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- first in order of importance; "the alpha male in the group of chimpanzees"; "the alpha star in a constellation is the brightest or main star"
- the 1st letter of the Greek alphabet
- the beginning of a series or sequence; "the Alpha and Omega, the first and the last, the beginning and the end"--Revelations
- early testing stage of a software or hardware product; "alpha version"
- the 14th letter of the Roman alphabet (同)n
- any high mountain
PrepTutorEJDIC
- アルファ(ギリシア語アルファベットの第1字A,α;英語のA,aに相当) / アルファ星(星座の主星)
- nitrogenの化学記号
- 高山,高峰
- neodymiumの化学記号
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2014/04/25 22:01:17」(JST)
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Alpha-N-acetylgalactosaminidase |
Identifiers |
EC number |
3.2.1.49 |
CAS number |
9075-63-2 |
Databases |
IntEnz |
IntEnz view |
BRENDA |
BRENDA entry |
ExPASy |
NiceZyme view |
KEGG |
KEGG entry |
MetaCyc |
metabolic pathway |
PRIAM |
profile |
PDB structures |
RCSB PDB PDBe PDBsum |
Search |
PMC |
articles |
PubMed |
articles |
NCBI |
proteins |
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α-N-acetylgalactosaminidase (EC 3.2.1.49) is a glycoside hydrolase from bacteria and animals.
The human gene that codes for this enzyme is NAGA. Mutations in this gene and the deficiency in alpha-N-acetylgalactosaminidase activity have been identified as the cause of Schindler disease.[1]
A-N-acetylgalactosaminidase or Nagalase (EC/3.2.1.49) is a glycoside hydrolase from bacteria and animals and promotes immune suppression by inactivating Macrophages.
Alpha-N-acetyl galactosaminidase (alpha-NaGalase) has been reported to accumulate in serum of cancer patients and be responsible for deglycosylation of Gc protein, which is a precursor of Gc-MAF-mediated macrophage activation cascade, finally leading to immunosuppression in advanced cancer patients.
Alpha-NaGalase
"The biochemical characterization of alpha-NaGalase from several human tumor cell lines were studied. We also examined its effect on the potency of GcMAF to activate mouse peritoneal macrophage to produce superoxide in GcMAF-mediated macrophage activation cascade. The specific activity of alpha-NaGalases from human colon tumor cell line HCT116, human hepatoma cell line HepG2, and normal human liver cells (Chang liver cell line) were evaluated using two types of substrates; GalNAc-alpha-PNP (exo-type substrate) and Gal-beta-GalNAc-alpha-PNP (endo-type substrate).
Tumor-derived alpha-NaGalase having higher activity than normal alpha-NaGalase, had higher substrate specificity to the exo-type substrate than to the endo-type substrate, and still maintained its activity at pH 7. GcMAF enhance superoxide production in mouse macrophage, and pre-treatment of GcMAF with tumor cell lysate reduce the activity.
We conclude that tumor-derived alpha-NaGalase is different in biochemical characterization compared to normal alpha-NaGalase from normal Chang liver cells. In addition, tumor cell-derived alpha-NaGalase decreases the potency of Gc-MAF on macrophage activation."[2]
References
- ^ Wang AM, Schindler D, Desnick R (November 1990). "Schindler disease: the molecular lesion in the alpha-N-acetylgalactosaminidase gene that causes an infantile neuroaxonal dystrophy". J. Clin. Invest. 86 (5): 1752–6. doi:10.1172/JCI114901. PMC 296929. PMID 2243144.
- ^ Tumor cell alpha-N-acetylgalactosaminidase activity and its involvement in GcMAF-related macrophage activation / tten by Saharuddin B. Mohamad, Hideko Nagasawa, Yoshihiro Uto and Hitoshi Hori (2001)Elsevier, Volume 132, Issue 1, May 2002, Pages 1–8, Comparative Biochemistry and Physiology - Part A: Molecular & Integrative Physiology
External links
- Macrophage-Activating Factors at the US National Library of Medicine Medical Subject Headings (MeSH)
Hydrolase: sugar hydrolases (EC 3.2)
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3.2.1: Glycoside hydrolases |
Disaccharidase |
- Sucrase/Sucrase-isomaltase/Invertase
- Maltase
- Trehalase
- Lactase
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Glucosidases |
- Cellulase
- Alpha-glucosidase
- Acid
- Neutral AB
- Neutral C
- Beta-glucosidase
- Debranching enzyme
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Other |
- Amylase
- Chitinase
- Lysozyme
- Neuraminidase
- NEU1
- NEU2
- NEU3
- NEU4
- Bacterial neuraminidase
- Viral neuraminidase
- Galactosidases
- alpha-Mannosidase
- Glucuronidase
- Hyaluronidase
- Pullulanase
- Glucosylceramidase
- Galactosylceramidase
- Alpha-N-acetylgalactosaminidase
- Alpha-N-acetylglucosaminidase
- Fucosidase
- Hexosaminidase
- Iduronidase
- Maltase-glucoamylase
- Heparanase
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3.2.2: Hydrolysing
N-Glycosyl compounds |
- DNA glycosylases: Oxoguanine glycosylase
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- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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UpToDate Contents
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English Journal
- Exploration of Structural and Functional Variations Owing to Point Mutations in α-NAGA.
- Meshach Paul D1, Rajasekaran R2.
- Interdisciplinary sciences, computational life sciences.Interdiscip Sci.2016 May 2. [Epub ahead of print]
- Schindler disease is a lysosomal storage disorder caused due to deficiency or defective activity of alpha-N-acetylgalactosaminidase (α-NAGA). Mutations in gene encoding α-NAGA cause wide range of diseases, characterized with mild to severe clinical features. Molecular effects of these mutations ar
- PMID 27138754
- Evaluation of group A1B erythrocytes converted to type as group O: studies of markers of function and compatibility.
- Gao HW1, Zhuo HL2, Zhang X1, Ji SP1, Tan YX1, Li SB1, Jia YJ3, Xu H4, Wu QF1, Yun ZM1, Luo Q2, Gong F1.
- Blood transfusion = Trasfusione del sangue.Blood Transfus.2016 Mar;14(2):168-74. doi: 10.2450/2015.0010-15. Epub 2015 Sep 2.
- BACKGROUND: Enzymatic conversion of blood group A1B red blood cells (RBC) to group O RBC (ECO) was achieved by combined treatment with α-galactosidase and α-N-acetylgalactosaminidase. The aim of this study was to evaluate the function and safety of these A1B-ECO RBC in vitro.MATERIALS AND METHODS:
- PMID 26509826
- Application of ion mobility tandem mass spectrometry to compositional and structural analysis of glycopeptides extracted from the urine of a patient diagnosed with Schindler disease.
- Sarbu M1,2, Zhu F3, Peter-Katalinić J4,5, Clemmer DE3, Zamfir AD2,6.
- Rapid communications in mass spectrometry : RCM.Rapid Commun Mass Spectrom.2015 Nov 15;29(21):1929-37. doi: 10.1002/rcm.7288.
- RATIONALE: Schindler disease is caused by the deficient activity of α-N-acetylgalactosaminidase, which leads to an abnormal accumulation of O-glycopeptides in tissues and body fluids. In this work the Schindler condition is for the first time approached by ion mobility (IMS) tandem mass spectrometr
- PMID 26443390
Japanese Journal
- Syntheses of mucin-type O-glycopeptides and oligosaccharides using transglycosylation and reverse-hydrolysis activities of Bifidobacterium endo-alpha-N-acetylgalactosaminidase.
- Use of a Modified alpha-N-Acetylgalactosaminidase in the Development of Enzyme Replacement Therapy for Fabry Disease
- Molecular cloning, expression, and characterization of a novel endo-alpha-N-acetylgalactosaminidase from Enterococcus faecalis
Related Links
- alpha-N-acetylgalactosaminidase - definition of alpha-N-acetylgalactosaminidase by Medical dictionary http://medical-dictionary.thefreedictionary.com/alpha-N-acetylgalactosaminidase Printer Friendly Dictionary, Encyclopedia and ...
- Species, Scientific Experts, Genomes and Genes, Research Grants, Publications, Research Topics about alpha N acetylgalactosaminidase ... ..Taken together, these results suggest that alpha-GalNAcase I and alpha-GalNAcase II ...
Related Pictures
★リンクテーブル★
[★]
- 英
- alpha-N-acetylgalactosaminidase
[★]
- 関
- number of experiment、sample size
- pの前の[n]はmと記載する。synptom→symptom
[★]
[★]
α、アルファ
- 関
- alfa
[★]
ネオジム neodymium