Inhibins
Glycoproteins that inhibit pituitary FOLLICLE STIMULATING HORMONE secretion. Inhibins are secreted by the Sertoli cells of the testes, the granulosa cells of the ovarian follicles, the placenta, and other tissues. Inhibins and ACTIVINS are modulators of FOLLICLE STIMULATING HORMONE secretions; both groups belong to the TGF-beta superfamily, as the TRANSFORMING GROWTH FACTOR BETA. Inhibins consist of a disulfide-linked heterodimer with a unique alpha linked to either a beta A or a beta B subunit to form inhibin A or inhibin B, respectively
alpha 1-Antitrypsin
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
alpha7 Nicotinic Acetylcholine Receptor
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
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
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
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
Integrin alpha5
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
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
Alpha Rhythm
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
Protein Binding
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.
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.
PPAR alpha
Dinoprost
Adrenergic alpha-Antagonists
Hepatocyte Nuclear Factor 1-alpha
Binding Sites
Transfection
alpha 1-Antichymotrypsin
Glycoprotein found in alpha(1)-globulin region in human serum. It inhibits chymotrypsin-like proteinases in vivo and has cytotoxic killer-cell activity in vitro. The protein also has a role as an acute-phase protein and is active in the control of immunologic and inflammatory processes, and as a tumor marker. It is a member of the serpin superfamily.
Transforming Growth Factor alpha
Signal Transduction
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
Gene Expression Regulation
Transcription Factors
Adrenergic alpha-1 Receptor Antagonists
alpha Karyopherins
Nucleocytoplasmic transport molecules that bind to the NUCLEAR LOCALIZATION SIGNALS of cytoplasmic molecules destined to be imported into the CELL NUCLEUS. Once attached to their cargo they bind to BETA KARYOPHERINS and are transported through the NUCLEAR PORE COMPLEX. Inside the CELL NUCLEUS alpha karyopherins dissociate from beta karypherins and their cargo. They then form a complex with CELLULAR APOPTOSIS SUSCEPTIBILITY PROTEIN and RAN GTP-BINDING PROTEIN which is exported to the CYTOPLASM.
Macromolecular Substances
Tumor Necrosis Factor-alpha
Serum glycoprotein produced by activated MACROPHAGES and other mammalian MONONUCLEAR LEUKOCYTES. It has necrotizing activity against tumor cell lines and increases ability to reject tumor transplants. Also known as TNF-alpha, it is only 30% homologous to TNF-beta (LYMPHOTOXIN), but they share TNF RECEPTORS.
Prazosin
6-Ketoprostaglandin F1 alpha
Protein Subunits
Cloning, Molecular
Dose-Response Relationship, Drug
Mutation
Mice, Knockout
Strains of mice in which certain GENES of their GENOMES have been disrupted, or "knocked-out". To produce knockouts, using RECOMBINANT DNA technology, the normal DNA sequence of the gene being studied is altered to prevent synthesis of a normal gene product. Cloned cells in which this DNA alteration is successful are then injected into mouse EMBRYOS to produce chimeric mice. The chimeric mice are then bred to yield a strain in which all the cells of the mouse contain the disrupted gene. Knockout mice are used as EXPERIMENTAL ANIMAL MODELS for diseases (DISEASE MODELS, ANIMAL) and to clarify the functions of the genes.
Gene Expression
Transcription, Genetic
GTP-Binding Proteins
Regulatory proteins that act as molecular switches. They control a wide range of biological processes including: receptor signaling, intracellular signal transduction pathways, and protein synthesis. Their activity is regulated by factors that control their ability to bind to and hydrolyze GTP to GDP. EC 3.6.1.-.
Blotting, Western
Protein Structure, Tertiary
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
Phosphorylation
Amino Acid Sequence
Clonidine
Collagen
Promoter Regions, Genetic
Tumor Cells, Cultured
Yohimbine
Protein Conformation
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
DNA-Binding Proteins
Recombinant Fusion Proteins
Cattle
Interleukin-1
A soluble factor produced by MONOCYTES; MACROPHAGES, and other cells which activates T-lymphocytes and potentiates their response to mitogens or antigens. Interleukin-1 is a general term refers to either of the two distinct proteins, INTERLEUKIN-1ALPHA and INTERLEUKIN-1BETA. The biological effects of IL-1 include the ability to replace macrophage requirements for T-cell activation.
DNA
A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).
Adrenergic alpha-2 Receptor Agonists
The extracellular matrix in the mouse brain: its reactions to endo-alpha-N-acetylgalactosaminidase and certain other enzymes. (1/59)
As our previous studies have indicated, the cingulate cortex of the adult mouse brain contains many neurons with rich cell surface glycoproteins which are linked by collagenous ligands to perineuronal proteoglycans. The present study demonstrated that exclusive incubation with endo-alpha-N-acetylgalactosaminidase abolished the lectin Vicia villosa or Wisteria floribunda agglutinin (VVA or WFA) labeling of the nerve cell surface glycoproteins, while it neither interfered with the cationic iron colloid or aldehyde fuchsin stainings of the perineuronal proteoglycans nor abolished the Gomori's ammoniacal silver impregnation of the collagenous ligands. Double incubations with endo-alpha-N-acetylgalactosaminidase and collagenase did not eliminate the lectin VVA or WFA labeling of the nerve cell surface glycoproteins, though they did eliminate the cationic iron colloid and aldehyde fuchsin stainings of the perineuronal proteoglycans as well as the Gomori's ammoniacal silver impregnation of the collagenous ligands. Triple incubations with endo-alpha-N-acetylgalactosaminidase, collagenase, and endo-alpha-N-acetylgalactosaminidase abolished the lectin VVA or WFA labeling of the nerve cell surface glycoproteins, and also eliminated the cationic iron colloid and aldehyde fuchsin stainings of the perineuronal proteoglycans and the Gomori's ammoniacal silver impregnation of the collagenous ligands. These findings indicate that: the nerve cell surface glycoproteins or their terminal N-acetylgalactosamines are digested by endo-alpha-N-acetylgalactosaminidase; these galactosamines associated with the collagenous ligands or perineuronal proteoglycans are not digested by endo-alpha-N-acetylgalactosaminidase; and the terminal N-acetylgalactosamines newly exposed by collagenase incubation are digested by this galactosaminidase. It was further demonstrated that hyaluronidase incubation neither digests the collagenous ligands nor revives the lectin VVA or WFA labeling of the nerve cell surface proteoglycans. (+info)Glycoprotein lysosomal storage disorders: alpha- and beta-mannosidosis, fucosidosis and alpha-N-acetylgalactosaminidase deficiency. (2/59)
Glycoproteinoses belong to the lysosomal storage disorders group. The common feature of these diseases is the deficiency of a lysosomal protein that is part of glycan catabolism. Most of the lysosomal enzymes involved in the hydrolysis of glycoprotein carbohydrate chains are exo-glycosidases, which stepwise remove terminal monosaccharides. Thus, the deficiency of a single enzyme causes the blockage of the entire pathway and induces a storage of incompletely degraded substances inside the lysosome. Different mutations may be observed in a single disease and in all cases account for the nonexpression of lysosomal glycosidase activity. Different clinical phenotypes generally characterize a specific disorder, which rather must be described as a continuum in severity, suggesting that other biochemical or environmental factors influence the course of the disease. This review provides details on clinical features, genotype-phenotype correlations, enzymology and biochemical storage of four human glycoprotein lysosomal storage disorders, respectively alpha- and beta-mannosidosis, fucosidosis and alpha-N-acetylgalactosaminidase deficiency. Moreover, several animal disorders of glycoprotein metabolism have been found and constitute valuable models for the understanding of their human counterparts. (+info)Human alpha-N-acetylgalactosaminidase: site occupancy and structure of N-linked oligosaccharides. (3/59)
Human alpha-N-acetylgalactosaminidase (alpha-GalNAc; also known as alpha-galactosidase B) is the lysosomal exoglycohydrolase that cleaves alpha-N-acetylgalactosaminyl moieties in glycoconjugates. Mutagenesis studies indicated that the first five (N124, N177, N201, N359, and N385) of the six potential N-glycosylation sites were occupied. Site 3 occupancy was important for enzyme function and stability. Characterization of the N-linked oligosaccharide structures on the secreted enzyme overexpressed in Chinese hamster ovary cells revealed highly heterogeneous structures consisting of complex (approximately 53%), hybrid (approximately 12%), and high mannose-type (approximately 33%) oligosaccharides. The complex structures were mono-, bi-, 2,4-tri-, 2,6-tri-, and tetraantennary, among which the biantennary structures were most predominant (approximately 53%). Approximately 80% of the complex oligo-saccharides had a core-region fucose and 50% of the complex oligosaccharides were sialylated exclusively with alpha-2,3-linked sialic acid residues. The majority of hybrid type oligo-saccharides were GalGlcNAcMan(6)GlcNAc-Fuc(0-1)GlcNAc. Approximately 54% of the hybrid oligosaccharide were phosphorylated and one-third of these structures were further sialylated, the latter representing unique phosphorylated and sialylated structures. Of the high mannose oligosaccharides, Man(5-7)GlcNAc(2) were the predominant species (approximately 90%) and about 50% of the high mannose oligosaccharides were phosphorylated, exclusively as monoesters whose positions were determined. Comparison of the oligosaccharide structures of alpha-GalNAc and alpha-galactosidase A, an evolutionary-related and highly homologous exoglycosidase, indicated that alpha-GalNAc had more completed complex chains, presumably due to differences in enzyme structure/domains, rate of biosynthesis, and/or aggregation of the overexpressed recombinant enzymes. (+info)Blood group A antigen is a coreceptor in Plasmodium falciparum rosetting. (4/59)
The malaria parasite Plasmodium falciparum utilizes molecules present on the surface of uninfected red blood cells (RBC) for rosette formation, and a dependency on ABO antigens has been previously shown. In this study, the antirosetting effect of immune sera was related to the blood group of the infected human host. Sera from malaria-immune blood group A (or B) individuals were less prone to disrupt rosettes from clinical isolates of blood group A (or B) patients than to disrupt rosettes from isolates of blood group O patients. All fresh clinical isolates and laboratory strains exhibited distinct ABO blood group preferences, indicating that utilization of blood group antigens is a general feature of P. falciparum rosetting. Soluble A antigen strongly inhibited rosette formation when the parasite was cultivated in A RBC, while inhibition by glycosaminoglycans decreased. Furthermore, a soluble A antigen conjugate bound to the cell surface of parasitized RBC. Selective enzymatic digestion of blood group A antigen from the uninfected RBC surfaces totally abolished the preference of the parasite to form rosettes with these RBC, but rosettes could still form. Altogether, present data suggest an important role for A and B antigens as coreceptors in P. falciparum rosetting. (+info)Adhesion of human lung mast cells to bronchial epithelium: evidence for a novel carbohydrate-mediated mechanism. (5/59)
Mast cells contribute to the pathophysiology of asthma through their immunomediator-secretory activity in response to both immunological and nonimmunological stimuli, and infiltrate the bronchial epithelium in this disease. We hypothesized that human lung mast cells (HLMC) localize to the bronchial epithelium via a specific cell-cell adhesion mechanism. We investigated the adhesion of HLMC to primary bronchial epithelial cells and the bronchial epithelial cell line BEAS-2B. HLMC adhered avidly to both primary cultures of bronchial epithelial cells and BEAS-2B cells (mean adhesion 68.4 and 60.1%, respectively) compared with eosinophil adhesion to BEAS-2B (mean adhesion 10.3%). HLMC adhesion did not alter after epithelial activation with cytokines, did not require Ca2+, and was not integrin-mediated. IgE-dependent activation of HLMC produced an approximately 40% inhibition of adhesion. There was significant attenuation of adhesion after incubation of HLMC with pronase, beta-galactosidase, and endo-alpha-N-acetylgalactosaminidase, indicating that HLMC adhere to bronchial epithelial cells via galactose-bearing carbohydrates expressed on a cell-surface peptide(s). (+info)Trypsin inhibitory activity of bovine fetuin de-O-glycosylated by endo-alpha-N-acetylgalactosaminidase. (6/59)
The effects of bovine fetuin O-glycans on its trypsin inhibitory activity were examined. De-sialylated (asialo-) and de-O-glycosylated fetuin were prepared from native fetuin using Arthrobacter neuraminidase and the mixture of it and Bacillus endo-alpha-N-acetylgalactosaminidase, respectively. De-sialylation and de-O-glycosylation from fetuin were confirmed with SDS-PAGE followed by western blotting using anti-human Thomsen-Friedenreich antigen (T antigen) antibody which recognizes O-linked galactosyl beta1,3 N-acetylgalactosamine (Gal beta1-->3GalNAc). Native fetuin completely inhibited the trypsin activity at about a 1:1 molar ratio. In contrast, the trypsin inhibitory activity of asialo- and de-O-glycosylated fetuin decreased about a half and one-third of that of native fetuin, respectively. (+info)Human alpha-N-acetylgalactosaminidase (alpha-NAGA) deficiency: no association with neuroaxonal dystrophy? (7/59)
Two new individuals with alpha-NAGA deficiency are presented. The index patient, 3 years old, has congenital cataract, slight motor retardation and secondary demyelinisation. Screening of his sibs revealed an alpha-NAGA deficiency in his 7-year-old healthy brother who had no clinical or neurological symptoms. Both sibs are homozygous for the E325K mutation, the same genotype that was found in the most severe form of alpha-NAGA deficiency presenting as infantile neuroaxonal dystrophy. Thus, at the age of 7 years the same genotype of alpha-NAGA may present as a 'non-disease' (present healthy case) and can be associated with the vegetative state (the first two patients described with alpha-NAGA deficiency). The clinical heterogeneity among the 11 known individuals with alpha-NAGA deficiency is extreme, with a 'non-disease' (two cases) and infantile neuroaxonal dystrophy (two cases) at the opposite sides of the clinical spectrum. The broad spectrum is completed by a very heterogeneous group of patients with various degrees of epilepsy/behavioural difficulties/psychomotor retardation (four patients) and a mild phenotype in adults without overt neurological manifestations who have angiokeratoma and clear vacuolisation in various cell types (three cases). These observations are difficult to reconcile with a straightforward genotype-phenotype correlation and suggest that factors or genes other than alpha-NAGA contribute to the clinical heterogeneity of the 11 patients with alpha-NAGA deficiency. (+info)Efficient synthesis of O-linked glycopeptide by a transglycosylation using endo alpha-N-acetylgalactosaminidase from Streptomyces sp. (8/59)
Gal beta-(1-->3)-GalNAc-linked hexapeptide was synthesized by a transglycosylation using Gal beta-(1-->3)-GalNAc beta-pNP as a donor and a serine-containing hexapeptide as an acceptor using endo GalNAc-ase from Streptomyces sp.. The Gal beta-(1-->3)-GalNAc residue was transferred to the hydroxyl group of the serine residue of the peptide. The total yield of the glycopeptide via this process was better than that of the chemoenzymatic method. This process was confirmed to be a versatile method for the synthesis of O-linked glycopeptides. (+info)
Schindler Disease Type 1 (Alpha-N-Acetylgalactosaminidase Deficiency Type 1): Symptoms, Diagnosis and Treatment - Symptoma
Human alpha-N-acetylgalactosaminidase (NAGA) gene, complete cds - Nucleotide - NCBI
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Alpha-N-acetylgalactosaminidase
Mutations in this gene and the deficiency in alpha-N-acetylgalactosaminidase activity have been identified as the cause of ... the molecular lesion in the alpha-N-acetylgalactosaminidase gene that causes an infantile neuroaxonal dystrophy". The Journal ... α-N-acetylgalactosaminidase (EC 3.2.1.49) is a glycoside hydrolase from bacteria and animals, also known as nagalase. The human ... August 2013). "N-acetylgalactosaminidase levels in advanced cancer patients". Oncoimmunology. 2 (8): e25769. doi:10.4161/onci. ...
Endo-alpha-N-acetylgalactosaminidase
... may refer to: Mucinaminylserine mucinaminidase, an enzyme Glycopeptide alpha-N- ... acetylgalactosaminidase, an enzyme This set index page lists enzyme articles associated with the same name. If an internal link ...
Glycopeptide alpha-N-acetylgalactosaminidase
Endo-alpha-N-acetylgalactosaminidase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC ... Ashida H, Yamamoto K, Murata T, Usui T, Kumagai H (January 2000). "Characterization of endo-alpha-N-acetylgalactosaminidase ... Endo-α-N-acetylgalactosaminidase (EC 3.2.1.97, endo-α-acetylgalactosaminidase, endo-α-N-acetyl-D-galactosaminidase, ... and characterization of a novel endo-alpha-N-acetylgalactosaminidase from Enterococcus faecalis". Biochemical and Biophysical ...
Morpheein
Corti, A; Fassina, G; Marcucci, F; Barbanti, E; Cassani, G (1992). "Oligomeric tumour necrosis factor alpha slowly converts ... Weissmann, Bernard; Hinrichsen, Dorotea F. (1969). "Mammalian α-acetylgalactosaminidase. Occurrence, partial purification, and ... Weissmann, Bernard; Wang, Ching-Te (1971). "Association-dissociation and abnormal kinetics of bovine .alpha.- ...
Robert J. Desnick
"Cloning and expression of biologically active alpha N-acetylgalactosaminidase", published 1996-02-13, assigned to Mount Sinai ... National Institute of Diabetes and Digestive and Kidney Diseases Alpha Galactosidases A And B - Molecular and Cellular ... Cloning and expression of biologically active alpha-galactosidase A as a fusion protein, (1996). Acid sphingomyelinase gene and ... Correction of the biochemical and functional deficits in Fabry mice following AAV8-mediated hepatic expression of alpha- ...
Mucinaminylserine mucinaminidase
Other names in common use include endo-alpha-N-acetylgalactosaminidase, and endo-alpha-N-acetyl-D-galactosaminidase. ... Endo Y, Kobata A (July 1976). "Partial purification and characterization of an endo-alpha-N-acetylgalactosaminidase from the ... Bhavanandan VP, Umemoto J, Davidson EA (1976). "Characterization of an endo-alpha-N-acetyl galactosaminidase from Diplococcus ... Umemoto J, Bhavanandan VP, Davidson EA (1977). "Purification and properties of an endo-alpha-N-acetyl-D-galactosaminidase from ...
NAGA (gene)
1996). "Human alpha-N-acetylgalactosaminidase (alpha-NAGA) deficiency: new mutations and the paradox between genotype and ... 1989). "Molecular cloning of a full-length cDNA for human alpha-N-acetylgalactosaminidase (alpha-galactosidase B)". Biochem. ... NAGA encodes the lysosomal enzyme alpha-N-acetylgalactosaminidase, which cleaves alpha-N-acetylgalactosaminyl moieties from ... "Structural organization and complete sequence of the human alpha-N-acetylgalactosaminidase gene: homology with the alpha- ...
Schindler disease
This lysosomal storage disorder is caused by a deficiency in the enzyme alpha-NAGA (alpha-N-acetylgalactosaminidase), ... Schindler disease, also known as Kanzaki disease and alpha-N-acetylgalactosaminidase deficiency is a rare disease found in ... the molecular lesion in the alpha-N-acetylgalactosaminidase gene that causes an infantile neuroaxonal dystrophy". J. Clin. ... A deficiency of the alpha-NAGA enzyme leads to an accumulation of glycosphingolipids throughout the body. This accumulation of ...
Infantile neuroaxonal dystrophy
... resulting in alpha-N-acetylgalactosaminidase deficiency, cause an infantile neuroaxonal dystrophy known as Schindler disease. ... the molecular lesion in the alpha-N-acetylgalactosaminidase gene that causes an infantile neuroaxonal dystrophy". J. Clin. ...
Glycoside hydrolase family 27
Alpha-N-acetylgalactosaminidase (EC 3.2.1.49) catalyzes the hydrolysis of terminal non-reducing N-acetyl-D-galactosamine ... Wang AM, Bishop DF, Desnick RJ (1990). "Human alpha-N-acetylgalactosaminidase-molecular cloning, nucleotide sequence, and ... a superfamily of alpha-galactosidases, alpha-N-acetylgalactosaminidases, and isomaltodextranases which are likely to share a ... Alpha-galactosidase (EC 3.2.1.22) (melibiase) catalyzes the hydrolysis of melibiose into galactose and glucose. In man, the ...
Glycoside hydrolase family 36
Alpha-N-acetylgalactosaminidase (EC 3.2.1.49) catalyzes the hydrolysis of terminal non-reducing N-acetyl-D-galactosamine ... Wang AM, Bishop DF, Desnick RJ (1990). "Human alpha-N-acetylgalactosaminidase-molecular cloning, nucleotide sequence, and ... Raffinose (O-alpha- D-galactopyranosyl- (1-->6)- O-alpha- D-glucopyranosyl-(1<-->2)- O-beta- D-fructofuranoside) is a ... a superfamily of alpha-galactosidases, alpha-N-acetylgalactosaminidases, and isomaltodextranases which are likely to share a ...
List of skin conditions
... alpha-N-acetylgalactosaminidase deficiency) Schinzel-Giedion syndrome Scleroatrophic syndrome of Huriez (Huriez syndrome, ... Acquired generalized lipodystrophy (Lawrence syndrome, Lawrence-Seip syndrome) Adiposis dolorosa (Dercum's disease) Alpha-1 ... Familial alpha-lipoprotein deficiency (Tangier disease) Familial amyloid polyneuropathy Familial apoprotein CII deficiency ...
GcMAF
... misleadingly based on reduced levels of the alpha-N-acetylgalactosaminidase enzyme (also known as nagalase), whose production ...
Naga
... which encodes the enzyme alpha-N-acetylgalactosaminidase Naga City (disambiguation) Nagar (disambiguation) Nagas ( ...
List of MeSH codes (D08)
... alpha-N-acetylgalactosaminidase MeSH D08.811.277.450.483.112 - Beta-N-acetylgalactosaminidase MeSH D08.811.277.450.483.180 - ... gtp-binding protein alpha subunits MeSH D08.811.277.040.330.300.200.100.100 - gtp-binding protein alpha subunits, g12-g13 MeSH ... gtp-binding protein alpha subunit, gi2 MeSH D08.811.277.040.330.300.200.100.300 - gtp-binding protein alpha subunits, gq-g11 ... steroid 12-alpha-hydroxylase MeSH D08.811.682.690.708.170.915.737 - steroid 16-alpha-hydroxylase MeSH D08.811.682.690.708.170. ...
Hexosaminidase
Even though the alpha and beta subunits of lysosomal hexosaminidase can both cleave GalNAc residues, only the alpha subunit is ... and β-N-acetylgalactosaminidase from calf brain". Biochemistry. 6 (9): 2775-82. doi:10.1021/bi00861a018. PMID 6055190. Li SC, ... and a loop structure that forms from the amino acid sequence in the alpha subunit. The loop in the alpha subunit, consisting of ... A glutamate residue (alpha Glu-323/beta Glu-355) works as an acid by donating its hydrogen to the glycosidic oxygen atom on the ...
Glycosylation
It has been suggested this rare finding may be linked to the fact that alpha dystroglycan is highly conserved from lower ... endo-α-N-Acetylgalactosaminidase (O-glycosidase from Streptococcus pneumoniae): removes O-glycosylation. This enzyme cleaves ... Mannose has recently been reported in a vertebrate, the mouse, Mus musculus, on the cell-surface laminin receptor alpha ... A C-C bond is formed between the first carbon of the alpha-mannose and the second carbon of the tryptophan. However, not all ...
Neuroaxonal dystrophy due to lysosomal alpha-N-acetylgalactosaminidase deficiency - PubMed
Neuroaxonal dystrophy due to lysosomal alpha-N-acetylgalactosaminidase deficiency ... Human alpha-N-acetylgalactosaminidase (alpha-NAGA) deficiency: no association with neuroaxonal dystrophy? Bakker HD, de ... Neuroaxonal dystrophy due to lysosomal alpha-N-acetylgalactosaminidase deficiency D Schindler 1 , D F Bishop, D E Wolfe, A M ... Neuroaxonal dystrophy due to lysosomal alpha-N-acetylgalactosaminidase deficiency D Schindler et al. N Engl J Med. 1989. . ...
Molecular cloning, structural organization, sequence, chromosomal assignment, and expression of the mouse alpha-N...
NAGA gene: MedlinePlus Genetics
The NAGA gene provides instructions for making the enzyme alpha-N-acetylgalactosaminidase. Learn about this gene and related ... Three dimensional structural studies of alpha-N-acetylgalactosaminidase (alpha-NAGA) in alpha-NAGA deficiency (Kanzaki disease ... Human alpha-N-acetylgalactosaminidase (alpha-NAGA) deficiency: new mutations and the paradox between genotype and phenotype. J ... Specifically, alpha-N-acetylgalactosaminidase helps remove a molecule called alpha-N-acetylgalactosamine from sugars in these ...
Angiokeratoma Corporis Diffusum (Fabry Disease) Differential Diagnoses
... is an X-linked inherited disorder caused by a deficiency of the lysosomal enzyme alpha-galactosidase. This inborn error of ... Michael J Wells, MD, FAAD is a member of the following medical societies: Alpha Omega Alpha, American Academy of Dermatology, ... Timothy McCalmont, MD is a member of the following medical societies: Alpha Omega Alpha, American Medical Association, American ... Quantification of alpha-galactosidase activity in intact leukocytes. Clin Chim Acta. 2010 Jun 25. [QxMD MEDLINE Link]. ...
SciELO - Brazil - Biochemical identification techniques and antibiotic susceptibility profile of lipolytic ambiental bacteria...
Schindler disease type 1 - About the Disease - Genetic and Rare Diseases Information Center
N-acetyl-alpha-D-galactosaminidase deficiency type III; Alpha-N-acetylgalactosaminidase deficiency, type 1; NAGA deficiency, ... Alpha-N-acetylgalactosaminidase deficiency type 3; NAGA deficiency type 3; Schindler disease type 3N-acetyl-alpha-D- ... Alpha-N-acetylgalactosaminidase deficiency type 3; NAGA deficiency type 3; Schindler disease type 3. Read More ... Alpha-N-acetylgalactosaminidase deficiency, type 1; NAGA deficiency, type 1; Neuroaxonal dystrophy, Schindler type; Schindler ...
Holistic Doctors being murdered? | Cassiopaea Forum
These patient sera contained alpha-N-acetylgalactosaminidase (Nagalase) that deglycosylates Gc protein. Deglycosylated Gc ... Pathogenic significance of alpha-N-acetylgalactosaminidase activity found in the hemagglutinin of influenza virus.. Yamamoto N1 ... GcMAF will induce a good phagocytosis without the bad IL-1 and TNF-alpha release. Bad macrophage activation by LPS is ...
SCOP 1.75: Family b.71.1.1: alpha-Amylases, C-terminal beta-sheet domain
alpha-N-acetylgalactosaminidase. *. Species Human (Homo sapiens) [TaxId:9606] [101919] (2 PDB entries). alpha-galactosidase A. ... alpha-galactosidase. *. Species Trichoderma reesei [TaxId:51453] [110300] (2 PDB entries). Uniprot Q92456; Alpha-galactosidase ... Timeline for Family b.71.1.1: alpha-Amylases, C-terminal beta-sheet domain: *Family b.71.1.1: alpha-Amylases, C-terminal beta- ... Family b.71.1.1: alpha-Amylases, C-terminal beta-sheet domain appears in SCOP 1.73. *Family b.71.1.1: alpha-Amylases, C- ...
PLA2G6-Associated Neurodegeneration - GeneReviews® - NCBI Bookshelf
Human alpha-N-acetylgalactosaminidase (alpha-NAGA) deficiency: new mutations and the paradox between genotype and phenotype. J ... Human alpha-N-acetylgalactosaminidase (alpha-NAGA) deficiency: no association with neuroaxonal dystrophy? Eur J Hum Genet. 2001 ... Neuroaxonal dystrophy due to lysosomal alpha-N-acetylgalactosaminidase deficiency. N Engl J Med. 1989;320:1735-40. [PubMed: ... and deficiency of α-N-acetylgalactosaminidase (α-NAGA) [Schindler et al 1989]. Alpha-NAGA deficiency underlies the ...
Biomarkers Search
1. Serum alpha-N-acetylgalactosaminidase is associated with diagnosis/prognosis of patients with squamous cell carcinoma of the ... 6. Tumor cell alpha-N-acetylgalactosaminidase activity and its involvement in GcMAF-related macrophage activation.. Mohamad SB ... Deglycosylation of serum vitamin D3-binding protein by alpha-N-acetylgalactosaminidase detected in the plasma of patients with ... 2. The value of serum alpha-N-acetylgalactosaminidase measurement for the assessment of tumour response to radio- and ...
Lysosomal Storage Disease: Overview, Classification of Lysosomal Storage Diseases, Glycogen Storage Disease Type II
Schindler disease results from the deficient activity of the enzyme alpha-N -acetylgalactosaminidase (alpha-galactosidase B), ... Alpha-Mannosidosis and Beta-Mannosidosis. Lysosomal alpha-mannosidase is a major exoglycosidase in the glycoprotein degradation ... Schindler disease/Kanzaki disease (alpha-N -acetylgalactosaminidase deficiency) (See Schindler Disease for detailed information ... Alpha-mannosidosis and beta-mannosidosis (See Alpha-Mannosidosis and Beta-Mannosidosis for detailed information.) ...
GSE5503 MLN DC VS SPLEEN DC ACTIVATED ALLOGENIC TCELL UP
Characterization of gana-1, a Caenorhabditis elegans gene encoding a single ortholog of vertebrate α-galactosidase and α-N...
... and α-N-acetylgalactosaminidase (α-NAGA) are presumed to share a common ancestor. Deficiencies of these enzymes cause two well- ... Purification and enzymatic properties of alpha-galactosidase B (alpha-N-acetylgalactosaminidase). J Biol Chem. 1979, 254: 10001 ... The identification of alpha-galactosidase B from human liver as an alpha-N-acetylgalactosaminidase. Biochem Biophys Res Commun ... Structural organization and complete sequence of the human alpha-N-acetylgalactosaminidase gene: homology with the alpha- ...
Coastal Post Online Article December, 2008
MeSH Browser
alpha-N-Acetyl-D-galactosaminidase endo-N-Acetyl-alpha-D-Galactosamidase endo-alpha-N-Acetylgalactosaminidase Registry Number. ... alpha-Galactosidase B Term UI T093960. LexicalTag NON. ThesaurusID NLM (2005). endo-alpha-N-Acetylgalactosaminidase Term UI ... alpha-D-N-Acetyl-Galactosaminyloligosaccharidase alpha-D-N-Acetylgalactosaminyloligosaccharidase alpha-Galactosidase B ... alpha-N-Acetylgalactosaminidase Preferred Term Term UI T093959. LexicalTag NON. ThesaurusID NLM (2005). ...
MeSH Browser
alpha-N-Acetyl-D-galactosaminidase endo-N-Acetyl-alpha-D-Galactosamidase endo-alpha-N-Acetylgalactosaminidase Registry Number. ... alpha-Galactosidase B Term UI T093960. LexicalTag NON. ThesaurusID NLM (2005). endo-alpha-N-Acetylgalactosaminidase Term UI ... alpha-D-N-Acetyl-Galactosaminyloligosaccharidase alpha-D-N-Acetylgalactosaminyloligosaccharidase alpha-Galactosidase B ... alpha-N-Acetylgalactosaminidase Preferred Term Term UI T093959. LexicalTag NON. ThesaurusID NLM (2005). ...
Adamtsl3 Mouse Gene Details | ADAMTS-like 3 | International Mouse Phenotyping Consortium
Code System Concept
American Journal of Immunology | Science Publications
Cellulose 1,4-beta-cellobiosidase - Wikipedia
Inosine nucleosidase - Wikipedia
pseudomyxoma peritonei; Ascites, Gelatinous
Angiokeratoma. Medical search
Alpha-N-acetylgalactosaminidase (NAGA) deficiency type 2 is a very rare mild adult type of NAGA deficiency (see this term) with ... alpha-Galactosidase. An enzyme that catalyzes the hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha- ... Angiokeratomaalpha-N-AcetylgalactosaminidaseFabry DiseaseTongue NeoplasmsSkin NeoplasmsDictionaries, MedicalScrotumDictionaries ... alpha-N-Acetylgalactosaminidase. A hexosaminidase with specificity for terminal non-reducing N-acetyl-D-galactosamine residues ...
Bio2Vec
GSVIVT01010478001 details
GlyConnect
Human alpha-N-acetylgalactosaminidase: site occupancy and structure of N-linked oligosaccharides. (2000 - Ohta M, Ohnishi T, ... Human alpha-N-acetylgalactosaminidase: site occupancy and structure of N-linked oligosaccharides. (2000 - Ohta M, Ohnishi T, ... Export GlyConnect protein list related to structure with id 404 P17050 # id : 45 Alpha-n-acetylgalactosaminidase Homo sapiens ... Analysis of site-specific N-glycosylation of recombinant Desmodus rotundus salivary plasminogen activator rDSPA alpha 1 ...
AMTR s00064p00187430 details
Arhgef2 Mouse Gene Details | rho/rac guanine nucleotide exchange factor (GEF) 2 | International Mouse Phenotyping Consortium
Reduced platelet alpha granules, Impaired ADP-induced platelet aggregation, Impaired collagen-ind.... OMIM:619130. ... Abnormal number of alpha granules, Impaired thrombin-induced platelet aggregation, Impaired colla.... OMIM:139090. ... Impaired platelet aggregation, Acute monocytic leukemia, Abnormal alpha granule content, Abnormal.... OMIM:601399. ... Alpha-N-Acetylgalactosaminidase Deficiency Type 1. Aplasia/Hypoplasia of the cerebellum, Abnormal brainstem morphology. ORPHA: ...
N-acetyl-alpha-D-galactosaminidase deficiency type III - Rare Oncology News
of the alpha-N-acetylgalactosaminidase gene. (NAGA; 22q13.2) have been reported in affected patients but also occasionally in ... Alpha-N-acetylgalactosaminidase deficiency type 3; NAGA deficiency type 3; Schindler disease type 3 ... PubMed is a searchable database of medical literature and lists journal articles that discuss N-acetyl-alpha-D- ...
NAGA4
- NAGA encodes the lysosomal enzyme alpha-N-acetylgalactosaminidase, which cleaves alpha-N-acetylgalactosaminyl moieties from glycoconjugates. (nih.gov)
- Three dimensional structural studies of alpha-N-acetylgalactosaminidase (alpha-NAGA) in alpha-NAGA deficiency (Kanzaki disease): different gene mutations cause peculiar structural changes in alpha-NAGAs resulting in different substrate specificities and clinical phenotypes. (nih.gov)
- The NAGA gene provides instructions for making the enzyme alpha-N-acetylgalactosaminidase. (medlineplus.gov)
- Kanekura T, Sakuraba H, Matsuzawa F, Aikawa S, Doi H, Hirabayashi Y, Yoshii N, Fukushige T, Kanzaki T. Three dimensional structural studies of alpha-N-acetylgalactosaminidase (alpha-NAGA) in alpha-NAGA deficiency (Kanzaki disease): different gene mutations cause peculiar structural changes in alpha-NAGAs resulting in different substrate specificities and clinical phenotypes. (medlineplus.gov)
Enzyme2
- Most of these mutations are believed to change the 3-dimensional shape of the alpha-N-acetylgalactosaminidase enzyme, interfering with its ability to break down glycoproteins and glycolipids. (medlineplus.gov)
- Dietary restriction has shown promise for disorders such as lysosomal acid lipase deficiency (Wolman disease), as has incorporation of lipid-lowering drugs in the regimen along with sebelipase alpha, a recombinant enzyme replacement therapy. (medscape.com)
Kanzaki1
- The 1.9 a structure of human alpha-N-acetylgalactosaminidase: The molecular basis of Schindler and Kanzaki diseases. (medlineplus.gov)
Schindler1
- Desnick RJ, Wang AM. Schindler disease: an inherited neuroaxonal dystrophy due to alpha-N-acetylgalactosaminidase deficiency. (medlineplus.gov)
Lysosomal1
- Michalski JC, Klein A. Glycoprotein lysosomal storage disorders: alpha- and beta-mannosidosis, fucosidosis and alpha-N-acetylgalactosaminidase deficiency. (medlineplus.gov)
Deficiency type3
- Winther is rated as a Distinguished expert by MediFind in the treatment of N-Acetyl-Alpha-D-Galactosaminidase Deficiency Type 3. (medifind.com)
- His top areas of expertise are N-Acetyl-Alpha-D-Galactosaminidase Deficiency Type 3 and H1N1 Influenza. (medifind.com)
- In particular, he has co-authored 2 articles in the study of N-Acetyl-Alpha-D-Galactosaminidase Deficiency Type 3. (medifind.com)
Molecule1
- Specifically, alpha-N-acetylgalactosaminidase helps remove a molecule called alpha-N-acetylgalactosamine from sugars in these complexes. (medlineplus.gov)
Symbol1
- endosulfine alpha [Source:HGNC Symbol;Ac. (gsea-msigdb.org)
Sugar1
- Chemically the A antigen differs from the O antigen only in that it has an additional terminal sugar residue, an alpha linked N acetylgalactostamine. (dtic.mil)
Deficiency8
- Lysosomal alpha-N-acetylgalactosaminidase deficiency, the enzymatic defect in angiokeratoma corporis diffusum with glycopeptiduria. (nih.gov)
- alpha-N-acetylgalactosaminidase deficiency, a new lysosomal storage disorder. (nih.gov)
- Schindler disease: an inherited neuroaxonal dystrophy due to alpha-N-acetylgalactosaminidase deficiency. (nih.gov)
- Human alpha-N-acetylgalactosaminidase (alpha-NAGA) deficiency: no association with neuroaxonal dystrophy? (nih.gov)
- Kanekura T, Sakuraba H, Matsuzawa F, Aikawa S, Doi H, Hirabayashi Y, Yoshii N, Fukushige T, Kanzaki T. Three dimensional structural studies of alpha-N-acetylgalactosaminidase (alpha-NAGA) in alpha-NAGA deficiency (Kanzaki disease): different gene mutations cause peculiar structural changes in alpha-NAGAs resulting in different substrate specificities and clinical phenotypes. (medlineplus.gov)
- Michalski JC, Klein A. Glycoprotein lysosomal storage disorders: alpha- and beta-mannosidosis, fucosidosis and alpha-N-acetylgalactosaminidase deficiency. (medlineplus.gov)
- An X-linked inherited metabolic disease caused by a deficiency of lysosomal ALPHA-GALACTOSIDASE A. It is characterized by intralysosomal accumulation of globotriaosylceramide and other GLYCOSPHINGOLIPIDS in blood vessels throughout the body leading to multi-system complications including renal, cardiac, cerebrovascular, and skin disorders. (lookformedical.com)
- PubMed is a searchable database of medical literature and lists journal articles that discuss N-acetyl-alpha-D-galactosaminidase deficiency type III. (rareoncologynews.com)
Nagalase3
- 8. Alteration of α-N-acetylgalactosaminidase (nagalase) concentration in alcohol-dependent individuals without liver disease, during the detoxification therapy. (nih.gov)
- But, as researchers explain it themselves, cancer cells secrete an enzyme known as alpha-N-acetylgalactosaminidase (also called Nagalase) that completely blocks conversion of Gc protein to Gc-MAF, preventing tumor-cell killing by the macrophages. (coastalpost.com)
- They do this by producing a protective enzyme called alpha-N-acetylgalactosaminidase, Nagalase for short. (healthkulture.net)
Gene1
- Fabry disease is a rare genetic disorder caused by mutations in the GLA gene - located on the X chromosome - that provides instructions for production of an enzyme called alpha-galactosidase A (alpha-GAL A). These mutations typically affect the activity of alpha-GAL A, leading to the accumulation of a type of fat called globotriaosylceramide (Gb3) in tissues and organs. (fabrydiseasenews.com)
Mutations1
- Most of these mutations are believed to change the 3-dimensional shape of the alpha-N-acetylgalactosaminidase enzyme, interfering with its ability to break down glycoproteins and glycolipids. (medlineplus.gov)
Activity5
- 6. Tumor cell alpha-N-acetylgalactosaminidase activity and its involvement in GcMAF-related macrophage activation. (nih.gov)
- 7. Pathogenic significance of alpha-N-acetylgalactosaminidase activity found in the hemagglutinin of influenza virus. (nih.gov)
- 9. Pathogenic significance of alpha-N-acetylgalactosaminidase activity found in the envelope glycoprotein gp160 of human immunodeficiency virus Type 1. (nih.gov)
- Dr. Bradstreet has published a paper: "Initial Observations of Elevated Alpha-N-Acetylgalactosaminidase Activity Associated with Autism and Observed Reductions from GC Protein-Macrophage Activating Factor Injections" which is groundbreaking in its discoveries. (nobelhealthsolutions.com)
- A single intravenous infusion of the construct in healthy mice increased alpha-GAL A activity 10-fold in the plasma and 20-fold in the liver, compared to animals treated with a vehicle solution (controls). (fabrydiseasenews.com)
Salivary1
- 11. Effect of salivary gland adenocarcinoma cell-derived alpha-N-acetylgalactosaminidase on the bioactivity of macrophage activating factor. (nih.gov)
Residues3
- A hexosaminidase with specificity for terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-alpha-D-galactosaminides. (nih.gov)
- An enzyme that catalyzes the hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-galactosides including galactose oligosaccharides, galactomannans, and galactolipids. (lookformedical.com)
- HN - 2005 MH - alpha-N-Acetylgalactosaminidase UI - D048809 MN - D8.811.277.450.483.44 MS - A hexosaminidase with specificity for terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-alpha-D-galactosaminides. (nih.gov)
Plasma1
- 12. Deglycosylation of serum vitamin D3-binding protein by alpha-N-acetylgalactosaminidase detected in the plasma of patients with systemic lupus erythematosus. (nih.gov)
Serum3
- 1. Serum alpha-N-acetylgalactosaminidase is associated with diagnosis/prognosis of patients with squamous cell carcinoma of the uterine cervix. (nih.gov)
- 2. The value of serum alpha-N-acetylgalactosaminidase measurement for the assessment of tumour response to radio- and photodynamic therapy. (nih.gov)
- 3. Prognostic utility of serum alpha-N-acetylgalactosaminidase and immunosuppression resulted from deglycosylation of serum Gc protein in oral cancer patients. (nih.gov)
Site1
- En continuant à naviguer sur le site, vous acceptez que nous utilisions des cookies. (redlabs.be)