α-N-アセチルガラクトサミニダーゼ

WordNet

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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[Wiki en表示]

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)

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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.

Glycoconjugate journal 27(1), 125-132, 2010-01
NAID 120002160188

Use of a Modified alpha-N-Acetylgalactosaminidase in the Development of Enzyme Replacement Therapy for Fabry Disease

AMERICAN JOURNAL OF HUMAN GENETICS 85(5), 569-580, 2009
NAID 120004710103

Molecular cloning, expression, and characterization of a novel endo-alpha-N-acetylgalactosaminidase from Enterococcus faecalis

Biochem. Biophys. Res. Commun. 375, 541-546, 2008
NAID 80019807502

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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
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PMC	articles
PubMed	articles
NCBI	proteins