is a normal byproduct of hemoglobin metabolism and is usually conjugated (made water-soluble) in the liver before being excreted through the bile into the digestive system. Elevated levels of bilirubin can cause jaundice, a yellowing of the skin and eyes. Increased bilirubin levels may indicate liver disease or other medical conditions such as gallstones or hemolysis. It is also measured to assess liver function and to help diagnose various liver disorders.

Hyperbilirubinemia is a medical condition characterized by an excessively high level of bilirubin in the bloodstream. Bilirubin is a yellowish pigment produced by the liver when it breaks down old red blood cells. Normally, bilirubin is conjugated (made water-soluble) in the liver and then excreted through the bile into the digestive system. However, if there is a problem with the liver's ability to process or excrete bilirubin, it can build up in the blood, leading to hyperbilirubinemia.

Hyperbilirubinemia can be classified as either unconjugated or conjugated, depending on whether the bilirubin is in its direct (conjugated) or indirect (unconjugated) form. Unconjugated hyperbilirubinemia can occur due to increased production of bilirubin (such as in hemolytic anemia), decreased uptake of bilirubin by the liver, or impaired conjugation of bilirubin in the liver. Conjugated hyperbilirubinemia, on the other hand, is usually caused by a problem with the excretion of conjugated bilirubin into the bile, such as in cholestatic liver diseases like hepatitis or cirrhosis.

Symptoms of hyperbilirubinemia can include jaundice (yellowing of the skin and eyes), dark urine, light-colored stools, itching, and fatigue. Treatment depends on the underlying cause of the condition and may involve medications, dietary changes, or surgery.

Uridine diphosphate sugars (UDP-sugars) are nucleotide sugars that play a crucial role in the biosynthesis of glycans, which are complex carbohydrates found on the surface of many cell types. UDP-sugars consist of a uridine diphosphate molecule linked to a sugar moiety, such as glucose, galactose, or xylose. These molecules serve as activated donor substrates for glycosyltransferases, enzymes that catalyze the transfer of sugar residues to acceptor molecules, including proteins and other carbohydrates. UDP-sugars are essential for various biological processes, such as cell recognition, signaling, and protein folding. Dysregulation of UDP-sugar metabolism has been implicated in several diseases, including cancer and congenital disorders of glycosylation.

Isoenzymes, also known as isoforms, are multiple forms of an enzyme that catalyze the same chemical reaction but differ in their amino acid sequence, structure, and/or kinetic properties. They are encoded by different genes or alternative splicing of the same gene. Isoenzymes can be found in various tissues and organs, and they play a crucial role in biological processes such as metabolism, detoxification, and cell signaling. Measurement of isoenzyme levels in body fluids (such as blood) can provide valuable diagnostic information for certain medical conditions, including tissue damage, inflammation, and various diseases.

Biotransformation is the metabolic modification of a chemical compound, typically a xenobiotic (a foreign chemical substance found within an living organism), by a biological system. This process often involves enzymatic conversion of the parent compound to one or more metabolites, which may be more or less active, toxic, or mutagenic than the original substance.

In the context of pharmacology and toxicology, biotransformation is an important aspect of drug metabolism and elimination from the body. The liver is the primary site of biotransformation, but other organs such as the kidneys, lungs, and gastrointestinal tract can also play a role.

Biotransformation can occur in two phases: phase I reactions involve functionalization of the parent compound through oxidation, reduction, or hydrolysis, while phase II reactions involve conjugation of the metabolite with endogenous molecules such as glucuronic acid, sulfate, or acetate to increase its water solubility and facilitate excretion.

The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:

1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.

Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

Camptothecin is a topoisomerase I inhibitor, which is a type of chemotherapeutic agent used in cancer treatment. It works by interfering with the function of an enzyme called topoisomerase I, which helps to uncoil DNA during cell division. By inhibiting this enzyme, camptothecin prevents the cancer cells from dividing and growing, ultimately leading to their death.

Camptothecin is found naturally in the bark and stem of the Camptotheca acuminata tree, also known as the "happy tree," which is native to China. It was first isolated in 1966 and has since been developed into several synthetic derivatives, including irinotecan and topotecan, which are used clinically to treat various types of cancer, such as colon, lung, and ovarian cancers.

Like other chemotherapeutic agents, camptothecin can have significant side effects, including nausea, vomiting, diarrhea, and myelosuppression (suppression of bone marrow function). It is important for patients receiving camptothecin-based therapies to be closely monitored by their healthcare team to manage these side effects effectively.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

High-performance liquid chromatography (HPLC) is a type of chromatography that separates and analyzes compounds based on their interactions with a stationary phase and a mobile phase under high pressure. The mobile phase, which can be a gas or liquid, carries the sample mixture through a column containing the stationary phase.

In HPLC, the mobile phase is a liquid, and it is pumped through the column at high pressures (up to several hundred atmospheres) to achieve faster separation times and better resolution than other types of liquid chromatography. The stationary phase can be a solid or a liquid supported on a solid, and it interacts differently with each component in the sample mixture, causing them to separate as they travel through the column.

HPLC is widely used in analytical chemistry, pharmaceuticals, biotechnology, and other fields to separate, identify, and quantify compounds present in complex mixtures. It can be used to analyze a wide range of substances, including drugs, hormones, vitamins, pigments, flavors, and pollutants. HPLC is also used in the preparation of pure samples for further study or use.

Genetic polymorphism refers to the occurrence of multiple forms (called alleles) of a particular gene within a population. These variations in the DNA sequence do not generally affect the function or survival of the organism, but they can contribute to differences in traits among individuals. Genetic polymorphisms can be caused by single nucleotide changes (SNPs), insertions or deletions of DNA segments, or other types of genetic rearrangements. They are important for understanding genetic diversity and evolution, as well as for identifying genetic factors that may contribute to disease susceptibility in humans.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.

An encyclopedia is a comprehensive reference work containing articles on various topics, usually arranged in alphabetical order. In the context of medicine, a medical encyclopedia is a collection of articles that provide information about a wide range of medical topics, including diseases and conditions, treatments, tests, procedures, and anatomy and physiology. Medical encyclopedias may be published in print or electronic formats and are often used as a starting point for researching medical topics. They can provide reliable and accurate information on medical subjects, making them useful resources for healthcare professionals, students, and patients alike. Some well-known examples of medical encyclopedias include the Merck Manual and the Stedman's Medical Dictionary.

I'm sorry for any confusion, but "Science" is a broad field that refers to a systematic and logical process used to discover how things in the universe work. It's not typically used as a medical term. However, within the context of medicine, "science" often refers to evidence-based practices, which are treatments and preventions that have been scientifically researched and proven to be effective. This could include areas like pharmacology (the study of drugs), pathophysiology (the study of changes in the body due to disease), or clinical trials (studies used to test new treatments). If you're looking for a specific medical term, could you please provide more context?

Insemination, in a medical context, refers to the introduction of semen into the reproductive system of a female for the purpose of achieving pregnancy. This can be done through various methods including intracervical insemination (ICI), intrauterine insemination (IUI), and in vitro fertilization (IVF).

Intracervical insemination involves placing the semen at the cervix, the opening to the uterus. Intrauterine insemination involves placing the sperm directly into the uterus using a catheter. In vitro fertilization is a more complex process where the egg and sperm are combined in a laboratory dish and then transferred to the uterus.

Insemination is often used in cases of infertility, either because of male or female factors, or unexplained infertility. It can also be used for those who wish to become pregnant but do not have a partner, such as single women and same-sex female couples.

Gymnema, also known as Gymnema sylvestre, is a woody climbing shrub native to the tropical forests of India and Africa. In traditional medicine, extracts from the leaves of this plant have been used for centuries to help manage diabetes, primarily by reducing sugar cravings and lowering blood sugar levels.

The active components in Gymnema are believed to be a group of triterpenoid saponins called gymnemic acids. These compounds have been shown to interfere with the ability of the tongue to taste sweetness, which may help reduce the desire for sugary foods and beverages. Additionally, gymnemic acids have been found to slow the absorption of glucose in the intestines, which can help regulate blood sugar levels after meals.

While Gymnema has a long history of use in traditional medicine, more research is needed to fully understand its potential health benefits and risks. It's important to consult with a healthcare provider before starting any new supplement regimen, especially if you have a medical condition like diabetes or are taking prescription medications.

Uridine 5'-diphospho-glucuronosyltransferase (UDP-glucuronosyltransferase, UGT) is a microsomal glycosyltransferase (EC 2.4. ... Glucuronosyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (Articles with ... A deficiency in the bilirubin specific form of glucuronosyltransferase is thought to be the cause of Gilbert's syndrome, which ... "UDP-glucuronosyltransferase 1-1". Drugbank. Retrieved 21 November 2019. Court MH; Greenblatt DJ (2000). "Molecular genetic ...
... (EC 2.4.1.262, UGASGT) is an enzyme with systematic name UDP-D-glucuronate:soyasapogenol ... Soyasapogenol+glucuronosyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ... Kurosawa Y, Takahara H, Shiraiwa M (August 2002). "UDP-glucuronic acid:soyasapogenol glucuronosyltransferase involved in ... 3-O-D-glucuronosyltransferase. This enzyme catalyses the following chemical reaction UDP-glucuronate + soyasapogenol B ⇌ {\ ...
... may refer to: UGT1A3, a human gene UGT1A4, a human gene UGT1A5, a human gene UGT1A6, a human ...
In enzymology, a bilirubin-glucuronoside glucuronosyltransferase (EC 2.4.1.95) is an enzyme that catalyzes the chemical ... The systematic name of this enzyme class is bilirubin-glucuronoside:bilirubin-glucuronoside D-glucuronosyltransferase. Other ... names in common use include bilirubin monoglucuronide transglucuronidase, and bilirubin glucuronoside glucuronosyltransferase. ...
In enzymology, a galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase (EC 2.4.1.135) is an enzyme that catalyzes ... Other names in common use include glucuronosyltransferase I, and uridine diphosphate glucuronic acid:acceptor ... Solubilization and partial purification of uridine diphosphate glucuronic acid: acceptor glucuronosyltransferase from mouse ... 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xyl osyl-protein D-glucuronosyltransferase. ...
... (EC 2.4.1.253, UBGAT) is an enzyme with systematic name UDP-D-glucuronate:5,6,7- ... Baicalein+7-O-glucuronosyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ... trihydroxyflavone 7-O-glucuronosyltransferase . This enzyme catalyses the following chemical reaction UDP-D-glucuronate + ... baicalein 7-O-glucuronosyltransferase from Scutellaria baicalensis Georgi. cell suspension cultures". Phytochemistry. 53 (5): ...
In enzymology, a luteolin 7-O-glucuronosyltransferase (EC 2.4.1.189) is an enzyme that catalyzes the chemical reaction UDP- ... The systematic name of this enzyme class is UDP-glucuronate:luteolin 7-O-glucuronosyltransferase. Other names in common use ... Schulz M, Weissenbock G (1988). "3 specific UDP-glucuronate-flavone-glucuronosyl-transferases from primary leaves of Secale ... include uridine diphosphoglucuronate-luteolin 7-O-glucuronosyltransferase, and LGT. ...
In enzymology, a N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase (EC 2.4.1.226) is an enzyme that catalyzes ... beta-D-glu curonosyl-proteoglycan 3-beta-glucuronosyltransferase. This enzyme is also called chondroitin glucuronyltransferase ...
In enzymology, a N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase (EC 2.4.1.225) is an enzyme that catalyzes ... glucuronosyl-proteoglycan 4-beta-glucuronosyltransferase. Other names in common use include N-acetylglucosaminylproteoglycan ...
UGT-1A is a uridine diphosphate glucuronosyltransferase (UDP-glucuronosyltransferase, UDPGT), an enzyme of the glucuronidation ... UDP-glucuronosyltransferase 1-1 also known as UGT-1A is an enzyme that in humans is encoded by the UGT1A1 gene. ... The UGT1A1 gene is part of a complex locus that encodes several UDP-glucuronosyltransferases. The locus includes thirteen ... Strassburg CP, Manns MP, Tukey RH (April 1998). "Expression of the UDP-glucuronosyltransferase 1A locus in human colon. ...
O-glucuronosyl-transferase, and LDT. Schulz M, Weissenbock G (1988). "3 specific UDP-glucuronate-flavone-glucuronosyl- ... In enzymology, a luteolin-7-O-diglucuronide 4'-O-glucuronosyltransferase (EC 2.4.1.191) is an enzyme that catalyzes the ... The systematic name of this enzyme class is UDP-glucuronate:luteolin-7-O-beta-D-diglucuronide 4'-O-glucuronosyltransferase. ... Other names in common use include uridine diphosphoglucuronate-luteolin 7-O-diglucuronide, glucuronosyltransferase, UDP- ...
O-beta-glucuronosyltransferase, BpUGAT, UDP-D-glucuronate:cyanidin-3-O-beta-glucoside 2-O-beta-glucuronosyltransferase) is an ... Cyanidin-3-O-glucoside+2-O-glucuronosyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) ... Enzymology and phylogenetics of a novel glucuronosyltransferase involved in flower pigment biosynthesis". The Journal of ... Cyanidin-3-O-glucoside 2-O-glucuronosyltransferase (EC 2.4.1.254, BpUGT94B1, UDP-glucuronic acid:anthocyanin ...
In enzymology, a luteolin-7-O-glucuronide 2"-O-glucuronosyltransferase (EC 2.4.1.190) is an enzyme that catalyzes the chemical ... The systematic name of this enzyme class is UDP-glucuronate:luteolin-7-O-beta-D-glucuronide 2''-O-glucuronosyltransferase. ... Schulz M; Weissenbock G (1988). "3 specific UDP-glucuronate-flavone-glucuronosyl-transferases from primary leaves of Secale ... Other names in common use include uridine diphosphoglucuronate-luteolin 7-O-glucuronide, glucuronosyltransferase, LMT, and UDP- ...
Crawford, JM; Ransil, BJ; Narciso, JP; Gollan, JL (1992-08-25). "Hepatic microsomal bilirubin UDP-glucuronosyltransferase. The ... "Genetic lesions of bilirubin uridine-diphosphoglucuronate glucuronosyltransferase (UGT1A1) causing Crigler-Najjar and Gilbert ...
O-Acetylation reactions are catalyzed by NAT, N-acetyltransferase; and UDP-glucuronosyltransferase (UGT) enzymes. Two different ...
King CD, Rios GR, Green MD, Tephly TR (September 2000). "UDP-glucuronosyltransferases". Current Drug Metabolism. 1 (2): 143-61 ... In humans, these include cytochrome P450 oxidases, UDP-glucuronosyltransferases, and glutathione S-transferases. This system of ...
The reaction is catalyzed by the enzyme UDP-glucuronosyltransferase. This form of bilirubin is excreted from the liver in bile ... King, C.; Rios, G.; Green, M.; Tephly, T. (2000). "UDP-Glucuronosyltransferases". Current Drug Metabolism. 1 (2): 143-161. doi: ...
UDP-glucuronosyltransferase 1-5 is an enzyme that in humans is encoded by the UGT1A5 gene. This gene encodes a UDP- ... "Entrez Gene: UDP glucuronosyltransferase 1 family". Ritter JK, Chen F, Sheen YY, Tran HM, Kimura S, Yeatman MT, Owens IS ( ... This gene is part of a complex locus that encodes several UDP-glucuronosyltransferases. The locus includes thirteen unique ... King CD, Rios GR, Green MD, Tephly TR (2000). "UDP-glucuronosyltransferases". Curr. Drug Metab. 1 (2): 143-61. doi:10.2174/ ...
UDP-glucuronosyltransferase 1-6 is an enzyme that in humans is encoded by the UGT1A6 gene. UDP-glucuronosyltransferase 1-6 is a ... This gene is part of a complex locus that encodes several UDP-glucuronosyltransferases. The locus includes thirteen unique ... Ritter JK, Crawford JM, Owens IS (January 1991). "Cloning of two human liver bilirubin UDP-glucuronosyltransferase cDNAs with ... "Entrez Gene: UGT1A6 UDP glucuronosyltransferase 1 family, polypeptide A6". Shrestha B, Reed JM, Starks PT, Kaufman GE, ...
King C, Rios G, Green M, Tephly T (2000). "UDP-glucuronosyltransferases". Curr Drug Metab. 1 (2): 143-61. doi:10.2174/ ... Enzymes that are important in detoxification metabolism include cytochrome P450 oxidases, UDP-glucuronosyltransferases, and ...
UDP-glucuronosyltransferase 1-9 is an enzyme that in humans is encoded by the UGT1A9 gene. This gene encodes a UDP- ... This gene is part of a complex locus that encodes several UDP-glucuronosyltransferases. The locus includes thirteen unique ... King CD, Rios GR, Green MD, Tephly TR (2000). "UDP-glucuronosyltransferases". Curr. Drug Metab. 1 (2): 143-61. doi:10.2174/ ... 2009). "In silico and in vitro approaches to elucidate the thermal stability of human UDP-glucuronosyltransferase (UGT) 1A9". ...
UDP-glucuronosyltransferase 1-4 is an enzyme that in humans is encoded by the UGT1A4 gene. This gene encodes a UDP- ... This gene is part of a complex locus that encodes several UDP-glucuronosyltransferases. The locus includes thirteen unique ... King CD, Rios GR, Green MD, Tephly TR (2001). "UDP-glucuronosyltransferases". Curr. Drug Metab. 1 (2): 143-61. doi:10.2174/ ... 1994). "Identification of defect in the genes for bilirubin UDP-glucuronosyl-transferase in a patient with Crigler-Najjar ...
UDP glucuronosyltransferase 1 family, polypeptide A7 is a protein that in humans is encoded by the UGT1A7 gene. This gene ... "Entrez Gene: UDP glucuronosyltransferase 1 family, polypeptide A7". Retrieved 2012-01-27. Tukey RH, Strassburg CP (2000). " ... Strassburg CP, Vogel A, Kneip S, Tukey RH, Manns MP (June 2002). "Polymorphisms of the human UDP-glucuronosyltransferase (UGT) ... This gene is part of a complex locus that encodes several UDP-glucuronosyltransferases. The locus includes thirteen unique ...
Bock K, Köhle C (2005). "UDP-glucuronosyltransferase 1A6: structural, functional, and regulatory aspects". Methods Enzymol. ... "UDP-glucuronosyltransferases". Curr. Drug Metab. 1 (2): 143-61. doi:10.2174/1389200003339171. PMID 11465080. Al-Zoughool M., ... "Determination of mRNA Expression of Human UDP-Glucuronosyltransferases and Application for Localization in Various Human ... acid component of uridine diphosphate glucuronic acid to a substrate by any of several types of UDP-glucuronosyltransferase. ...
UDP glucuronosyltransferase 1 family, polypeptide A cluster (UGT1A) is a human gene locus which includes several UDP ... 2005). "UDP-glucuronosyltransferases 1A expression in human urinary bladder and colon cancer by immunohistochemistry". Oncol. ... "Entrez Gene: UGT1A@ UDP glucuronosyltransferase 1 family, polypeptide A cluster". Mackenzie PI, Owens IS, Burchell B, et al. ( ... King CD, Rios GR, Green MD, Tephly TR (2001). "UDP-glucuronosyltransferases". Curr. Drug Metab. 1 (2): 143-61. doi:10.2174/ ...
Dilokpimol, Adiphol; Geshi, Naomi (2014-06-01). "Arabidopsis thaliana glucuronosyltransferase in family GT14". Plant Signaling ... "A β-glucuronosyltransferase from Arabidopsis thaliana involved in biosynthesis of type II arabinogalactan has a role in cell ... β-glucuronosyltransferases, α-rhamnosyltransferases, and α- fucosyltransferases are responsible for the synthesis of these ...
UDP-glucuronosyltransferase 2B10 is an enzyme that in humans is encoded by the UGT2B10 gene. It is responsible for ... "Entrez Gene: UGT2B10 UDP glucuronosyltransferase 2 family, polypeptide B10". Chen G, Giambrone NE, Dluzen DF, Muscat JE, Berg A ... "cDNA cloning and expression of two new members of the human liver UDP-glucuronosyltransferase 2B subfamily". Biochemical and ... "Regulation and function of family 1 and family 2 UDP-glucuronosyltransferase genes (UGT1A, UGT2B) in human oesophagus". The ...
UDP glucuronosyltransferase 2 family, polypeptide A2, also known as UGT2A2, is an enzyme that in humans is encoded by the ... "Entrez Gene: UDP glucuronosyltransferase 2 family, polypeptide A2". Mackenzie PI, Bock KW, Burchell B, Guillemette C, Ikushiro ...
Bock K, Köhle C (2005). "UDP-glucuronosyltransferase 1A6: structural, functional, and regulatory aspects". Methods Enzymol. ... "Determination of mRNA Expression of Human UDP-Glucuronosyltransferases and Application for Localization in Various Human ...
In humans, UDP-Glucuronosyltransferase-2B7 is encoded by the UGT2B7 gene. The UGTs serve a major role in the conjugation and ... UGT2B7 (UDP-Glucuronosyltransferase-2B7) is a phase II metabolism isoenzyme found to be active in the liver, kidneys, ... Yuan L, Qian S, Xiao Y, Sun H, Zeng S (May 2015). "Homo- and hetero-dimerization of human UDP-glucuronosyltransferase 2B7 ( ... Hwang MS, Lee SJ, Jeong HE, Lee S, Yoo MA, Shin JG (2010). "Genetic variations in UDP-glucuronosyltransferase 2B7 gene (UGT2B7 ...
  • UDP-glucuronosyltransferases (UGTs), expressed in various tissues including liver and intestine, catalyze phase II metabolic biotransformation. (aspetjournals.org)
  • Human UDP-glucuronosyltransferases (UGTs) are important enzymes in metabolic elimination of endo- and xenobiotics. (nih.gov)
  • UDP-Glucuronosyltransferases (UGTs) are important in the elimination of most xenobiotics, including 5-( p -hydroxyphenyl)-5-phenylhydantoin (HPPH), the major, reputedly nontoxic, metabolite of the anticonvulsant drug phenytoin. (aspetjournals.org)
  • Revisiting the Latency of Uridine Diphosphate-Glucuronosyltransferases (UGTs)-How Does the Endoplasmic Reticulum Membrane Influence Their Function? (mdpi.com)
  • Uridine diphosphate-glucuronosyltransferases (UGTs) are phase 2 conjugation enzymes mainly located in the endoplasmic reticulum (ER) of the liver and many other tissues, and can be recovered in artificial ER membrane preparations (microsomes). (mdpi.com)
  • UDP-Glucuronosyltransferases (UGTs) are classified into three subfamilies in mice: Ugt1a, 2b, and 2a. (elsevierpure.com)
  • To identify the association between gastrointestinal carcinomas (GIC) risk and UDP-glucuronosyltransferases (UGTs) 1A7 polymorphisms through a systematic review and network meta-analysis. (oncotarget.com)
  • However, there haven't been systematic study about the inhibition of tucatinib on UDP-Glucuronosyltransferases (UGTs) and the potential risk of drug-drug interactions (DDIs). (bvsalud.org)
  • Uridine 5'-diphosphate glucuronosyltransferases are phase II detoxifying enzymes capable of tobacco-borne toxicant inactivation and cellular protection. (nih.gov)
  • Data relating to the inhibition of UDP-glucuronosyltransferase (UGT) enzymes by KIs is sparse. (edu.au)
  • UDP-glucuronosyltransferases are a family of drug metabolizing enzymes contributing to hepatic drug metabolism and protection against environmental toxins. (wikigenes.org)
  • Several in vitro studies were conducted in incubations of [14C]GDC-0810, synthetic M6 and M4 with liver microsomes, intestinal microsomes, and hepatocytes of different species as well as recombinant UDP-glucuronosyltransferase (UGT) enzymes to further understand the formation of M2. (bvsalud.org)
  • A deficiency in the bilirubin specific form of glucuronosyltransferase is thought to be the cause of Gilbert's syndrome, which is characterized by unconjugated hyperbilirubinemia. (wikipedia.org)
  • SYN: UDPglucuronate-bilirubin glucuronosyltransferase. (theodora.com)
  • Yamamoto A, Nishio H, Waku S, Yokoyama N, Yonetani M, Uetani Y. Gly71Arg mutation of the bilirubin UDP-glucuronosyltransferase 1A1 gene is associated with neonatal hyperbilirubinemia in the Japanese population. (medscape.com)
  • Bilirubin metabolism and UDP-glucuronosyltransferase 1A1 variants in Asians: Pathogenic implications and therapeutic response. (cdc.gov)
  • Uridine 5'-diphospho-glucuronosyltransferase (UDP-glucuronosyltransferase, UGT) is a microsomal glycosyltransferase (EC 2.4.1.17) that catalyzes the transfer of the glucuronic acid component of UDP-glucuronic acid to a small hydrophobic molecule. (wikipedia.org)
  • Bioavailability of testosterone enanthate dependent on genetic variation in the phosphodiesterase 7B but not on the uridine 5'-diphospho-glucuronosyltransferase (UGT2B17) gene. (bioseek.eu)
  • To study the disposition of serum testosterone and seven of its metabolites before and after 2 days of an intramuscular dose (500 mg) of testosterone enanthate in relation to the phosphodiesterase (PDE7B) and the uridine 5'-diphospho-glucuronosyltransferase (UGT2B17) genotypes. (bioseek.eu)
  • Alternative names: glucuronyltransferase UDP-glucuronyl transferase UDP-GT Glucuronosyltransferases are responsible for the process of glucuronidation, a major part of phase II metabolism. (wikipedia.org)
  • The procedure has been used to characterize paracetamol glucuronidation kinetics in human liver microsomes and to assess the substrate specificity of the paracetamol UDP-glucuronosyltransferase (UDPGT) activity. (edu.au)
  • Tetrahydrocannabinol (Δ 9 -THC), the primary psychoactive ingredient in marijuana, is subject to cytochrome P450 oxidation and subsequent UDP-glucuronosyltransferase (UGT)-dependent glucuronidation. (thecannabisadvisory.com)
  • Rat androsterone UDP-glucuronosyltransferase gene (UGT2B2) was regionally assigned to chromosome band 14p21.2-p22 by fluorescence in situ hybridization using a biotinylated cDNA (1,8-kb insert) probe. (elsevierpure.com)
  • This gene is part of a complex locus that encodes several UDP-glucuronosyltransferases. (nih.gov)
  • The aim of this work was to determine if a non-mammalian species had multiple UDP-glucuronosyltransferase (UDPGT) isoforms. (hud.ac.uk)
  • Role of extrahepatic UDP-glucuronosyltransferase 1A1: Advances in understanding breast milk-induced neonatal hyperbilirubinemia. (medscape.com)
  • The present study investigated whether BCP N-glucuronide (BCP-NG, the primary metabolite of BCP) was produced in mammalian species other than rats, and attempted to identify the UDP-glucuronosyltransferase (UGT) isoform (s) responsible for formation of BCP-NG in humans. (scirp.org)
  • We find that natural variation in the putative glucuronosyltransferase GLCT-3, a homolog of human B3GAT, partly explains differences in propionate sensitivity in one of these genomic intervals. (umassmed.edu)
  • 2019. Formation of (2)- and (2)-8-Prenylnaringenin Glucuronides by Human UDP-Glucuronosyltransferases. . (oregonstate.edu)
  • UDP-glucuronosyltransferase 1-9 is an enzyme that in humans is encoded by the UGT1A9 gene . (wikipedia.org)
  • The study was designed to investigate the substrate specifities of the isofunctional Phase II enzyme UDP-glucuronosyltransferase (UDPGT) and to determine possible differences in the regulation. (europa.eu)
  • The activity of the phase II enzyme UDP-glucuronosyltransferase towards linalool was enhanced by induction with phenobarbital in microsomes of both Wistar rats and guinea pigs. (europa.eu)
  • In this study, the substrate specifities of the isofunctional Phase II enzyme UDP-glucuronosyltransferase (UDPGT) and possible differences in the regulation were investigated. (europa.eu)
  • PCBs may in turn affect TH levels by inducing the microsomal enzyme uridinediphosphate glucuronosyltransferase (UDP-GT), which is involved in TH elimination. (cdc.gov)
  • The UGT1A1 gene belongs to a family of genes that provide instructions for making enzymes called UDP-glucuronosyltransferases. (medlineplus.gov)
  • 16. Polymorphisms of UDP-glucuronosyltransferase and pharmacokinetics of irinotecan. (nih.gov)
  • The cDNA encoding the UDP glucuronosyltransferase, UGT1A3, has been cloned and expressed in cell culture. (nih.gov)
  • Developmental increases in rat hepatic microsomal UDP-glucuronosyltransferase activities toward xenoestrogens and decreases during pregnancy. (nih.gov)
  • Orthologous to human UGT1A3 (UDP glucuronosyltransferase family 1 member A3). (nih.gov)
  • 2019. Formation of (2)- and (2)-8-Prenylnaringenin Glucuronides by Human UDP-Glucuronosyltransferases. . (oregonstate.edu)
  • Ontogenic isoform switching of UDP-glucuronosyltransferase family 1 in rat liver. (nih.gov)
  • Data suggest that activation of UDP-glucuronosyltransferase 1A2 (UGT1A2) by nuclear factor I (NFI)-A1 is suppressed by NFI-C1 in the liver, and culture-associated expression of UGT1A2 is triggered by disappearance of NFI-C1 in cultured hepatocytes. (nih.gov)
  • Transcriptional enhancement of UDP-glucuronosyltransferase form 1A2 (UGT1A2) by nuclear factor I-A (NFI-A) in rat hepatocytes. (nih.gov)

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