Glucosidases: Enzymes that hydrolyze O-glucosyl-compounds. (Enzyme Nomenclature, 1992) EC 3.2.1.-.Oligo-1,6-Glucosidase: An enzyme that catalyzes the endohydrolysis of 1,6-alpha-glucosidic linkages in isomaltose and dextrins produced from starch and glycogen by ALPHA-AMYLASES. EC 3.2.1.10.alpha-Glucosidases: Enzymes that catalyze the exohydrolysis of 1,4-alpha-glucosidic linkages with release of alpha-glucose. Deficiency of alpha-1,4-glucosidase may cause GLYCOGEN STORAGE DISEASE TYPE II.Indolizines1-Deoxynojirimycin: An alpha-glucosidase inhibitor with antiviral action. Derivatives of deoxynojirimycin may have anti-HIV activity.Polyisoprenyl Phosphate Oligosaccharides: These compounds function as activated glycosyl carriers in the biosynthesis of glycoproteins and glycophospholipids. Include the pyrophosphates.Oligosaccharides: Carbohydrates consisting of between two (DISACCHARIDES) and ten MONOSACCHARIDES connected by either an alpha- or beta-glycosidic link. They are found throughout nature in both the free and bound form.GlucosidesSwainsonine: An indolizidine alkaloid from the plant Swainsona canescens that is a potent alpha-mannosidase inhibitor. Swainsonine also exhibits antimetastatic, antiproliferative, and immunomodulatory activity.beta-Glucosidase: An exocellulase with specificity for a variety of beta-D-glycoside substrates. It catalyzes the hydrolysis of terminal non-reducing residues in beta-D-glucosides with release of GLUCOSE.Calnexin: A lectin found in ENDOPLASMIC RETICULUM membranes that binds to specific N-linked OLIGOSACCHARIDES found on newly synthesized proteins. It may play role in PROTEIN FOLDING or retention and degradation of misfolded proteins in the endoplasmic reticulum.GlucosamineAlkaloids: Organic nitrogenous bases. Many alkaloids of medical importance occur in the animal and vegetable kingdoms, and some have been synthesized. (Grant & Hackh's Chemical Dictionary, 5th ed)Glycoside HydrolasesGlycoproteins: Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Endoplasmic Reticulum: A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed)Glycosylation: The chemical or biochemical addition of carbohydrate or glycosyl groups to other chemicals, especially peptides or proteins. Glycosyl transferases are used in this biochemical reaction.alpha 1-Antitrypsin: Plasma glycoprotein member of the serpin superfamily which inhibits TRYPSIN; NEUTROPHIL ELASTASE; and other PROTEOLYTIC ENZYMES.Molecular Sequence Data: 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.Chromatography, Gel: Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.Kinetics: The rate dynamics in chemical or physical systems.Receptors, Adrenergic, alpha: One of the two major pharmacological subdivisions of adrenergic receptors that were originally defined by the relative potencies of various adrenergic compounds. The alpha receptors were initially described as excitatory receptors that post-junctionally stimulate SMOOTH MUSCLE contraction. However, further analysis has revealed a more complex picture involving several alpha receptor subtypes and their involvement in feedback regulation.Hypoxia-Inducible Factor 1, alpha Subunit: Hypoxia-inducible factor 1, alpha subunit is a basic helix-loop-helix transcription factor that is regulated by OXYGEN availability and is targeted for degradation by VHL TUMOR SUPPRESSOR PROTEIN.alpha7 Nicotinic Acetylcholine Receptor: A member of the NICOTINIC ACETYLCHOLINE RECEPTOR subfamily of the LIGAND-GATED ION CHANNEL family. It consists entirely of pentameric a7 subunits expressed in the CNS, autonomic nervous system, vascular system, lymphocytes and spleen.Integrin alpha3beta1: Cell surface receptor for LAMININ, epiligrin, FIBRONECTINS, entactin, and COLLAGEN. Integrin alpha3beta1 is the major integrin present in EPITHELIAL CELLS, where it plays a role in the assembly of BASEMENT MEMBRANE as well as in cell migration, and may regulate the functions of other integrins. Two alternatively spliced isoforms of the alpha subunit (INTEGRIN ALPHA3), are differentially expressed in different cell types.Integrin alpha4: An integrin alpha subunit that is unique in that it does not contain an I domain, and its proteolytic cleavage site is near the middle of the extracellular portion of the polypeptide rather than close to the membrane as in other integrin alpha subunits.Integrin alpha6: An integrin alpha subunit that primarily associates with INTEGRIN BETA1 or INTEGRIN BETA4 to form laminin-binding heterodimers. Integrin alpha6 has two alternatively spliced isoforms: integrin alpha6A and integrin alpha6B, which differ in their cytoplasmic domains and are regulated in a tissue-specific and developmental stage-specific manner.Integrin alpha5beta1: An integrin found in FIBROBLASTS; PLATELETS; MONOCYTES, and LYMPHOCYTES. Integrin alpha5beta1 is the classical receptor for FIBRONECTIN, but it also functions as a receptor for LAMININ and several other EXTRACELLULAR MATRIX PROTEINS.Integrin alpha4beta1: Integrin alpha4beta1 is a FIBRONECTIN and VCAM-1 receptor present on LYMPHOCYTES; MONOCYTES; EOSINOPHILS; NK CELLS and thymocytes. It is involved in both cell-cell and cell- EXTRACELLULAR MATRIX adhesion and plays a role in INFLAMMATION, hematopoietic cell homing and immune function, and has been implicated in skeletal MYOGENESIS; NEURAL CREST migration and proliferation, lymphocyte maturation and morphogenesis of the PLACENTA and HEART.Interleukin-1alpha: An interleukin-1 subtype that occurs as a membrane-bound pro-protein form that is cleaved by proteases to form a secreted mature form. Unlike INTERLEUKIN-1BETA both membrane-bound and secreted forms of interleukin-1alpha are biologically active.Integrin alpha2beta1: An integrin found on fibroblasts, platelets, endothelial and epithelial cells, and lymphocytes where it functions as a receptor for COLLAGEN and LAMININ. Although originally referred to as the collagen receptor, it is one of several receptors for collagen. Ligand binding to integrin alpha2beta1 triggers a cascade of intracellular signaling, including activation of p38 MAP kinase.Receptors, Adrenergic, alpha-1: A subclass of alpha-adrenergic receptors that mediate contraction of SMOOTH MUSCLE in a variety of tissues such as ARTERIOLES; VEINS; and the UTERUS. They are usually found on postsynaptic membranes and signal through GQ-G11 G-PROTEINS.Integrin alpha5: This integrin alpha subunit combines with INTEGRIN BETA1 to form a receptor (INTEGRIN ALPHA5BETA1) that binds FIBRONECTIN and LAMININ. It undergoes posttranslational cleavage into a heavy and a light chain that are connected by disulfide bonds.Integrin alpha1beta1: Integrin alpha1beta1 functions as a receptor for LAMININ and COLLAGEN. It is widely expressed during development, but in the adult is the predominant laminin receptor (RECEPTORS, LAMININ) in mature SMOOTH MUSCLE CELLS, where it is important for maintenance of the differentiated phenotype of these cells. Integrin alpha1beta1 is also found in LYMPHOCYTES and microvascular endothelial cells, and may play a role in angiogenesis. In SCHWANN CELLS and neural crest cells, it is involved in cell migration. Integrin alpha1beta1 is also known as VLA-1 and CD49a-CD29.Receptors, Adrenergic, alpha-2: A subclass of alpha-adrenergic receptors found on both presynaptic and postsynaptic membranes where they signal through Gi-Go G-PROTEINS. While postsynaptic alpha-2 receptors play a traditional role in mediating the effects of ADRENERGIC AGONISTS, the subset of alpha-2 receptors found on presynaptic membranes signal the feedback inhibition of NEUROTRANSMITTER release.Integrin alpha6beta1: A cell surface receptor mediating cell adhesion to the EXTRACELLULAR MATRIX and to other cells via binding to LAMININ. It is involved in cell migration, embryonic development, leukocyte activation and tumor cell invasiveness. Integrin alpha6beta1 is the major laminin receptor on PLATELETS; LEUKOCYTES; and many EPITHELIAL CELLS, and ligand binding may activate a number of signal transduction pathways. Alternative splicing of the cytoplasmic domain of the alpha6 subunit (INTEGRIN ALPHA6) results in the formation of A and B isoforms of the heterodimer, which are expressed in a tissue-specific manner.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Integrin alpha6beta4: This intrgrin is a key component of HEMIDESMOSOMES and is required for their formation and maintenance in epithelial cells. Integrin alpha6beta4 is also found on thymocytes, fibroblasts, and Schwann cells, where it functions as a laminin receptor (RECEPTORS, LAMININ) and is involved in wound healing, cell migration, and tumor invasiveness.Integrin alpha Chains: The alpha subunits of integrin heterodimers (INTEGRINS), which mediate ligand specificity. There are approximately 18 different alpha chains, exhibiting great sequence diversity; several chains are also spliced into alternative isoforms. They possess a long extracellular portion (1200 amino acids) containing a MIDAS (metal ion-dependent adhesion site) motif, and seven 60-amino acid tandem repeats, the last 4 of which form EF HAND MOTIFS. The intracellular portion is short with the exception of INTEGRIN ALPHA4.Integrins: A family of transmembrane glycoproteins (MEMBRANE GLYCOPROTEINS) consisting of noncovalent heterodimers. They interact with a wide variety of ligands including EXTRACELLULAR MATRIX PROTEINS; COMPLEMENT, and other cells, while their intracellular domains interact with the CYTOSKELETON. The integrins consist of at least three identified families: the cytoadhesin receptors(RECEPTORS, CYTOADHESIN), the leukocyte adhesion receptors (RECEPTORS, LEUKOCYTE ADHESION), and the VERY LATE ANTIGEN RECEPTORS. Each family contains a common beta-subunit (INTEGRIN BETA CHAINS) combined with one or more distinct alpha-subunits (INTEGRIN ALPHA CHAINS). These receptors participate in cell-matrix and cell-cell adhesion in many physiologically important processes, including embryological development; HEMOSTASIS; THROMBOSIS; WOUND HEALING; immune and nonimmune defense mechanisms; and oncogenic transformation.Integrin alpha1: An integrin alpha subunit that binds COLLAGEN and LAMININ though its I domain. It combines with INTEGRIN BETA1 to form the heterodimer INTEGRIN ALPHA1BETA1.Alpha Rhythm: Brain waves characterized by a relatively high voltage or amplitude and a frequency of 8-13 Hz. They constitute the majority of waves recorded by EEG registering the activity of the parietal and occipital lobes when the individual is awake, but relaxed with the eyes closed.Integrin alpha3: An integrin alpha subunit that occurs as alternatively spliced isoforms. The isoforms are differentially expressed in specific cell types and at specific developmental stages. Integrin alpha3 combines with INTEGRIN BETA1 to form INTEGRIN ALPHA3BETA1 which is a heterodimer found primarily in epithelial cells.alpha 1-Antitrypsin Deficiency: Deficiency of the protease inhibitor ALPHA 1-ANTITRYPSIN that manifests primarily as PULMONARY EMPHYSEMA and LIVER CIRRHOSIS.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Receptors, Nicotinic: One of the two major classes of cholinergic receptors. Nicotinic receptors were originally distinguished by their preference for NICOTINE over MUSCARINE. They are generally divided into muscle-type and neuronal-type (previously ganglionic) based on pharmacology, and subunit composition of the receptors.Adrenergic alpha-Agonists: Drugs that selectively bind to and activate alpha adrenergic receptors.PPAR alpha: A nuclear transcription factor. Heterodimerization with RETINOID X RECEPTOR GAMMA is important to metabolism of LIPIDS. It is the target of FIBRATES to control HYPERLIPIDEMIAS.Dinoprost: A naturally occurring prostaglandin that has oxytocic, luteolytic, and abortifacient activities. Due to its vasocontractile properties, the compound has a variety of other biological actions.Adrenergic alpha-Antagonists: Drugs that bind to but do not activate alpha-adrenergic receptors thereby blocking the actions of endogenous or exogenous adrenergic agonists. Adrenergic alpha-antagonists are used in the treatment of hypertension, vasospasm, peripheral vascular disease, shock, and pheochromocytoma.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Hepatocyte Nuclear Factor 1-alpha: Hepatocyte nuclear factor 1-alpha is a transcription factor found in the LIVER; PANCREAS; and KIDNEY that regulates HOMEOSTASIS of GLUCOSE.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Transfection: The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.

Alternative splicing of transcripts encoding the alpha- and beta-subunits of mouse glucosidase II in T lymphocytes. (1/973)

Glucosidase II is a processing enzyme of the endoplasmic reticulum that functions to hydrolyze two glucose residues in immature N -linked oligosaccharides attached to newly synthesized polypeptides. We previously reported the cDNA cloning of the alpha- and beta-subunits of mouse glucosidase II from T cells following copurification of these proteins with the highly glycosylated transmembrane protein-tyrosine phosphatase CD45. Subsequent examination of additional cDNA clones, coupled with partial genomic DNA sequencing, has revealed that both subunits are encoded by gene products that undergo alternative splicing in T lymphocytes. The catalytic alpha-subunit possesses two variably expressed segments, box Alpha1, consisting of 22 amino acids located proximal to the amino-terminus, and box Alpha2, composed of 9 amino acids situated between the amino-terminus and the putative catalytic site in the central region of the molecule. Box Beta1, a variably expressed 7 amino acid segment in the beta-subunit of glucosidase II, is located immediately downstream of an acidic stretch near the carboxyl-terminus. Screening of reverse transcribed RNA by polymerase chain reaction confirms the variable inclusion of each of these segments in transcripts obtained from a panel of T-lymphocyte cell lines. Thus, distinct isoforms of glucosidase II exist that may perform specialized functions.  (+info)

The AcbC protein from Actinoplanes species is a C7-cyclitol synthase related to 3-dehydroquinate synthases and is involved in the biosynthesis of the alpha-glucosidase inhibitor acarbose. (2/973)

The putative biosynthetic gene cluster for the alpha-glucosidase inhibitor acarbose was identified in the producer Actinoplanes sp. 50/110 by cloning a DNA segment containing the conserved gene for dTDP-D-glucose 4,6-dehydratase, acbB. The two flanking genes were acbA (dTDP-D-glucose synthase) and acbC, encoding a protein with significant similarity to 3-dehydroquinate synthases (AroB proteins). The acbC gene was overexpressed heterologously in Streptomyces lividans 66, and the product was shown to be a C7-cyclitol synthase using sedo-heptulose 7-phosphate, but not ido-heptulose 7-phosphate, as its substrate. The cyclization product, 2-epi-5-epi-valiolone ((2S,3S,4S,5R)-5-(hydroxymethyl)cyclohexanon-2,3,4,5-tetrol), is a precursor of the valienamine moiety of acarbose. A possible five-step reaction mechanism is proposed for the cyclization reaction catalyzed by AcbC based on the recent analysis of the three-dimensional structure of a eukaryotic 3-dehydroquinate synthase domain (Carpenter, E. P., Hawkins, A. R., Frost, J. W., and Brown, K. A. (1998) Nature 394, 299-302).  (+info)

Trypanosoma cruzi calreticulin is a lectin that binds monoglucosylated oligosaccharides but not protein moieties of glycoproteins. (3/973)

Trypanosoma cruzi is a protozoan parasite that belongs to an early branch in evolution. Although it lacks several features of the pathway of protein N-glycosylation and oligosaccharide processing present in the endoplasmic reticulum of higher eukaryotes, it displays UDP-Glc:glycoprotein glucosyltransferase and glucosidase II activities. It is herewith reported that this protozoan also expresses a calreticulin-like molecule, the third component of the quality control of glycoprotein folding. No calnexin-encoding gene was detected. Recombinant T. cruzi calreticulin specifically recognized free monoglucosylated high-mannose-type oligosaccharides. Addition of anti-calreticulin serum to extracts obtained from cells pulse-chased with [35S]Met plus [35S]Cys immunoprecipitated two proteins that were identified as calreticulin and the lysosomal proteinase cruzipain (a major soluble glycoprotein). The latter but not the former protein disappeared from immunoprecipitates upon chasing cells. Contrary to what happens in mammalian cells, addition of the glucosidase II inhibitor 1-deoxynojirimycin promoted calreticulin-cruzipain interaction. This result is consistent with the known pathway of protein N-glycosylation and oligosaccharide processing occurring in T. cruzi. A treatment of the calreticulin-cruzipain complexes with endo-beta-N-acetylglucosaminidase H either before or after addition of anti-calreticulin serum completely disrupted calreticulin-cruzipain interaction. In addition, mature monoglucosylated but not unglucosylated cruzipain isolated from lysosomes was found to interact with recombinant calreticulin. It was concluded that the quality control of glycoprotein folding appeared early in evolution, and that T. cruzi calreticulin binds monoglucosylated oligosaccharides but not the protein moiety of cruzipain. Furthermore, evidence is presented indicating that glucosyltransferase glucosylated cruzipain at its last folding stages.  (+info)

Murine acid alpha-glucosidase: cell-specific mRNA differential expression during development and maturation. (4/973)

Acid alpha-glucosidase (GAA) cleaves the alpha1-4 and alpha1-6 glycosidic linkages of glycogen and related alpha-glucosyl substrates within lysosomes. Its deficiency results in glycogen storage disease type II (GSDII) variants including Pompe disease. To gain insight into the tissue patterns of involvement by glycogen storage in GSDII, GAA mRNA expression in mouse tissues was evaluated by Northern blot and in situ hybridization analyses. Extensive temporal and spatial variation of GAA mRNA was observed. During preterm maturation, GAA mRNA levels of whole mice progressively increased as assessed by Northern analysis. By in situ hybridization with GAA antisense mRNA, low signals were detected in most tissues throughout gestation. However, increased expression in specific cell types of different tissues was observed beginning at 16 days post coitum in developing brain neurons, primitive inner ear cells, and seminiferous tubular epithelium. In adult mice, whole-organ GAA mRNA levels were highest in brain, moderate in heart, liver, and skeletal muscle, and lowest in the series kidney > lung > testis > spleen. By in situ hybridization, the highest-intensity signals were in neurons of the central and peripheral nervous systems whereas neuroglial cells had only low-level signal. Signals of moderate intensity were in cardiomyocytes whereas low signals were in hepatocytes and skeletal muscle myocytes and very low in cells of the lungs, thymus, pancreas, spleen, and adrenal glands. However, testicular Sertoli cells and kidney tubular epithelial cells had significant signals even though surrounding cells had very low signals. The discrete temporal and spatial variations of GAA mRNA during development indicate different physiological roles for this enzyme in various cell types and developmental stages.  (+info)

Delayed symptom onset and increased life expectancy in Sandhoff disease mice treated with N-butyldeoxynojirimycin. (5/973)

Sandhoff disease is a neurodegenerative disorder resulting from the autosomal recessive inheritance of mutations in the HEXB gene, which encodes the beta-subunit of beta-hexosaminidase. GM2 ganglioside fails to be degraded and accumulates within lysosomes in cells of the periphery and the central nervous system (CNS). There are currently no therapies for the glycosphingolipid lysosomal storage diseases that involve CNS pathology, including the GM2 gangliosidoses. One strategy for treating this and related diseases is substrate deprivation. This would utilize an inhibitor of glycosphingolipid biosynthesis to balance synthesis with the impaired rate of catabolism, thus preventing storage. One such inhibitor is N-butyldeoxynojirimycin, which currently is in clinical trials for the potential treatment of type 1 Gaucher disease, a related disease that involves glycosphingolipid storage in peripheral tissues, but not in the CNS. In this study, we have evaluated whether this drug also could be applied to the treatment of diseases with CNS storage and pathology. We therefore have treated a mouse model of Sandhoff disease with the inhibitor N-butyldeoxynojirimycin. The treated mice have delayed symptom onset, reduced storage in the brain and peripheral tissues, and increased life expectancy. Substrate deprivation therefore offers a potentially general therapy for this family of lysosomal storage diseases, including those with CNS disease.  (+info)

Androgen regulation of glycosidase secretion in epithelial cell cultures from human epididymis. (6/973)

The human epididymis and its secretions actively promote sperm fertilizing capacity and provide protection for spermatozoa against harmful influences. Among epididymal secretions, glycosidases have been recently studied and associated with molecular changes on the sperm surface. In the present work, we studied the influence of different concentrations of testosterone, dihydrotestosterone and cyproterone acetate on the secretion of alpha-glucosidase, N-acetyl-glucosaminidase, beta-glucuronidase and alpha-mannosidase by isolated and cultured epithelial cells from human caput, corpus and cauda epididymides. Cell cultures were obtained from aggregates of isolated tubule fragments plated on extracellular matrix-covered multi-well plates. Activities of the glycosidases were measured in conditioned culture media and were higher in the distal regions of the epididymis. Testosterone and dihydrotestosterone significantly increase the enzyme secretion in a concentration-dependent manner. This increase was higher in corpus and/or cauda than in caput epididymis. Cyproterone acetate caused a dose-dependent decrease in glycosidase secretion in cultures from all epididymal regions. It is concluded that the secretion of epididymal glycosidases is regulated by androgen, being stimulated by dihydrotestosterone and testosterone and inhibited by the androgen antagonist cyproterone acetate.  (+info)

Coordinate transcriptional control in the hyperthermophilic archaeon Sulfolobus solfataricus. (7/973)

The existence of a global gene regulatory system in the hyperthermophilic archaeon Sulfolobus solfataricus is described. The system is responsive to carbon source quality and acts at the level of transcription to coordinate synthesis of three physically unlinked glycosyl hydrolases implicated in carbohydrate utilization. The specific activities of three enzymes, an alpha-glucosidase (malA), a beta-glycosidase (lacS), and an alpha-amylase, were reduced 4-, 20-, and 10-fold, respectively, in response to the addition of supplementary carbon sources to a minimal sucrose medium. Western blot analysis using anti-alpha-glucosidase and anti-beta-glycosidase antibodies indicated that reduced enzyme activities resulted exclusively from decreased enzyme levels. Northern blot analysis of malA and lacS mRNAs revealed that changes in enzyme abundance arose primarily from reductions in transcript concentrations. Culture conditions precipitating rapid changes in lacS gene expression were established to determine the response time of the regulatory system in vivo. Full induction occurred within a single generation whereas full repression occurred more slowly, requiring nearly 38 generations. Since lacS mRNA abundance changed much more rapidly in response to a nutrient down shift than to a nutrient up shift, transcript synthesis rather than degradation likely plays a role in the regulatory response.  (+info)

Purification and characterization of an alpha-glucosidase from Rhizobium sp. (Robinia pseudoacacia L.) strain USDA 4280. (8/973)

A novel alpha-glucosidase with an apparent subunit mass of 59 +/- 0. 5 kDa was purified from protein extracts of Rhizobium sp. strain USDA 4280, a nodulating strain of black locust (Robinia pseudoacacia L), and characterized. After purification to homogeneity (475-fold; yield, 18%) by ammonium sulfate precipitation, cation-exchange chromatography, hydrophobic chromatography, dye chromatography, and gel filtration, this enzyme had a pI of 4.75 +/- 0.05. The enzyme activity was optimal at pH 6.0 to 6.5 and 35 degrees C. The activity increased in the presence of NH4+ and K+ ions but was inhibited by Cu2+, Ag+, Hg+, and Fe2+ ions and by various phenyl, phenol, and flavonoid derivatives. Native enzyme activity was revealed by native gel electrophoresis and isoelectrofocusing-polyacrylamide gel electrophoresis with fluorescence detection in which 4-methylumbelliferyl alpha-glucoside was the fluorogenic substrate. The enzyme was more active with alpha-glucosides substituted with aromatic aglycones than with oligosaccharides. This alpha-glucosidase exhibited Michaelis-Menten kinetics with 4-methylumbelliferyl alpha-D-glucopyranoside (Km, 0.141 microM; Vmax, 6.79 micromol min-1 mg-1) and with p-nitrophenyl alpha-D-glucopyranoside (Km, 0.037 microM; Vmax, 2.92 micromol min-1 mg-1). Maltose, trehalose, and sucrose were also hydrolyzed by this enzyme.  (+info)

*Alpha-glucosidase

... alpha-D-glucosidase, alpha-glucoside hydrolase, alpha-1,4-glucosidase, alpha-D-glucoside glucohydrolase) is a glucosidase ... Alglucosidase alfa Alpha-glucosidase inhibitor alpha-Glucosidases at the US National Library of Medicine Medical Subject ... Diabetes: Acarbose, an alpha-glucosidase inhibitor, competitively and reversibly inhibits alpha-glucosidase in the intestines. ... Other glucosidases include: Cellulase Beta-glucosidase Debranching enzyme Alpha-glucosidase hydrolyzes terminal non-reducing (1 ...

*Glucosidases

Members marked with a "#" are considered by MeSH to be glucosidases. They are targeted by alpha-glucosidase inhibitors such as ... Glucosidases are glycoside hydrolase enzymes categorized under the EC number 3.2.1. α-glucosidases are enzymes involved in ... into their monomers They catalyze the cleavage of individual glucosyl residues from various glycoconjugates including alpha- or ... acarbose and miglitol to control diabetes mellitus type 2. DNA glycosylases Mucopolysaccharidoses Glucosidases at the US ...

*Sucrose alpha-glucosidase

... (EC 3.2.1.48, sucrose alpha-glucohydrolase, sucrase, sucrase-isomaltase, sucrose.alpha.- ... Sucrose alpha-glucosidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... This enzyme catalyses the following chemical reaction Hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action ... glucohydrolase, intestinal sucrase, sucrase(invertase)) is an enzyme with systematic name sucrose-alpha-D-glucohydrolase. ...

*Acid alpha-glucosidase

Lysosomal alpha-glucosidase, also called α-1,4-glucosidase and acid maltase, is an enzyme (EC 3.2.1.20) that in humans is ... 1991). "Human lysosomal alpha-glucosidase. Characterization of the catalytic site". J. Biol. Chem. 266 (21): 13507-12. PMID ... Errors in this gene cause glycogen storage disease type II (Pompe disease). This gene encodes acid alpha-glucosidase, which is ... Ratner L, vander Heyden N, Dedera D (1991). "Inhibition of HIV and SIV infectivity by blockade of alpha-glucosidase activity". ...

*Alpha-glucosidase inhibitor

Hence, alpha-glucosidase inhibitors reduce the impact of carbohydrates on blood sugar. Examples of alpha-glucosidase inhibitors ... Acarbose also blocks pancreatic alpha-amylase in addition to inhibiting membrane-bound alpha-glucosidases. Pancreatic alpha- ... Moreover, acarbose inhibits pancreatic alpha-amylase in addition to alpha-glucosidase. There are a large number of natural ... specifically alpha-glucosidase enzymes in the brush border of the small intestines. The membrane-bound intestinal alpha- ...

*Glucan endo-1,3-alpha-glucosidase

... (EC 3.2.1.59, endo-1,3-alpha-glucanase, mutanase, endo-(1->3)-alpha-glucanase, cariogenase, ... Glucan endo-1,3-alpha-glucosidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ... 3-alpha-D-glucan) are nigerose and alpha-D-glucose. Hasegawa, S.; Nordin, J.H.; Kirkwood, S. (1969). "Enzymes that hydrolyze ... alpha-D-glucan 3-glucanohydrolase) is an enzyme with systematic name 3-alpha-D-glucan 3-glucanohydrolase. This enzyme catalyses ...

*Glucan 1,3-alpha-glucosidase

... (EC 3.2.1.84, exo-1,3-alpha-glucanase, glucosidase II, 1,3-alpha-D-glucan 3-glucohydrolase) is an ... Glucan 1,3-alpha-glucosidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ... This enzyme catalyses the following chemical reaction Hydrolysis of terminal (1->3)-alpha-D-glucosidic links in (1->3)-alpha-D- ... enzyme with systematic name 3-alpha-D-glucan 3-glucohydrolase. ...

*Branched-dextran exo-1,2-alpha-glucosidase

2-alpha-glucosidase (EC 3.2.1.115, dextran 1,2-alpha-glucosidase, dextran alpha-1,2 debranching enzyme, 1,2-alpha-D-glucosyl- ... Branched-dextran exo-1,2-alpha-glucosidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and ... This enzyme catalyses the following chemical reaction Hydrolysis of (1->2)-alpha-D-glucosidic linkages at the branch points of ... 2-alpha-glucosidic linkages. Mitsuishi, Y.; Kobayashi, M.; Matsuda, K. (1979). "Dextran α-1,2-debranching enzyme from ...

*Amylo-alpha-1,6-glucosidase

... (EC 3.2.1.33, amylo-1,6-glucosidase, dextrin 6-alpha-D-glucosidase, amylopectin 1,6-glucosidase, ... dextrin-1,6-glucosidase, glycogen phosphorylase-limit dextrin alpha-1,6-glucohydrolase) is an enzyme with systematic name ... Lee, E.Y.C.; Carter, J.H.; Nielsen, L.D.; Fischer, E.H. (1970). "Purification and properties of yeast amylo-1,6-glucosidase- ... Nelson, T.E.; Kolb, E.; Larner, J. (1969). "Purification and properties of rabbit muscle amylo-1,6-glucosidase-oligo-1,4-1,4- ...

*Hesperidin 6-O-alpha-L-rhamnosyl-beta-D-glucosidase

... (EC 3.2.1.168) is an enzyme with systematic name hesperetin 7-(6-O-alpha-L- ... doi:10.1007/s00203-011-0709-6. Hesperidin 6-O-alpha-L-rhamnosyl-beta-D-glucosidase at the US National Library of Medicine ... rhamnopyranosyl-beta-D-glucopyranoside) 6-O-alpha-rhamnopyranosyl-beta-glucohydrolase. This enzyme catalyses the following ...

*Glycoside hydrolase family 15

... alpha-glucosidase (EC 3.2.1.20); glucodextranase (EC 3.2.1.70). Glucoamylase (GA) catalyses the release of D-glucose from the ... The protein belongs to the mainly alpha class, and contains 19 helices and 9 strands. Henrissat B, Callebaut I, Mornon JP, ...

*Maltase-glucoamylase

Alpha-glucosidase Maltase ENSG00000282607 GRCh38: Ensembl release 89: ENSG00000257335, ENSG00000282607 - Ensembl, May 2017 ... Maltase-glucoamylase is an alpha-glucosidase digestive enzyme. It consists of two subunits with differing substrate specificity ... 2008). "Clinical, endocrine, and metabolic effects of acarbose, an alpha-glucosidase inhibitor, in overweight and nonoverweight ... alpha-glucosidase)". Nichols BL, Eldering J, Avery S, Hahn D, Quaroni A, Sterchi E (January 1998). "Human small intestinal ...

*Glycogen debranching enzyme

6-glucosidase (EC 3.2.1.33), or glucosidase, cleaves the remaining alpha-1,6 linkage, producing glucose and a linear chain of ... Yamamoto E, Makino Y, Omichi K (May 2007). "Active site mapping of amylo-alpha-1,6-glucosidase in porcine liver glycogen ... Gillard BK, White RC, Zingaro RA, Nelson TE (September 1980). "Amylo-1,6-glucosidase/4-alpha-glucanotransferase. Reaction of ... Gillard BK, Nelson TE (September 1977). "Amylo-1,6-glucosidase/4-alpha-glucanotransferase: use of reversible substrate model ...

*Trefoil domain

... and lysosomal alpha-glucosidase (EC 3.2.1.20). Human gene encoding proteins containing the trefoil domain include: acid alpha- ... glucosidase, MGAM, TFF1, TFF2, TFF3, and ZP4. Gajhede M, Petersen TN, Henriksen A, et al. (December 1993). "Pancreatic ...

*Glycoside hydrolase family 4

6-phospho-alpha-glucosidase (EC 3.2.1.122); alpha-galactosidase (EC 3.2.1.22). 6-phospho-alpha-glucosidase requires both NAD(H ... dependent 6-phospho-alpha-glucosidase. Assignment to family 4 of the glycosylhydrolase superfamily". J. Biol. Chem. 273 (42): ... Glycoside hydrolase family 4 CAZY GH_4 comprises enzymes with several known activities; 6-phospho-beta-glucosidase (EC 3.2.1.86 ...

*Diplazium esculentum

The extract also had alpha-glucosidase inhibitory activity. Yam phak khut: a Thai salad of fern leaves and pork. A vegetable ... Ethnobotanical Leaflets Chai TT, Yeoh LY, Mohd Ismail NI, Ong HC, Abd Manan F, Wong FC (2015) Evaluation of glucosidase ...

*Miglitol

Alpha-glucosidase inhibitor Miglustat "Migliotl: MedlinePlus Drug Information". MedlinePlus. National Institutes of Health. 1 ... In contrast to acarbose (another alpha-glucosidase inhibitor), miglitol is systemically absorbed; however, it is not ... Miglitol, and other structurally-related iminosugars, inhibit glycoside hydrolase enzymes called alpha-glucosidases. Since ...

*Maltose-6'-phosphate glucosidase

This enzyme is also called phospho-alpha-glucosidase. As of late 2007, only one structure has been solved for this class of ... In enzymology, a maltose-6'-phosphate glucosidase (EC 3.2.1.122) is an enzyme that catalyzes the chemical reaction maltose 6'- ... "Purification from Fusobacterium mortiferum ATCC 25557 of a 6-phosphoryl-O-alpha-D-glucopyranosyl:6-phosphoglucohydrolase that ... hydrolyzes maltose 6-phosphate and related phospho-alpha-D-glucosides". J. Bacteriol. 177 (9): 2505-12. PMC 176911 . PMID ...

*GANC

Kamimura H, Ogata H, Takahara H (1992). "Alpha-glucoside formation of xenobiotics by rat liver alpha-glucosidases". Drug ... Neutral alpha-glucosidase C is an enzyme that in humans is encoded by the GANC gene. Glycoside hydrolase enzymes hydrolyse the ... "Entrez Gene: GANC glucosidase, alpha; neutral C". Feizi T, Larkin M (Sep 1990). "AIDS and glycosylation". Glycobiology. 1 (1): ... Hirschhorn R, Huie ML, Kasper JS (Oct 2002). "Computer assisted cloning of human neutral alpha-glucosidase C (GANC): a new ...

*Streptomyces galbus

Drug Concentration Monitoring Microbial Alpha-Glucosidase Inhibitors Plasminogen Activators. Berlin, Heidelberg: Springer ...

*Glycoside hydrolase family 31

... alpha-glucosidase (EC 3.2.1.20), alpha-galactosidase (EC 3.2.1.22); glucoamylase (EC 3.2.1.3), sucrase-isomaltase (EC 3.2.1.48 ... van Beeumen J, Kroos MA, Oostra BA, Hermans MM, Reuser AJ (1991). "Human lysosomal alpha-glucosidase. Characterization of the ... Homology with the rabbit intestinal sucrase-isomaltase complex and human lysosomal alpha-glucosidase". Eur. J. Biochem. 202 (2 ... and lysosomal alpha-glucosidase. Henrissat B, Callebaut I, Mornon JP, Fabrega S, Lehn P, Davies G (1995). "Conserved catalytic ...

*Sucrase-isomaltase

6-glucosidase, dextrin 6alpha-glucanohydrolase, alpha-limit dextrine, dextrin 6-glucanohydrolase, and oligosaccharide alpha-1,6 ... "SI sucrase-isomaltase (alpha-glucosidase) [Homo sapiens (human)] - Gene - NCBI". "The mode of association of the enzyme complex ... Sucrase-isomaltase (EC 3.2.1.10), is a glucosidase enzyme located on the brush border of the small intestine. It has ... The systematic name of systematic name of sucrase-isomaltase is oligosaccharide 6-alpha-glucohydrolase. This enzyme is also ...

*Medicinal fungi

Many fungal isolates act as DPP-4 inhibitors, alpha-glucosidase inhibitors, and alpha amylase inhibitors in vitro. Ternatin is ... Aspergillusol A is an alpha-glucosidase inhibitor made by Aspergillus. Sclerotiorin is an aldose reductase inhibitor made by ...

*Aspergillusol A

Ullah, N.; Haladu, S. A. (2010). "The first total synthesis of aspergillusol A, an alpha-glucosidase inhibitor". Natural ... Aspergillusol A is an alpha-glucosidase inhibitor isolated from marine Aspergillus. Structurally, it consists of an erythritol ... an alpha-glucosidase inhibitor from the marine-derived fungus Aspergillus aculeatus". Journal of Natural Products. 72 (11): ...

*Castanospermine

"Castanospermine inhibits alpha-glucosidase activities and alters glycogen distribution in animals". PNAS. 82 (1): 93-97. doi: ... It is a potent inhibitor of some glucosidase enzymes and has antiviral activity in vitro and in mouse models. Castanospermine ...

*Naringinase

It is a multienzyme complex which possesses alpha-L-rhamnosidase and beta glucosidase active centers. The E.C. No.(EC 3.2.1.40 ... Lastly glucosidase breaks prunin into glucose and naringenin, a flavorless flavanone also found in various citrus. Ram gene is ...

*GCS1

Glucosidase I is the first enzyme in the N-linked oligosaccharide processing pathway. GCS1 cleaves the distal alpha-1,2-linked ... Ratner L, vander Heyden N, Dedera D (1991). "Inhibition of HIV and SIV infectivity by blockade of alpha-glucosidase activity". ... "Entrez Gene: GCS1 glucosidase I". "Gamete Fusion: Key Protein Identified". Retrieved 06.05.09. Check date values in: ,access- ... Kalz-Fuller B, Heidrich-Kaul C, Nothen M, Bause E, Schwanitz G (Sep 1996). "Localization of the human glucosidase I gene to ...
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Castilla, C.; Paris, H.; Murat, J.C., 1979: Evidence of a similar distribution of neutral alpha glucosidase ec 3.2.1.3 and glucose 6 phosphatase in sub cellular fractions of rat and trout liver
Global Lysosomal Alpha Glucosidase Sales Market Report 2017 is a market research report available at US $4000 for a Single User PDF License from RnR Market Research Reports Library.
... (AGIs) are a class of drugs used to treat type 2 diabetes. The key benefit of AGIs is that they do not cause hypoglycemia (low blood sugar) or weight gain and are taken orally. These drugs help lower blood sugar levels in the body by blocking the breakdown of starchy foods like bread and potatoes in the intestine and thus delaying the absorption of carbohydrates, according to the American Diabetes Association They also slow down the breakdown of some sugars, like table sugar. Because they work to slow digestion, AGIs are taken at the start of a meal. The alpha-glucosidase inhibitors available today (with brand names in parenthesis) are: acarbose (Precose) miglitol (Glyset) An ADA published article states that
Alpha-glucosidase (EC 3.2.1.20, maltase, glucoinvertase, glucosidosucrase, maltase-glucoamylase, alpha-glucopyranosidase, glucosidoinvertase, alpha-D-glucosidase, alpha-glucoside hydrolase, alpha-1,4-glucosidase, alpha-D-glucoside glucohydrolase) is a glucosidase located in the brush border of the small intestine that acts upon α(1→4) bonds. This is in contrast to beta-glucosidase. Alpha-glucosidase breaks down starch and disaccharides to glucose. Maltase, a similar enzyme that cleaves maltose, is nearly functionally equivalent. Other glucosidases include: Cellulase Beta-glucosidase Debranching enzyme Alpha-glucosidase hydrolyzes terminal non-reducing (1→4)-linked alpha-glucose residues to release a single alpha-glucose molecule. Alpha-glucosidase is a carbohydrate-hydrolase that releases alpha-glucose as opposed to beta-glucose. Beta-glucose residues can be released by glucoamylase, a functionally similar enzyme. The substrate selectivity of alpha-glucosidase is due to subsite affinities ...
Alpha-glucosidase Inhibitors are great treatment options for those with high glucose levels. Get facts about Alpha-glucosidase inhibitors.
This gene encodes the alpha subunit of glucosidase II and a member of the glycosyl hydrolase 31 family of proteins. The heterodimeric enzyme glucosidase II plays a role in protein folding and quality control by cleaving glucose residues from immature glycoproteins in the endoplasmic reticulum. Expression of the encoded protein is elevated in lung tumor tissue and in response to UV irradiation. Mutations in this gene cause autosomal-dominant polycystic kidney and liver disease. [provided by RefSeq, Jul 2016 ...
In general terms, skeletal muscle mass is maintained by a precise dynamic balance between protein synthesis and degradation. Even a small sustained decrease in synthesis or increase in protein breakdown can affect the equilibrium and lead to atrophy (Sandri, 2016). At a molecular level, the reduced rate of protein synthesis is associated with impaired signaling through mTORC1, a major regulator of this anabolic process. This study is the first attempt to systematically analyze mTOR signaling pathway in Pompe disease, an inherited deficiency of lysosomal acid alpha‐glucosidase, in which the primary defect-intralysosomal glycogen accumulation-leads to numerous secondary abnormalities including defective autophagy, aberrant mitochondria and calcium homeostasis, and severe muscle wasting (reviewed in Lim et al 2014). We have found that the basal activity of mTOR in Pompe muscle cells is reduced; that mTOR is less sensitive to starvation and refeeding; that the relationship between the mTOR ...
In general terms, skeletal muscle mass is maintained by a precise dynamic balance between protein synthesis and degradation. Even a small sustained decrease in synthesis or increase in protein breakdown can affect the equilibrium and lead to atrophy (Sandri, 2016). At a molecular level, the reduced rate of protein synthesis is associated with impaired signaling through mTORC1, a major regulator of this anabolic process. This study is the first attempt to systematically analyze mTOR signaling pathway in Pompe disease, an inherited deficiency of lysosomal acid alpha‐glucosidase, in which the primary defect-intralysosomal glycogen accumulation-leads to numerous secondary abnormalities including defective autophagy, aberrant mitochondria and calcium homeostasis, and severe muscle wasting (reviewed in Lim et al 2014). We have found that the basal activity of mTOR in Pompe muscle cells is reduced; that mTOR is less sensitive to starvation and refeeding; that the relationship between the mTOR ...
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Alpha-glucosidase inhibitors work by ambitious and reversible inhibition of those intestinal enzymes. They diminish the digestion of carbohydrates and delay glucose absorption. This happens in a smaller and moderate rise in blood glucose levels following meals, and efficiently throughout the day.. AGIs have exhibited in reducing post-meal blood sugars and therefore helping to lower HbA1c, especially while used in combination with other diabetes drugs.. ...
alpha Glucosidase II antibody [N1N2], N-term (glucosidase, alpha; neutral AB) for ICC/IF, IHC-P, WB. Anti-alpha Glucosidase II pAb (GTX102237) is tested in Human, Mouse samples. 100% Ab-Assurance.
Alpha-glucosidase inhibitors, a class of drugs also known as starch blockers, function by slowing the absorption of certain carbohydrates in the gastrointestinal tract.
An enzyme which removes the last 1,4-linked alpha-D-glucose residue from the nonreducing end of a long chain (or polymer) of such residues, making an al...
Im sorry Nancy, but they are two completely different enzymes, that catalyze two totally different reactions. The only similarities are that they are both acid hydrolases, and are present in lysosomes, but thats like saying a Kia and a Lexus are both cars. Acid phosphatase (EC 3.1.3.2) catalyzes the hydrolysis of esters of orthophosphoric acid. It also nydrolyses pyrophosphate compounds and acts as a transphosphorylase. It has an optimum pH of between 4 and 5. Acid phosphatase is mainly found in lysosomes. However there are also extralysosomal acid phosphatases found in endoplasmic reticulum. It is possible to differentiate the acid phosphatases by their sensitivity to various inhibitors. Acid phosphatase activity is high in spleen, kidney, liver, intestine, and adrenals. Acid maltase (EC 3.1.3.20), also know as acid alpha-d-glucosidase, in simple terms breaks down maltose to glucose. It has a optimal pH of 5. Acid maltase is present in liver kidney and brain. A deficiency of acid maltase ...
The present invention relates to an allosteric non-inhibitory chaperone of the lysosomal acid alpha-glucosidase (GAA) for use in the treatment of a pathological condition characterized by a deficiency of the lysosomal acid alpha-glucosidase (GAA), to pharmaceutical composition thereof, to a method for increasing the activity of GAA in a subject
en] Type 2 diabetes mellitus is a major health problem associated with excess morbidity and mortality. As the prevalence of this metabolic disorder is rapidly increasing and current treatment fails to stabilise the disease in most patients, prevention should be considered as a key objective in the near future. People who develop type 2 diabetes pass through a phase of impaired glucose tolerance (IGT). Defects in the action and/or secretion of insulin are the two major abnormalities leading to development of glucose intolerance. Any intervention in the impaired glucose tolerance phase that reduces resistance to insulin or protects the beta-cells, or both, should prevent or delay progression to diabetes.Acarbose, miglitol and voglibose act by competitively inhibiting the alpha-glucosidases, a group of key intestinal enzymes involved in the digestion of carbohydrates. They decrease both postprandial hyperglycaemia and hyperinsulinaemia, and thereby may improve sensitivity to insulin and release the ...
A Century of Diabetes Care Pump therapy Human insulin Insulin analogs First human treated NPH insulin Type Insulin therapy 1920 Type Diet Sulfonylureas Alpha-glucosidase Inhibitors Biguanide Glitazones Meglitinides Insulin therapy Type 1 Since the early 1920s the only therapy available for type 1 diabetes has been insulin. (Banting and Best discovered insulin 1921) Improvements in insulin delivery have included pump therapy (mid-1970s), transition from animal to human insulin (1980s)1979 and the introduction of rapid acting insulin analogs (1990s) Type 2 Altlhough insulin has been available for type 2 diabetes patients since the 1920s, the major development has been the introduction of a number of oral agents: Sulfonylureas, the first available oral hypoglycemic agents (1956) Metformin (biguanides), although available in Europe for many years, recently available in this country since 1995 Alpha glucosidase inhibitors (starch blockers), thiazolidinediones (glitazones) and megltinides, agents
Aims: This paper mentions of the investigation of the enzymes binding to Voglibose and the choice of the enzyme which is suitable for drug enzyme interaction as used in biosensing. Voglibose is an antidiabetic drug which is reactive and hence used in very low concentrations. The existing methods of analysis of this drug are associated with certain disadvantages. Hence there is a need to establish alternative and simpler method of analysis which could be based on biosensing. The paper focuses on identification of the enzyme binding to the drug Voglibose.. Study Design: In this work there are two enzyme namely alpha amylase and alpha glucosidase which are considered as the potential targets for drug enzyme interaction for the drug Voglibose. The study is based on two approaches. The first one is molecular docking process done to verify the inhibition activity of the enzyme by the drug and the next method is chemical analysis to confirm the results obtained in molecular docking.. Place and Duration ...
A 52-week, Randomised, Multi-centre, Parallel Group Study to Investigate the Safety and Efficacy of BI 10773 (10 mg or 25 mg Administered Orally Once Daily) as add-on Therapy to an Oral Antidiabetic Drug (Sulfonylurea, Biguanide, Thiazolidinedione, Alpha Glucosidase Inhibitor, DPP-IV Inhibitor, or Glinide) in Patients With Type 2 Diabetes Mellitus With Insufficient Glycaemic ...
In the previous Medicare study of patients with diabetes discharged after hospital admission for acute myocardial infarction,w3 after multivariate adjustment, the risk of all cause mortality at one year was no different for patients who received thiazolidinediones (n=255) than for patients treated with sulfonylureas, non-sulfonylurea insulin secretagogues, alpha glucosidase inhibitors, or insulin (1.04, 0.83 to 1.31; table 1). There was a trend, however, towards an increased risk of readmission for heart failure associated with thiazolidinediones (n=255; 1.15, 0.97 to 1.38).w3. In the second Medicare study of patients with diabetes discharged with a primary diagnosis of heart failure, after multivariate adjustment as above (n=12 069), all cause mortality at one year was significantly lower for patients treated with thiazolidinediones (n=2226; 0.87, 0.80 to 0.94; table 1).w1 This study also found no difference in the risk for all cause hospital readmissions for patients receiving ...
Neutral a-glucosidase (NAG) activity in human seminal plasma is an important indicator for epididymis functionality. In the present study, the classic World Health Organization (WHO) method has been adapted to enhance assay robustness. Changes include modified enzyme reaction buffer composition and usage of an alternative enzyme inhibitor for background correction (glucose instead of castanospermine). Both methods have been tested in parallel on 144 semen samples, obtained from 94 patients/donors and 50 vasectomized men (negative control), respectively. Passing-Bablok regression analysis demonstrated equal assay performance. In terms of assay validation, analytical specificity, detection limit, measuring range, precision, and cut-off values have been calculated. These data confirm that the adapted method is a reliable, improved tool for NAG analysis in human semen.
Neutral a-glucosidase (NAG) activity in human seminal plasma is an important indicator for epididymis functionality. In the present study, the classic World Health Organization (WHO) method has been adapted to enhance assay robustness. Changes include modified enzyme reaction buffer composition and usage of an alternative enzyme inhibitor for background correction (glucose instead of castanospermine). Both methods have been tested in parallel on 144 semen samples, obtained from 94 patients/donors and 50 vasectomized men (negative control), respectively. Passing-Bablok regression analysis demonstrated equal assay performance. In terms of assay validation, analytical specificity, detection limit, measuring range, precision, and cut-off values have been calculated. These data confirm that the adapted method is a reliable, improved tool for NAG analysis in human semen.
Professionals recommend that, most of hypoglycemic drugs may have a harmful effect on the body. Sulfonylurea and glinides can cause liver damage. Biguanides also lead to gastrointestinal reaction and lactic acidosis, or anaphylaxis and large cell anemia reaction for the little users. As to alpha glucosidase inhibitor, the main side effect is causing gastrointestinal reaction, and which may cause abdominal distension, stomachache, diarrhea and intestinal exhaust too much. Besides, it is reported that the drugs might lead to severe hepatic lesion. Insulin sensitizer can not only trigger liver damage3but also increase the blood volume and the burden of heart ...
Alpha glucosidase inhibitor --- ( Kwon, Y., Apostolidis, E., Labbe, R. and Shetty, K. (2007). Inhibition of Staphylococcus aureus by Phenolic Phytochemicals of Selected Clonal Herbs Species of Lamiaceae Family and Likely Mode of Action through Proline Oxidation. Food Biotechnology, 21(1), pp.71-89 ...
The other activity is similar to that of EC 2.4.1.25, which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-alpha-glucosidase activity can then hydrolyze ...
D,L-1,2-Anhydro-myo-inositol; Inhibits alpha-glucosidase activity; specific inhibitor of glucocerebrosidase in cultured cells ...
In the present study a comparative investigation on the divergence of α-glucosidase (α-Gls) enzyme was performed. The complete amino acid sequences of different species as stated in the materials and methods were aligned. The mammalian α-Gls enzymes are heterodimeric proteins with α-glucosidic activity. The enzymes contain a region responsible for the catalytic site for an enzyme termed glucoamylase. The comparative results from the present investigation showed that human and chimpanzee α-glucosidases had the closest similarity, and may have come from the same ancestor. There are two conserve P-type domains in human MGAM located in positions 88-134 and 954-1000 [16], which is completely conserved in chimpanzee`s enzyme. These domains have some synonymous amino acid alterations in rat and mouse MGAM. Interestingly, these domains are absent in plants and bacterial counterparts. There are two catalytic aspartic acid residues in mammalian enzymes which due to their nucleophilic nature has a ...
Figure 6: Total phenolics and Antioxidant activity of long term stored apples from Grocery stores (Levels are maintained and in several cases increased with post-harvest storage) Figure 7: Long term stored grocery store varieties maintain and in some cases increase the alpha-glucosidase bioactive function in proportion to total phenolics and antioxidant activity. Table 1: Quercetin Content as Determined by HPLC: units: micrograms/gram peel) Water Extracts of Peel Ethanol Extracts of Peel Ginger gold 128 ± 5 142 ± 3 Honeycrisp 144 ± 3 554 ± 5 Gala 93 ± 2 68 ± 1 McIntosh 101 ± 2 534 ± 6 Jonagold 286 ± 5 213 ± 2 Empire 41 ± 1 327 ± 5 Braeburn 390 ± 3 419 ± 6 Golden delicious 84 ± 3 119 ± 3 Fuji 136 ± 2 74 ± 2 Red delicious 133 ± 3 171 ± 3 The peel samples have higher diabetes relevant alpha-glucosidase inhibitory activity , which the target of the current pharmaceutical acarabose for this early stages type 2 diabetes target (Figure 1& 5). All varieties have good baseline and ...
Home » Maltobionate alpha-glucosidase. Maltobionate alpha-glucosidase (Science: enzyme) An intracellular enzyme capable of hydrolyzing maltobionic acid; from alkalophilic bacillus sp. N-1053 registry number: EC 3.2.1.- Synonym: maltobionate alpha-d-glucohydrolase ...
Mgam - mouse gene knockout kit via CRISPR, 1 kit. |dl||dt|Kit Component:|/dt||dd|- |strong|KN310054G1|/strong|, Mgam gRNA vector 1 in |a href=http://www.origene.com/CRISPR-CAS9/Detail.
When programmed with yeast prepro-α-factor mRNA, the heterologous reticulocyte/dog pancreas translation system synthesizes two pheromone related polypeptides, a cytosolically located primary translation product (pp-α-Fcyt, 21 kDa) and a membrane-specific and multiply glycosylated e-factor precursor (pp-α-F3, 27.5 kDa). Glycosylation of the membrane specific pp-α-F3 species is competitively inhibited by synthetic peptides containing the consensus sequence Asn-Xaa-Thr as indicated by a shift of its molecular mass from 27.5 kDa to about 19.5 kDa (pp-α-F0), whereas the primary translation product pp-α-F cyt is not affected. Likewise, only the glycosylated pp-α-F3 structure is digested by Endo H yielding a polypeptide with a molecular mass between PP-α-F0 and pp-α-F cyt. These observations strongly suggest that the primary translation product is proteolytically processed during/on its translocation into the lumen of the microsomal vesicles. We believe that this proteolytic processing is due ...
An alpha-glucosidase test can reveal a secretory dysfunction of the epididymis and reduced quality of the semen caused by this disorder.
2QLY: Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity
Pompe disease is caused by a deficiency of a critical enzyme in the body called acid alpha glucosidase (GAA). Normally, GAA is used by the bodys cells to break down glycogen (a stored form of sugar) within specialized structures called lysosomes. In infants with severe cases of Pompe disease (called Classical Infantile Pompe disease), an excessive amount of glycogen accumulates and is stored in various tissues, especially heart, skeletal muscle, and liver, which prevents their normal function. This study being conducted to evaluate the safety and effectiveness of recombinant human acid alpha-glucosidase (rhGAA) as a potential enzyme replacement therapy for Pompe disease. Patients diagnosed with Classical Infantile Pompe disease who have a small, but inactive, amount of natural GAA enzyme present in their bodies (called Cross-Reacting Immunologic Material-Positive or CRIM (+) patients), will be studied ...
This report demonstrates that a single intravenous administration of a gene therapy vector can potentially result in the correction of all affected muscles in a mouse model of a human genetic muscle disease. These results were achieved by capitalizing both on the positive attributes of modified adenovirus-based vectoring systems and receptor-mediated lysosomal targeting of enzymes. The muscle disease treated, glycogen storage disease type II, is a lysosomal storage disorder that manifests as a progressive myopathy, secondary to massive glycogen accumulations in the skeletal and/or cardiac muscles of affected individuals. We demonstrated that a single intravenous administration of a modified Ad vector encoding human acid alpha-glucosidase (GAA) resulted in efficient hepatic transduction and secretion of high levels of the precursor GAA proenzyme into the plasma of treated animals. Subsequently, systemic distribution and uptake of the proenzyme into the skeletal and cardiac muscles of the GAA-knockout
Alglucosidase alfa contains an enzyme that naturally occurs in the body in healthy people. Some people lack this enzyme because of a genetic disorder. Alglucosidase alfa helps replace this missing enzyme in such people. Alglucosidase alfa is used to treat a glycogen storage disorder called Pompe disease, (also called...
Abstract of Dr. Amalfitanos proposal: Acid Maltase Deficiency (AMD, also known as Pompe Disease), is due to a patients inability to produce enough acid alpha glucosidase (GAA). This results in glycogen accumulation in the patients limb muscles, as well as cardiac muscles (in those patients affected by the early age onset (infantile) form of the disease). Based upon published results using animal models, intravenous infusion of recombinant rhGAA (Myozyme® or Lumizyme®) at current doses is not adequate to provide maximal improvement to so-treated AMD/Pompe patients. However, current production methods for recombinant proteins such as GAA may not be capable of producing enough GAA enzyme to support higher and more frequent dosing. Our multiple, previously published studies confirm that a single "Gene Therapy" treatment of most AMD/Pompe patients can potentially overcome this problem, by allowing for high level production of GAA from the livers of AMD/Pompe patients for a continuous period of ...
CONCORD, Mass., July 11, 2017-Valerion Therapeutics, a clinical-stage biotechnology company that specializes in the development of therapies for orphan genetic diseases, today announced that it has initiated dosing in a Phase 1/2 clinical trial evaluating VAL-1221 in patients with late-onset Pompe disease. VAL-1221 is a novel fusion protein that combines Valerions antibody-mediated delivery technology with recombinant human acid alpha-glucosidase (rhGAA) to uniquely target both lysosomal and extra-lysosomal glycogen in the cytoplasm through enhanced intracellular delivery to affected tissues. By leveraging two uptake mechanisms, rather than one, VAL-1221 offers the potential for improved glycogen clearance and better patient outcomes. The Company expects to report top-line data from the Phase 1/2 study in the fourth quarter of 2017.. "After a brief period of modest improvement with currently approved treatments, nearly all patients with late-onset Pompe disease resume their downward trajectory ...
Glycogen storage disease type II or Pompe disease is a severe neuromuscular disorder caused by mutations in the lysosomal enzyme, acid α-glucosidase (GAA), which result in pathological accumulation of glycogen throughout the body. Enzyme replacement therapy is available for Pompe disease; however, it has limited efficacy, has high immunogenicity, and fails to correct pathological glycogen accumulation in nervous tissue and skeletal muscle. Using bioinformatics analysis and protein engineering, we developed transgenes encoding GAA that could be expressed and secreted by hepatocytes. Then, we used adeno-associated virus (AAV) vectors optimized for hepatic expression to deliver the GAA transgenes to Gaa knockout (Gaa−/−) mice, a model of Pompe disease. Therapeutic gene transfer to the liver rescued glycogen accumulation in muscle and the central nervous system, and ameliorated cardiac hypertrophy as well as muscle and respiratory dysfunction in the Gaa−/− mice; mouse survival was also ...
[Effect of Psidium guajava leaf extract on alpha-glucosidase activity in small intestine of diabetic mouse].: The GPL water-soluble extract possesses the potent
Pompe disease, also called glycogen storage disease type II (GSD-II), is an autosomal recessive disorder due to a deficiency of the lysosomal enzyme acid alpha-1,4-glucosidase (abbreviated GAA). The function of the GAA enzyme, also known as acid maltase, is to breakdown glycogen in the lysosome. Absent or reduced GAA activity results in accumulation of glycogen within the lysosome, particularly in muscle cells. GSD-II is divided into two forms; an infantile form and a juvenile/adult onset form. In individuals with the infantile form of Pompe disease there is less than 1% of normal enzymatic activity, whereas in the juvenile/adult onset form there is some residual enzymatic activity. In Pompe disease, affected infants are severely hypotonic and have cardiomegaly. In addition, patients may have an enlarged tongue. The disease is usually fatal within the first year of life due cardiorespiratory failure. The clinical presentation in the juvenile/adult onset form (onset after 12 months of age) is ...
Pompe disease is a genetic condition that is caused by a specific gene in the body called GAA not working correctly. Normally, GAA makes an enzyme called alpha-glucosidase, also known as acid maltase. This enzyme breaks down glycogen in certain parts of cells called the lysosomes. Pompe disease is part of a larger group of about 50 conditions called lysosomal storage diseases, which all involve the lysosome not working properly. Glycogen is a type of carbohydrate, or nutrient, that needs to be broken down into a smaller form for our bodies to use. When GAA doesnt work, it cant make acid maltase and glycogen builds up in the cells instead of being broken down. Excess glycogen damages cells and causes progressive muscle weakness (myopathy), including the muscles needed for the body to move (skeletal muscle), the heart to pump (cardiac muscle), and the lungs to breathe (respiratory muscle). The symptoms of Pompe disease can start as early as the newborn period or even before birth, but some types ...
When the film Extraordinary Measures debuts on January 22, it will tell the story of one mans quest to obtain treatment for his children who suffer from a rare metabolic disorder called Pompe disease.. The real story began 20 years ago at Duke University Medical Center when pediatric geneticist Y.T. Chen, MD, PhD, began work on the first and only life-saving treatment for Pompe. In 2006, the FDA approved the use of Myozyme, which is manufactured and marketed by Genzyme Corporation, based on Dukes research. As a result, the children portrayed in the movie, and those who are living with Pompe worldwide, were treated with Myozyme and given their first fighting chance at life.. What Is Pompe Disease?. Pompe disease results when mutations occur in the gene that triggers the production of an enzyme called acid alpha-glucosidase (GAA). That enzyme is responsible for helping the body break down glycogen (sugar).. When it is absent or deficient the glycogen builds up in the bodys cells, damages ...
Recent studies have established the regulatory role of transcription factor EB (TFEB) in the lysosomal/autophagosomal fusion and exocytosis. We have shown that transcription factor E3 (TFE3) is another master regulator of lysosomal/autophagosomal biogenesis. ChIP-seq in muscle cells identified , 1000 TFE3 direct targets which are similar to known TFEB binding locations. The studies on the regulatory role of TFEB/TFE3 stem from our longstanding interest in Pompe disease, a lysosomal glycogen storage disorder caused by a deficiency of acid alpha glucosidase (GAA). In this severe myopathy, lysosomal glycogen accumulation leads to excessive autophagy and inhibition of the autophagic flux. Autophagic defect is associated with poor muscle response to enzyme replacement therapy. An alternative approach relies on the ability of TFEB and TFE3 to re-establish autophagic flux and induce lysosomal exocytosis in affected muscles. Indeed, overexpression of TFEB or TFE3 in Pompe muscle reduced the lysosomal ...
Find a comprehensive guide to possible side effects including common and rare side effects when taking Lumizyme (Alglucosidase Alfa) for healthcare professionals and consumers.
... the total loss of lysosomal glycogen-hydrolyzing enzyme acid -glucosidase (GAA) activity, which results in lysosomal glycogen build up and prominent cardiac and skeletal muscle pathology. higher electrophoretic mobility compared with control iPSC-CMs. Brefeldin A caused disruption of the Golgi in control iPSC-CMs reproduced the higher mobility forms of the LAMPs, suggesting that Pompe iPSC-CMs create LAMPs lacking appropriate glycosylation. Isoelectric focusing studies exposed that Light2 offers a more alkaline pI in Pompe compared with control iPSC-CMs due mainly to hyposialylation. MALDI-TOF-MS analysis of = 100 m for and … TABLE 2 iPS cell collection nomenclature, Paeoniflorin supplier GAA genotype, and phenotype Pompe iPS Cells Have Disease-causing Acid -Glucosidase Mutations Ensuing in Undetectable Mature Protein and Enzymatic Activity The mutations in the gene in the unique Pompe fibroblasts were ...
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In the human adenocarcinoma cell line Caco-2 a substantial amount of a precursor form of the lysosomal enzyme alpha-glucosidase is not segregated into lysosomes, but instead secreted from the apical membrane. In this study we addressed the question whether this process is mediated by mannose 6-phosphate receptors. The subcellular distribution ... read more of the cation-independent mannose 6-phosphate receptor was studied by means of electron microscopic immunocytochemistry. The bulk of label was found in the perinuclear region in electron-lucent and dense vesicles, some of the latter bearing a coat. Receptor-containing dense vesicles were also found throughout the cytoplasm. In the apical part of the cells, label for the receptor was present over the surrounding membrane and the interior vesicles of multivesicular bodies, but not over lysosomes. Label on the plasma membrane was mainly restricted to the apical domain. In contrast to alpha-glucosidase, the secreted forms of the lysosomal enzymes ...
TY - JOUR. T1 - Impaired organization and function of myofilaments in single muscle fibers from a mouse model of Pompe disease. AU - Xu, Sengen. AU - Galperin, Mikhail. AU - Melvin, Gary. AU - Horowits, Robert. AU - Raben, Nina. AU - Plotz, Paul. AU - Yu, Leepo. PY - 2010/5. Y1 - 2010/5. N2 - Pompe disease, a defi-ciency of lysosomal acid α-glucosidase, is a disorder of glycogen, metabolism that can affect infants, children, or adults. In all forms of the disease, there is progressive muscle pathology leading to premature death. The pathology is characterized by accumulation of glycogen in lysosomes, autophagic buildup, and muscle atrophy. The purpose of the present investigation was to determine if myofibrillar dysfunction in Pompe disease contributes to muscle weakness beyond that attributed to atrophy. The study was performed on isolated myofibers dissected from severely affected fast glycolytic muscle in the α-glucosidase knockout mouse model. Psoas muscle fibers were first permeabilized, ...
article{af4d8b27-7220-4534-9530-791b537e1db7, abstract = {,p,Pompe disease is a progressive metabolic myopathy caused by deficiency in lysosomal acid α-glucosidase and results in cellular lysosomal and cytoplasmic glycogen accumulation. A wide spectrum of clinical phenotypes exists from hypotonia and severe cardiac hypertrophy in the first few months of life to a milder form with the onset of symptoms in adulthood. The disease is typically due to severe mutations in GAA gene. In the present study, we described a newborn boy with clinical features of Pompe disease particularly with hypertrophic cardiomyopathy, hypotonia and hepatomegaly. This case was at first misdiagnosed as mitochondrial disorder. Accordingly, we performed a mitochondrial mutational analysis that revealed a novel mutation m.12908T,A in the ND5 gene. Secondary structure analysis of the ND5 protein further supported the deleterious role of the m.12908T,A mutation, as it was found to involve an extended imbalance in its ...
... is an anti-diabetic drug used to treat type 2 diabetes mellitus and, in some countries, prediabetes. It belongs to a class of drugs called alpha-glucosidase inhibitors which also includes miglitol. It mainly influences the level of blood sugar after eating. This decreases the amount of sugar that passes into the blood after a meal and prevents periods of hyperglycemia. Acarbose also has important implications for the ageing process. Acarbose comes as a tablet to take by mouth. It is an inhibitor of alpha glucosidase, an enteric enzyme that releases glucose from larger carbohydrates. Acarbose delays the digestion of carbohydrates (forms of sugar) in the body. This decreases the amount of sugar that passes into the blood after a meal and prevents periods of hyperglycemia (high blood sugar). Acarbose may also be used for purposes other than those listed in this medication guide. Acarbose comes as a tablet to take by mouth. It is usually taken three times a day. It is very important to take ...
The research of medical geneticist Silvia Tortorelli, M.D., Ph.D., and her Mayo colleagues is outlined in, "Moonlighting Newborn Screening Markers: The Incidental Discovery of a Second-Tier Test for Pompe Disease," which appeared as an advanced publication in Genetics in Medicine on November 2.. Through the teams work, a novel biochemical marker was discovered in dried blood spots that not only allows for a faster turnaround time of results but will be more cost-effective than molecular genetic analysis. The new marker was calculated by dividing the creatine/creatinine ratio by the activity of acid A-glucosidase.. According to Dr. Tortorelli, Consultant in the Biochemical Genetics Laboratory, the team used tools created by the Collaborative Laboratory Integrated Reports (CLIR) software to incorporate the new marker into an interpretation algorithm that achieved almost complete segregation between Pompe disease and false-positive cases.. "This new test, once further clinically validated, will ...
Lumizyme (alglucosidase alfa) is an enzyme replacement treatment for Pompe disease developed by Sanofi Genzyme and approved by the FDA.
Hi everybody! My name is really Arthur, but some people call me "Red". Hope you like the case format. These cases are not complete and are not intended to really teach, but are just for fun.....A three month old girl presents with profound muscle weakness, and "Floppyness". On exam, hepatomegaly is noted. The chest X-ray is shown. Note Cardiomegaly. There has been no exposure to honey or home canned goods. .....The child has Pompe disease......An autosomal recessively inherited lysosomal storage disease. The deficient enzyme is alpha glucosidase, which is needed for glycogen breakdown.......The disease was first characterized by Johann Pompe in 1932. Pompe was danish, and was executed in 1945 by Nazi Germany for espionage.....The disease is also featured prominantly in the upcoming film Extraordinary Measures, which I believe is a statement against big pharama, and Bristol Myers Squib in particular. ......Besides Botulism (alluded to in the pertinent negatives of the case), a differential would ...
All Pompe disease patients have symptoms that affect their hearts, so its important to maintain healthy habits to ensure good cardiac health.
Evidence-Based Complementary and Alternative Medicine (eCAM) is an international peer-reviewed, Open Access journal that seeks to understand the sources and to encourage rigorous research in this new, yet ancient world of complementary and alternative medicine.
Evidence-Based Complementary and Alternative Medicine (eCAM) is an international peer-reviewed, Open Access journal that seeks to understand the sources and to encourage rigorous research in this new, yet ancient world of complementary and alternative medicine.
Acarbose (INN) is an anti-diabetic drug used to treat diabetes mellitus type 2 and, in some countries, prediabetes. It is a generic sold in Europe and China as Glucobay (Bayer AG), in North America as Precose (Bayer Pharmaceuticals), and in Canada as Prandase (Bayer AG). It is cheap and popular in China, but not in the U.S. One physician explains the use in the U.S. is limited because it is not potent enough to justify the side effects of diarrhea and flatulence. However, a recent large study concludes "acarbose is effective, safe and well tolerated in a large cohort of Asian patients with type 2 diabetes." A possible explanation for the differing opinions is an observation that acarbose is significantly more effective in patients eating a relatively high carbohydrate Eastern diet. It is a starch blocker, and inhibits alpha glucosidase, an intestinal enzyme that releases glucose from larger carbohydrates. It is composed of an acarviosin moiety with a maltose at the reducing terminus. Acarbose ...
The information contained in the Truven Health Analytics products is intended as an educational aid only. It is not intended as medical advice for individual conditions or treatment. It is not a substitute for a medical exam, nor does it replace the need for services provided by medical professionals. Talk to your doctor, nurse or pharmacist before taking any prescription or over the counter drugs (including any herbal medicines or supplements) or following any treatment or regimen. Only your doctor, nurse or pharmacist can provide you with advice on what is safe and effective for you.. The use of the Truven Health Analytics products is at your sole risk. These products are provided "AS IS" and "as available" for use, without warranties of any kind, either express or implied. Truven Health Analytics makes no representation or warranty as to the accuracy, reliability, timeliness, usefulness or completeness of any of the information contained in the products. Additionally, TRUVEN HEALTH ANALYTICS ...
It is very important that your doctor check the progress of you or your child at regular visits to make sure that this medicine is working properly. Blood tests may be needed to check for unwanted effects. This medicine may cause chest pain, fever, chills, itching, hives or a rash, a fast heartbeat, flushing of the face, dizziness, fainting, or lightheadedness, trouble breathing, or swelling of the face, tongue, and throat within a few hours after it is given. Check with your doctor or nurse right away if you or your child have any of these symptoms. ...
BioAssay record AID 696532 submitted by ChEMBL: Inhibition of rat small intestinal maltase after 30 mins by glucose-oxidase method.
This trial is investigating the effects of miglitol [Sanwa Kagaku Kenkyusho] versus acarbose versus sitagliptin versus no treatment on glucose metabolism and
Both muscle ultrasound and electromyogram were normal. Because of progressive muscular weakness, initially thought to be attributable to polymyositis, a biopsy of the quadriceps muscle was taken. The histologic picture showed predominant lysosomal storage of glycogen, which is characteristic of Pompe disease. This diagnosis was confirmed by measurement of acid α-glucosidase, which showed enzyme activity below detection level in both leukocytes and cultured skin fibroblasts using glycogen (respectively) glycogen and 4-methylumbelliferyl α-d-glucopyranoside as substrate.5. DNA analysis was performed to establish the patients α-glucosidase genotype. DNA analysis in leukocytes from this girl did not show any of the 3 most common mutations in the Netherlands (IVS1 [−13 G], 525 del T, and del exon 18 allele).6,7 Full-length cDNA sequence analysis by reverse transcriptase-polymerase chain reaction7 led to detection of a single, apparently homozygous, A to T transversion at position 875 in exon 5, ...
cDNA encoding Schizosaccharomyces pombe a-glucosidase was cloned, and expressed in Saccharomyces cerevisiae. The deduced amino acid sequence categorized under the α-glucosidase family II showed a high homology to those of a-glucosidase from molds, plants and mammals. By site direct mutagenesis, Asp481, G1u484, and Asp647 residues were confirmed to be essential in the catalytic reaction. The carboxyl group (-COON) of the Asp647 residue was for the first time pointed out to be the candidate of proton donor in the a-glucosidase of family II. The carboxylate group (-COO-) of the Asp481 residue was assumed to be the secondary carboxylate group, which stabilize the oxocarbenium ion through electrostatic interaction, and the Asp481 was considered to be modified by the chemical modification with conduritol B epoxide. The role of the G1u484 residue, which was the third residue, was presumed to be to fix the reaction intermediate of substrates.. ...
Pompe disease is inherited in an autosomal recessive manner, meaning that an affected individual must inherit an abnormal allele from both parents. Thus, t
Research Report on Global Pompe Disease Drugs Sales Market Report 2017. The Report includes market price, demand, trends, size, Share, Growth, Forecast, Analysis & Overview.
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
Pompe disease is a rare neuromuscular disorder caused by deficiency of acid α-glucosidase. Treatment with recombinant human α-glucosidase recently received marketing approval based on prolonged survival of affected infants. The current open-label study was performed to evaluate the response in older children (age 5.9-15.2 years). The five patients that we studied had limb-girdle muscle weakness and three of them also had decreased pulmonary function in upright and supine position. They received 20-mg/kg recombinant human α-glucosidase every two weeks over a 3-year period. No infusion-associated reactions were observed. Pulmonary function remained stable (n= 4) or improved slightly (n= 1). Muscle strength increased. Only one patient approached the normal range. Patients obtained higher scores on the Quick Motor Function Test. None of the patients deteriorated. Follow-up data of two unmatched historical cohorts of adults and children with Pompe disease were used for comparison. They showed an ...
Complete information for GAA gene (Protein Coding), Glucosidase Alpha, Acid, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Abstract The inhibitory activity of six groups of flavonoids against yeast and rat small intestinal alpha-glucosidases and porcine pancreatic alpha-amylase was compared, and chemic..
N-Glycans are modified as part of a quality control mechanism during glycoprotein folding in the endoplasmic reticulum (ER). Glucosidase II (GII) plays a critical role by generating monoglucosylated glycans that are recognized by lectin chaperones, calnexin and calreticulin. To understand how the hydrolytic activity of GIIα is enhanced by the mannose 6-phosphate receptor (MPR) homology domain (MRH domain) of its β subunit, we now report a 1.6 Å resolution crystal structure of the MRH domain of GIIβ bound to mannose. A comparison of ligand-bound and unbound structures reveals no major difference in their overall fold, but rather a repositioning of side chains throughout the binding pocket, including Y372. Mutation of Y372 inhibits GII activity, demonstrating an important role for Y372 in regulating GII activity. Comparison of the MRH domains of GIIβ, MPRs, and the ER lectin OS-9 identified conserved residues that are critical for the structural integrity and architecture of the carbohydrate ...
β-Glucosidases (3.2.1.21) are found in all domains of living organisms, where they play essential roles in the removal of nonreducing terminal glucosyl residues from saccharides and glycosides. β-Glucosidases function in glycolipid and exogenous glycoside metabolism in animals, defense, cell wall lignification, cell wall β-glucan turnover, phytohormone activation, and release of aromatic compounds in plants, and biomass conversion in microorganisms. These functions lead to many agricultural and industrial applications. β-Glucosidases have been classified into glycoside hydrolase (GH) families GH1, GH3, GH5, GH9, and GH30, based on their amino acid sequences, while other β-glucosidases remain to be classified. The GH1, GH5, and GH30 β-glucosidases fall in GH Clan A, which consists of proteins with (β/α)8-barrel structures. In contrast, the active site of GH3 enzymes comprises two domains, while GH9 enzymes have (α/α)6 barrel structures. The mechanism by which GH1 enzymes recognize and ...
BioAssay record AID 769002 submitted by ChEMBL: Inhibition of Saccharomyces sp. alpha-glucosidase using p-nitrophenyl a-D-glucopyranoside as substrate by spectrophotometric analysis.
Mazzaferro E M, Greco D S, Turner A S & Fettman M J (2003)Treatment of feline diabetes mellitus using an alpha-glucosidase inhibitor and a low-carbohydrate diet. J Feline Med Surg5(3), 183-189 PubMed ...
PURPOSE: Glucosidase II plays a major role in regulating the post-translational modification of N-linked glycoproteins. Previously, we found that the beta subunit of glucosidase II (GluIIβ) levels are significantly increased in lung carcinoma tissues, indicating a potential role in lung tumorigenesis. Here, we investigated the role of GluIIβ in the regulation of autophagy and apoptosis in lung carcinoma- and immortalized human bronchial epithelial-derived cells. METHODS: A selective glucosidase II inhibitor, bromoconduritol, was used to inhibit GluII enzyme activity and a siRNA-based technology was used to suppress the expression of the GluIIβ encoding gene PRKCSH in lung carcinoma cells differing in p53 status ...
Using N-butyl-deoxynojirimycin (NB-DNJ), a competitive inhibitor of the ER alpha-glucosidases, we have recently addressed the impact of this inhibition on both assembly and infectivity of the virions released from infected hepatoma cells. Southern and Western blotting analysis of HBV secreted from drug-treated cells showed that the envelope glycoprotein composition was severely altered, resulting in a significant reduction of HBV infectivity (80% compared to controls ...
RESULTS After the study treatment, HbA1c and plasma glucose in the patients who had received voglibose were comparable to those of patients in the control group. M-value was lower in the patients treated with voglibose than in the control subjects (5.7 ± 0.9 vs. 9.8 ± 1.2, P , 0.05). 1,5-AG was higher in the patients treated with voglibose than in the control subjects (12.2 ± 1.0 vs. 8.2 ± 0.7 μg/ml, P , 0.01). A statistically significant decrease in AUCinsuiin occurred after treatment with voglibose (2,223.5 ± 390.6 to 1,546.7 ± 303.4 pmol · l−1 · h, P , 0.05), but no change occurred in the control group (2,364.5 ± 315.4 to 2,464.2 ± 269.3 pmol · l−1 · h, P = 0.60). Insulin sensitivity (KITT) was improved to a statistically significant level in both the patients treated with voglibose and the patients in the control group. KITT in the patients after voglibose treatment was comparable to that of the control group (3.18 ± 0.30 vs. 3.21 ± 0.23%/min, P = 0.94).. ...
Since enzymes are prone to degradation in blood, the addition of a pharmacological chaperone AT2221 should, theoretically, improve efficacy.
Cranbury, NJ, DECEMBER 14, 2006 - Amicus Therapeutics, a biopharmaceutical company developing small molecule, orally-administered pharmacological chaperones for
Alpha-glucosidase is a glucosidase located in the brush border of the small intestine that acts upon 1,4-alpha bonds. This is in contrast to beta-glucosidase. Alpha-gluco
Boc Sciences offers cas 73285-50-4 1-Deoxynojirimycin HCl in bulk,please inquire us to get a quote for 73285-50-4 1-Deoxynojirimycin HCl.
SciShow explores the unexpected. Seven days a week, Hank Green, Michael Aranda, and Olivia Gordon delve into the scientific subjects that defy our expectations and make us even more curious ...
(KudoZ) French to English translation of pompe de soutirage sous vide/recette [production process - Chemistry; Chem Sci/Eng (Tech/Engineering)].
Miglitol is a medicine available in a number of countries worldwide. A list of US medications equivalent to Miglitol is available on the Drugs.com website.
α-グルコシダーゼ阻害薬(α-gi)の作用機序 . 速攻型インスリン分泌促進薬は食後高血糖を改善する薬ですが、同じように .... ...
Berechnung des absoluten Risiko in %, innerhalb von 10 Jahren ein tödliches Koronaereignis (z.B. Herzinfarkt) oder einen nicht-tödlichen Herzinfarkt zu erleiden.. ...
One normal and two carrier calves, and two calves affected by generalized glycogenosis type II were given multiple transplants of normal bovine amnion inserted below the external oblique abdominal muscle in the flank. The interval between transplants was approximately 5 months. The amniotic tissue was not acutely rejected but a host versus graft reaction did occur. The level of acid alpha-glucosidase activity in the amniotic tissue fell rapidly but was still present 2 months after transplantation. Enzyme levels in blood or other tissues did not rise. Excess glycogen deposition and muscle damage occurred in the affected calves and appeared to progress at a rate similar to that in untreated affected animals. One of the affected animals died aged 16 months, which was the same age as the longest surviving non-treated animal in our herd. The other treated animal died aged 24 months.. ...
As a continuous searching for anti-diabetic(type II) substances, seven mucilage polysaccharides from selected plants were studied as follow: aerial parts of Basella alba Linn., fruits of Hibiscus esculentus Linn., leaves of Litsea glutinosa (Lour.) C.B. Robinson, seeds of Ocimum canum Sims., seeds of Plantago ovata Forssk., fruits of Scaphium scaphigerum G. Don. and seeds of Trigonella foenum-graecum Linn. The bioactive properties for entrapping glucose, inhibiting enzyme alpha-glucosidase and free radical scavenger were in vitro studied compared to glucomannan. The physical characteristics for water holding capacity and viscosity were determined. The chemical characteristics were assayed for monosaccharide composition using methanolysis, TMSderivatization and gas chromatography. O. canum mucilage superiorly entrapped glucose compared to glucomannan. This activity was relevant to its highly viscous gelation. S. scaphigerum showed another property of alphaglucosidase inhibition. S. scaphigerum mucilage
Glycogenosis type II is an inherited lysosomal storage disorder caused by acid α-glucosidase deficiency. The disorder is inbred in Brahman cattle, and the incidence of carriers in Australian herds averages 15%. Affected animals are lethargic and die typically in the eighth or ninth month after birth, A complete lack of acid α-glucosidase synthesis was demonstrated in cultured fibroblasts and muscle tissue of affected animals. Moreover, the tissue was found to be devoid of acid α-glucosidase mRNA. Gross abnormalities of the acid α-glucosidase gene itself were not detected by Southern blot analysis. These results suggest Brahman glycogenosis type II to be caused by a point mutation or a micro deletion/insertion in the acid α-glucosidase gene ...
The U.S. Food and Drug Administration (FDA) has approved U.S. sales of the enzyme-replacement drug Lumizyme, the first treatment in the U.S. specifically for late-onset Pompe disease.. The decision was reported via press release by the drugs manufacturer, Genzyme of Cambridge, Mass., and comes three weeks ahead of the scheduled decision date of June 17, 2010. (For more on Lumizymes development, see Lumizyme on the Horizon.). Lumizyme (alglucosidase alfa) is a laboratory-developed enzyme used to replace the acid maltase enzyme deficient in people with Pompe disease ages 8 and older.. Genzyme received FDA approval in 2006 to market Myozyme, the first-ever U.S. treatment for infants and children with Pompe disease. Due to limited production capacity, Myozyme has been reserved for children 17 and younger.. MDA-supported basic research played a role in the development of these enzyme-replacement drugs.. Meaning for people with Pompe disease. Severely affected adults who have been receiving ...
Acid maltase deficiency (AMD), also known as Pompe disease, is a genetically inherited disease that affects muscle function. Inherited diseases are passed on from parents to a child. Patients with AMD have a defect, or mutation, in a gene that functions in muscles, called the acid alpha-glucosidase (GAA) gene. This genetic mutation causes a substance called glycogen to build up in the muscles of patients with AMD. Glycogen is a form of starch that is used to store short-term energy.
More than 200 mutations in the GAA gene have been identified in people with Pompe disease. Many of these mutations change one of the protein building blocks (amino acids) used to make acid alpha-glucosidase. Other mutations insert or delete genetic material in the GAA gene. Mutations in this gene significantly reduce the activity of acid alpha-glucosidase, preventing the enzyme from breaking down glycogen effectively. As a result, this complex sugar can build up to toxic levels in lysosomes. The abnormal buildup of glycogen damages organs and tissues throughout the body, particularly the muscles, leading to progressive muscle weakness, heart problems, and the other features of Pompe disease. ...
TY - JOUR. T1 - Adult acid maltase deficiency. Abnormalities in fibroblasts cultured from patients.. AU - Angelini, C.. AU - Engel, Andrew G. AU - Titus, J. L.. PY - 1972/11/9. Y1 - 1972/11/9. UR - http://www.scopus.com/inward/record.url?scp=0015499592&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=0015499592&partnerID=8YFLogxK. M3 - Article. VL - 287. SP - 948. EP - 951. JO - New England Journal of Medicine. JF - New England Journal of Medicine. SN - 1533-4406. IS - 19. ER - ...
Several studies have demonstrated that the diaphragm can be successfully targeted for gene transfer during the fetal period, by injecting gene transfer vectors directly into the uterine cavity. In a murine model of Pompe disease (Glycogen storage disease type II) which is defined by a lack of the enzyme acid a-glucosidase (GAA), Rucker et al (2004) injected adeno-associated virus vectors (AAV1 and AAV2) into the fetal peritoneal cavity on day 15 of gestation. These authors found that several weeks after birth, GAA levels in the diaphragm were significantly increased, and this was associated with improvements in histopathology and the contractile function of the diaphragm up to 6 months of age. Using fetal mice of the same gestational age, Gregory et al (2004) showed high-level LacZ gene transfer to the diaphragm by equine infectious anemia virus (EIAV) lentivirus vectors pseudo-typed with VSV-G. By combining intrapleural and intraperitoneal injections of EIAV in the fetus, not only the diaphragm ...
Recently, the U.S. Discretionary Advisory Committee on Heritable Disorders in Newborns and Children recommended that Pompe disease be added to the Recommended Uniform Screening Panel. - Newborn Screening and Pompe Disease Update - Neuromuscular Diseases at BellaOnline
Doctors announced that they are able to treat a lethal genetic disorder called Pompes disease by giving the patients an intravenous supply of the missing enzyme alpha-glucosidase, which their bodies are unable to produce. The researchers, from Sophia Childrens Hospital and Erasmus University, both in Rotterdam, presented their work at the annual meeting of the American Society of Human Genetics in Philadelphia.. Pompes disease is caused by a buildup of large quantities of glycogen in the heart and muscle cells that progressively breaks down the muscle until there is little healthy tissue remaining. In a short video segment during the presentation, physician researcher Ans van der Ploeg showed babies with the infantile form of the disease; their bodies were like rag dolls and they were completely unable to raise their heads or legs. The infants usually die of respiratory and cardiac failure within the first year, without ever being able to roll over or sit up. Onset of Pompes disease during ...
Enhanced efficacy of enzyme replacement therapy in Pompe disease through mannose-6-phosphate receptor expression in skeletal muscle.s profile, publications, research topics, and co-authors
Observational clinical study in juvenile-adult glycogenosis type 2 patients undergoing enzyme replacement therapy for up to 4 years.Authors: Angelini C, Semplicini C, Ravaglia S, Bembi B, Servidei S, Pegoraro E, Moggio M, Filosto M, Sette E, Crescimanno G, Tonin P, Parini R, Morandi L, Marrosu G, Greco G, Musumeci O, Di Iorio G, Siciliano G, Donati MA, Carubbi F, Ermani M, Mongini T, Toscano A, Italian GSDII Group ...
An autosomal recessively inherited glycogen storage disease caused by glucan 1,4-Alpa-Glucosidase Definciency. Large amounts of glycogen accumulate in the lysomes of skeletal muscle ( muscle, skeletal); heart; liver; spinal cord; and brain.
THONG, WONG KUM (2015) A generic assay for whole-genome amplification and deep sequencing of enterovirus A71. Journal of Virological Methods. pp. 30-36. THONG, WONG KUM (2015) Enterovirus 71 neuropathogenesis and its impact on other neurotropic enteroviruses. Brain Pathology, 25. pp. 614-624. THONG, WONG KUM (2014) Late-onset glycogen storage disease Type II (Pompes Disease) with a novel mutation: A Malaysian perspective. Case reports in Neurological Medicine, 2014. doi. 10.115/2014/926510. THONG, WONG KUM (2013) Protection against henipavirus infection using recombinant AAV vector vaccines. pp. 469-478. THONG, WONG KUM (2013) Transgenic mouse model for the study of enterovirus 71 neuropathogenesis. Proceedings of the National Academy of Sciences of the United States of America, 110. pp. 14753-14758. THONG, WONG KUM (2012) Clinical and pathological manifestations of human Henipavirus infection. THONG, WONG KUM (2012) Immunization with recombinant enterovirus 71 viral capsid protein 1 fragment ...
Congenital sucrase-isomaltase deficiency (CSID) is an intestinal disease caused by mutations of the SI gene (1-3). The membrane-bound complex (SI) has isomaltase and sucrase activity on the N- and C-terminal subunits, respectively. Both subunits also contribute maltase activities (4), which together with the 2 maltase activities of the maltase-glucoamylase (MGAM) complex digest starch to free glucose. Patients with CSID have reductions of activity or total absence of 1 or both subunits (5-7). In addition to the maldigestion of sucrose, because patients with CSID also have reduced maltase activity, they have maldigestion of starchy foods and may contribute to symptoms of dyspepsia and recurrent abdominal pain (5).. Starchy foods are common carbohydrate sources for human populations. To digest starch to glucose, 6 enzymes, including 2 α-amylases, 2 terminal subunits each of SI and MGAM, are involved. Because the structure of starch is highly correlated to the susceptibility of α-amylase, this ...
K12316 GAA; lysosomal alpha-glucosidase [EC:3.2.1.20] K12316 GAA; lysosomal alpha-glucosidase [EC:3.2.1.20] K00963 UGP2; UTP--glucose-1-phosphate uridylyltransferase [EC:2.7.7.9] K00963 UGP2; UTP--glucose-1-phosphate uridylyltransferase [EC:2.7.7.9] K05349 bglX; beta-glucosidase [EC:3.2.1.21] K00694 bcsA; cellulose synthase (UDP-forming) [EC:2.4.1.12] K01179 E3.2.1.4; endoglucanase [EC:3.2.1.4] K01179 E3.2.1.4; endoglucanase [EC:3.2.1.4] K01179 E3.2.1.4; endoglucanase [EC:3.2.1.4] K01179 E3.2.1.4; endoglucanase [EC:3.2.1.4] K01179 E3.2.1.4; endoglucanase [EC:3.2.1.4] K01179 E3.2.1.4; endoglucanase [EC:3.2.1.4] K01179 E3.2.1.4; endoglucanase [EC:3.2.1.4] K01179 E3.2.1.4; endoglucanase [EC:3.2.1.4] K01225 CBH1; cellulose 1,4-beta-cellobiosidase [EC:3.2.1.91] K01225 CBH1; cellulose 1,4-beta-cellobiosidase [EC:3.2.1.91] K18447 NUDX14; ADP-sugar diphosphatase [EC:3.6.1.21] K00693 GYS; glycogen synthase [EC:2.4.1.11] K00700 GBE1; 1,4-alpha-glucan branching enzyme [EC:2.4.1.18] K00688 PYG; glycogen ...
During constant work-rate exercise above the lactic acidosis threshold, oxygen consumption fails to plateau by 3 minutes, but continues to rise slowly. This slow component correlates closely with the rise in lactate in normal subjects. We investigated if oxygen consumption during constant work-rate exercise could rise after 3 minutes in the absence of a rise in lactate. We studied five patients with McArdles disease, one patient with phosphofructokinase deficiency and six normal subjects. Subjects performed two 6-minute duration constant work-rate exercise tests at 40 and 70% of peak oxygen consumption. During low-intensity exercise, oxygen consumption reached steady state by 3 minutes in both groups. Lactate rose slightly in control subjects but not in patients. During high-intensity exercise, oxygen consumption rose from the third to the sixth minute by 144 (21-607) ml/minute (median and range) in control subjects and by 142 (73-306) ml/minute in patients (p = not significant, Mann-Whitney U ...
A mammalian N-acetylglucosamine (GlcNAc) transferase I (GnT I)-independent fucosylation pathway is revealed by the use of matrix-assisted laser desorption/ionization (MALDI) and negative-ion nano-electrospray ionization (ESI) mass spectrometry of N-linked glycans from natively folded recombinant glycoproteins, expressed in both human embryonic kidney (HEK) 293S and Chinese hamster ovary (CHO) Lec3.2.8.1 cells deficient in GnT I activity. The biosynthesis of core fucosylated Man5GlcNAc2 glycans was enhanced in CHO Lec3.2.8.1 cells by the alpha-glucosidase inhibitor, N-butyldeoxynojirimycin (NB-DNJ), leading to the increase in core fucosylated Man5GlcNAc2 glycans and the biosynthesis of a novel core fucosylated monoglucosylated oligomannose glycan, Glc1Man7GlcNAc2Fuc. Furthermore, no fucosylated Man9GlcNAc2 glycans were detected following inhibition of alpha-mannosidase I with kifunensine. Thus, core fucosylation is prevented by the presence of terminal alpha1-2 mannoses on the 6-antennae but not ...
Glycogen storage disease type Ia (GSDIa) is an inherited disorder of glucose metabolism, due to the selective deficiency of the hepatic enzyme glucose-6-phosphatase. Clinical manifestations include severe hypoglycaemia three to four hours post-prandially, increased production of lactic acid, triglycerides and uric acid, hepatic glycogen storage disease with development of multiple adenomas and kidney disease with proteinuria. Liver transplantation is frequently performed in order to achieve metabolic control and when malignant transformation of adenomas is suspected. Long term outcome following transplantation is good, but immunosuppressive therapy can worsen the progression of associated kidney disease. Hepatocyte transplantation could be considered as a less invasive procedure in such patients. Our experience with hepatocyte transplantation in a 47 year-old woman affected by glycogen storage disease type Ia and suffering of severe fasting hypoglycaemia indicates that the procedure can ...

Binding parameters and thermodynamics of the interaction of imino sugars with a recombinant human acid alpha-glucosidase ...Binding parameters and thermodynamics of the interaction of imino sugars with a recombinant human acid alpha-glucosidase ...

We examined the inhibitory and binding effects of four imino sugars on a recombinant human acid alpha-glucosidase, ... Binding parameters and thermodynamics of the interaction of imino sugars with a recombinant human acid alpha-glucosidase ( ... which act as potential inhibitors of acid alpha-glucosidases in vitro, to improve the stability and/or transportation of mutant ... acid alpha-glucosidases in cells was studied and attracted interest. However, the mechanism underlying the molecular ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/18328816

Acid alpha-glucosidase - WikipediaAcid alpha-glucosidase - Wikipedia

alpha-1,4-glucosidase activity. • alpha-glucosidase activity. Cellular component. • membrane. • lysosomal membrane. • lysosomal ... Acid alpha-glucosidase, also called α-1,4-glucosidase[5] and acid maltase,[6] is an enzyme (EC 3.2.1.20) that helps to break ... maltose alpha-glucosidase activity. • catalytic activity. • hydrolase activity. • carbohydrate binding. • isomaltase. • ... This gene encodes lysosomal alpha-glucosidase, which is essential for the degradation of glycogen to glucose in lysosomes. ...
more infohttps://en.wikipedia.org/wiki/Acid_alpha-glucosidase

Alpha-glucosidase - WikipediaAlpha-glucosidase - Wikipedia

... alpha-D-glucosidase, alpha-glucoside hydrolase, alpha-1,4-glucosidase, alpha-D-glucoside glucohydrolase) is a glucosidase ... Alglucosidase alfa Alpha-glucosidase inhibitor alpha-Glucosidases at the US National Library of Medicine Medical Subject ... Diabetes: Acarbose, an alpha-glucosidase inhibitor, competitively and reversibly inhibits alpha-glucosidase in the intestines. ... Other glucosidases include: Cellulase Beta-glucosidase Debranching enzyme Alpha-glucosidase hydrolyzes terminal non-reducing (1 ...
more infohttps://en.wikipedia.org/wiki/Alpha-glucosidase

alpha glucosidase - Everything2.comalpha glucosidase - Everything2.com

4-linked alpha-D-glucose residue from the nonreducing end of a long chain (or polymer) of such residues, making an al... ... An enzyme which removes the last 1,4-linked alpha-D-glucose residue from the nonreducing end of a long chain (or polymer) of ... such residues, making an alpha-D-glucose molecule out of it in the process. ...
more infohttps://everything2.com/title/alpha+glucosidase

Sucrose alpha-glucosidase - WikipediaSucrose alpha-glucosidase - Wikipedia

Sucrose alpha-glucosidase (EC 3.2.1.48, sucrose alpha-glucohydrolase, sucrase, sucrase-isomaltase, sucrose.alpha.- ... Sucrose alpha-glucosidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... This enzyme catalyses the following chemical reaction Hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action ... glucohydrolase, intestinal sucrase, sucrase(invertase)) is an enzyme with systematic name sucrose-alpha-D-glucohydrolase. ...
more infohttps://en.wikipedia.org/wiki/Sucrose_alpha-glucosidase

Alpha-glucosidase Inhibitors | HowStuffWorksAlpha-glucosidase Inhibitors | HowStuffWorks

Alpha-glucosidase Inhibitors are great treatment options for those with high glucose levels. Get facts about Alpha-glucosidase ... Possible Side Effects of Alpha-Glucosidase Inhibitors. You may have these side effects when you take an alpha-glucosidase ... Possible Drug Interactions With Alpha-Glucosidase Inhibitors. Before you take an alpha-glucosidase inhibitor, tell all your ... People who have a history of stomach or bowel trouble should not use alpha-glucosidase inhibitors. Not everyone who takes alpha ...
more infohttps://health.howstuffworks.com/diseases-conditions/diabetes/alpha-glucosidase-inhibitors.htm

Alpha-glucosidase inhibitors: MedlinePlus Medical Encyclopedia ImageAlpha-glucosidase inhibitors: MedlinePlus Medical Encyclopedia Image

Alpha-glucosidase inhibitors (such as acarbose) decrease the absorption of carbohydrates from the digestive tract, thereby ... Alpha-glucosidase inhibitors (such as acarbose) decrease the absorption of carbohydrates from the digestive tract, thereby ...
more infohttps://medlineplus.gov/ency/imagepages/19826.htm

Alpha-Glucosidase InhibitorsAlpha-Glucosidase Inhibitors

The alpha-glucosidase inhibitors available today (with brand names in parenthesis) are: acarbose (Precose) miglitol (Glyset) An ... Alpha-glucosidase inhibitors (AGIs) are a class of drugs used to treat type 2 diabetes. The key benefit of AGIs is that they do ... Alpha-Glucosidase Inhibitors. Alpha-glucosidase inhibitors (AGIs) are a class of drugs used to treat type 2 diabetes. The key ...
more infohttps://www.diabetesdaily.com/learn-about-diabetes/overview-of-diabetes-drugs/alpha-glucosidase-inhibitors/

alpha Glucosidases - Medical Dictionary online-medical-dictionary.orgalpha Glucosidases - Medical Dictionary online-medical-dictionary.org

alpha Glucosidases. Enzymes that catalyze the exohydrolysis of 1,4-alpha-glucosidic linkages with release of alpha-Glucose. ... Deficiency of alpha-1,4-Glucosidase may cause Glycogen Storage Disease Type II. ...
more infohttp://www.online-medical-dictionary.org/definitions-a/alpha-glucosidases.html

Anti-alpha Glucosidase II/ganab antibody (ab96757)Anti-alpha Glucosidase II/ganab antibody (ab96757)

Rabbit polyclonal alpha Glucosidase II antibody validated for Western Blot, IHC, ICC/IF & tested in Human & Mouse. Immunogen ... Anti-alpha Glucosidase II antibody. See all alpha Glucosidase II primary antibodies. ... Anti-alpha Glucosidase II antibody (ab96757) at 1/1000 dilution + NIH-3T3 whole cell lysate at 30 µg. Predicted band size: 107 ... All lanes : Anti-alpha Glucosidase II antibody (ab96757) at 1/1000 dilution. Lane 1 : 293T whole cell lysate. Lane 2 : A431 ...
more infohttps://www.abcam.com/alpha-glucosidase-ii-antibody-ab96757.html

alpha Glucosidase 2 Lysates: Novus Biologicalsalpha Glucosidase 2 Lysates: Novus Biologicals

Browse our alpha Glucosidase 2 Lysate catalog backed by our Guarantee+. ... Alternate Names for alpha Glucosidase 2 Lysates. alpha Glucosidase 2 lysate, GANAB lysate, Alpha-glucosidase 2 lysate, EC 3.2.1 ... KIAA0088alpha glucosidase II alpha subunit lysate, neutral alpha-glucosidase AB lysate. 2 Results for "alpha-glucosidase-2" in ... We offer alpha Glucosidase 2 Lysates for use in common research applications: Western Blot. Each alpha Glucosidase 2 Lysate is ...
more infohttps://www.novusbio.com/lysates/alpha-glucosidase-2?related_diseases=Multiple%20Sclerosis

alpha Glucosidase 2 Lysates: Novus Biologicalsalpha Glucosidase 2 Lysates: Novus Biologicals

Browse our alpha Glucosidase 2 Lysate catalog backed by our Guarantee+. ... Alternate Names for alpha Glucosidase 2 Lysates. alpha Glucosidase 2 lysate, GANAB lysate, Alpha-glucosidase 2 lysate, EC 3.2.1 ... KIAA0088alpha glucosidase II alpha subunit lysate, neutral alpha-glucosidase AB lysate. 2 Results for "alpha-glucosidase-2" in ... We offer alpha Glucosidase 2 Lysates for use in common research applications: Western Blot. Each alpha Glucosidase 2 Lysate is ...
more infohttps://www.novusbio.com/lysates/alpha-glucosidase-2

Go to Alpha-Glucosidase Inhibitors.Go to Alpha-Glucosidase Inhibitors.

The use of alpha-glucosidase inhibitors results in a lower, delayed rise in blood glucose after a meal when taken with the ... Alpha-Glucosidase Inhibitors. By Mark Marino , Published September 4, 2009. , Updated December 22, 2014. ... The use of alpha-glucosidase inhibitors results in a lower, delayed rise in blood glucose after a meal. Since these drugs lower ... Alpha-glucosidase is an intestinal enzyme that breaks down a variety of carbohydrates, but two of the more important ones are ...
more infohttps://www.diabetesselfmanagement.com/blog/alpha-glucosidase-inhibitors/

5HJR: Murine endoplasmic reticulum alpha-glucosidase II with bound covalent intermediate5HJR: Murine endoplasmic reticulum alpha-glucosidase II with bound covalent intermediate

Glucosidase 2 subunit betaNeutral alpha-glucosidase AB1,2-ETHANEDIOL5-FLUORO-BETA-D-GLUCOPYRANOSEALPHA-D-MANNOSECALCIUM IOND ...
more infohttps://www.ncbi.nlm.nih.gov/Structure/pdb/5HJR

Alpha Glucosidase Inhibitors - Suitability, Benefits & Side EffectsAlpha Glucosidase Inhibitors - Suitability, Benefits & Side Effects

Alpha-glucosidase inhibitors, sometimes referred to as starch blockers, are anti-diabetic medicines that help to reduce post ... Who are alpha-glucosidase inhibitors suitable for?. Alpha-glucosidase inhibitors are suitable for people with type 2 diabetes ... Alpha-glucosidase inhibitors slow down the digestion of carbohydrates Alpha-glucosidase inhibitors (AGIs), sometimes referred ...
more infohttps://www.diabetes.co.uk/diabetes-medication/alpha-glucosidase-inhibitor.html

Inhibitory Properties of Aqueous Ethanol Extracts of Propolis on Alpha-GlucosidaseInhibitory Properties of Aqueous Ethanol Extracts of Propolis on Alpha-Glucosidase

F. Ye, Z. Shen, and M. Xie, "Alpha-glucosidase inhibition from a Chinese medical herb (Ramulus mori) in normal and diabetic ... Inhibitory Properties of Aqueous Ethanol Extracts of Propolis on Alpha-Glucosidase. Hongcheng Zhang,1,2 Guangxin Wang,1 Trust ... L. J. Shai, P. Masoko, M. P. Mokgotho et al., "Yeast alpha glucosidase inhibitory and antioxidant activities of six medicinal ... "Effective control of postprandial glucose level through inhibition of intestinal alpha glucosidase by Cymbopogon martinii (Roxb ...
more infohttps://www.hindawi.com/journals/ecam/2015/587383/ref/

Inhibitory Properties of Aqueous Ethanol Extracts of Propolis on Alpha-GlucosidaseInhibitory Properties of Aqueous Ethanol Extracts of Propolis on Alpha-Glucosidase

Inhibitory Activity Assay for Bakers Yeast Alpha-Glucosidase. Alpha-glucosidase inhibitory effect of propolis extracts was ... glucosidase.. In the present study, we assessed inhibitory effects of aqueous ethanol extracts of propolis on alpha-glucosidase ... glucosidase was tested according to procedure described previously [4] with minor modifications. Alpha-glucosidase activity was ... Inhibition of Aqueous Ethanol Extracts of Propolis against Alpha-Glucosidase. The -glucosidase inhibitory activity of various ...
more infohttps://www.hindawi.com/journals/ecam/2015/587383/

Go to Alpha-Glucosidase Inhibitors.Go to Alpha-Glucosidase Inhibitors.

Alpha-glucosidase inhibitors, a class of drugs also known as starch blockers, function by slowing the absorption of certain ... A second alpha-glucosidase inhibitor, miglitol (Glyset) became available in 1999. They may be used by people with either Type 1 ... However, while alpha-glucosidase inhibitors themselves do not cause low blood glucose, when they are used in combination with ... The first alpha-glucosidase inhibitor to become available in the United States was acarbose (Precose), which was approved by ...
more infohttps://www.diabetesselfmanagement.com/diabetes-resources/definitions/alpha-glucosidase-inhibitors/

alpha-Glucosidase ELISA & Assay Kitsalpha-Glucosidase ELISA & Assay Kits

Compare and order alpha-Glucosidase ELISA Kits. View citations, images, detection ranges, sensitivity, prices and more. ... glucosidase, alpha; acid (Pompe disease, glycogen storage disease type II) , lysosomal alpha-glucosidase , CG11909-PA , alpha- ... Images for product: alpha-Glucosidase (AGLU) ELISA Kit Diagramm of the ELISA kit to detect Rat a-Gluwith the optical density on ... Images for product: alpha-Glucosidase (AGLU) ELISA Kit Diagramm of the ELISA kit to detect Rat a-Gluwith the optical density on ...
more infohttps://www.antibodies-online.com/cellular-glucan-metabolic-process-pathway-69/aglu-elisa-kit-6102/

alpha-Glucosidase ELISA & Assay Kitsalpha-Glucosidase ELISA & Assay Kits

Compare and order alpha-Glucosidase ELISA Kits. View citations, images, detection ranges, sensitivity, prices and more. ... alpha glucosidase 2 , maltase , alpha-glucosidase , CG11909-PA , alpha-Glucosidase , tobi-PA , acid (Pompe disease, glycogen ... acid alpha-glucosidase , acid maltase , glucosidase, alpha; acid (Pompe disease, glycogen storage disease type II) , lysosomal ... Search alpha-Glucosidase ELISA Kits for other reactivities: Mammalian,. Rabbit,. Guinea Pig,. Pig (Porcine),. Dog (Canine),. ...
more infohttps://www.antikoerper-online.de/cellular-glucan-metabolic-process-pathway-69/aglu-elisa-kit-6102/

T2D Medicine Alpha Glucosidase Inhibitors | Healthy-ojasT2D Medicine Alpha Glucosidase Inhibitors | Healthy-ojas

How does an alpha glucosidase inhibitor control the blood-glucose level? What are its side effects? ... Alpha-glucosidase inhibitors mechanism of action. Alpha-Glucosidase inhibitors work by inhibiting alpha-glucosidase, an enzyme ... Side effects of alpha-glucosidase. Side effects of alpha-glucosidase inhibitors include flatulence (77%), diarrhea (33%), and ... What you can expect for Alpha-glucosidase inhibitors?. As a mono-therapy, alpha-glucosidase inhibitors can decrease your ...
more infohttps://healthy-ojas.com/diabetes/alpha-glucosidase.html

anti-alpha Glucosidase II antibody [N1N2], N-term  | GeneTexanti-alpha Glucosidase II antibody [N1N2], N-term | GeneTex

... glucosidase, alpha; neutral AB) for ICC/IF, IHC-P, WB. Anti-alpha Glucosidase II pAb (GTX102237) is tested in Human, Mouse ... alpha-glucosidase 2 antibody, glucosidase II subunit alpha antibody, neutral alpha-glucosidase AB antibody, alpha glucosidase ... alpha Glucosidase II antibody [N1N2], N-term detects alpha Glucosidase II protein at cytoplasm in human breast carcinoma by ... alpha Glucosidase II antibody [N1N2], N-term detects alpha Glucosidase II protein at cytoplasm in human breast carcinoma by ...
more infohttp://www.genetex.com/alpha-Glucosidase-II-antibody-N1N2-N-term-GTX102237.html

alpha-Glucosidase Inhibitor international drug patents, pharmaceutical manufacturers and genericsalpha-Glucosidase Inhibitor international drug patents, pharmaceutical manufacturers and generics

Generic options for alpha-Glucosidase Inhibitor pharmaceutical drugs, including patent status, patent expiration dates, and ...
more infohttps://www.drugpatentwatch.com/p/drug-class/alpha-Glucosidase+Inhibitor

US20040091554A1 - Nutritional supplement containing alpha-glucosidase and alpha-amylase inhibitors 
        - Google PatentsUS20040091554A1 - Nutritional supplement containing alpha-glucosidase and alpha-amylase inhibitors - Google Patents

The composition can include touchi extract and phaseolamin as the alpha-glucosidase and alpha-amylase inhibitor, respectively. ... A nutritional supplement composition contains inhibitors of alpha-glucosidase and alpha-amylase substantially in the absence of ... alpha-glucosidase inhibitor and between about 15 and 48% alpha-amylase inhibitor. More desirable, the alpha-glucosidase ... Alpha-glucosidase inhibitors prevent the enzyme from performing this function. A wide variety of alpha-glucosidase inhibitors ...
more infohttps://patents.google.com/patent/US20040091554A1/en
  • Midgut alpha-glucosidase (EC 3.2.1.20) activities were measured after ingestion of blood and sugar meals by the phlebotomine sandfly Phlebotomus langeroni. (lancs.ac.uk)
  • To our knowledge, this is the first report on the characterization of an alpha-glucosidase from the halophilic Archaea, which could serve as a new model to gain insights into carbon metabolism in this understudied microbial group. (mdpi.com)
  • alpha-Glucosidase activity increased significantly within 1 hr after a blood meal and was maintained at significantly high activities until 48 hr postfeeding, when it fell to basal activity levels. (lancs.ac.uk)
  • Midgut alpha-glucosidase activity also increased within 1 hr of feeding on a sucrose meal, but there was no discernable peak in activity during the days postingestion. (lancs.ac.uk)
  • Moreover, computational analyses for the detection of functional domains, active and catalytic sites, as well as 3D structural predictions revealed a close relationship with an E. coli YicI-like alpha-xylosidase of the GH31 family. (mdpi.com)