Molecular cloning of a full-length cDNA for human α-N-acetylgalactosaminidase (α-galactosidase B)

Tsuji, Shoji; Yamauchi, Toyoaki; Hiraiwa, Masao; Isobe, Toshiaki; Okuyama, Tsuneo; Sakimura, Kenji; Takahashi, Yasuo; Nishizawa, Masatoyo; Uda, Yutaka; Miyatake, Tadashi

doi:10.1016/0006-291x(89)91149-2

Cited by 30 publications

(8 citation statements)

References 17 publications

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“…Of the five protein components, the 64-kDa protein was thought to be b-galactosidase and the 32-kDa and 20-kDa proteins were thought to be the components of protective protein, which has recently been identified as cathepsin A. 7,11) We have since confirmed that the 46-kDa protein is a-N-acetylgalactosaminidase using cDNA cloning, 12) while the 78-kDa protein was identified as the heavy chain of immunoglobulin M by van der Horst et al 13) Thus the protein band on SDS-PAGE derived from human placental sialidase remains unknown.…”

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confidence: 70%

Photoaffinity Labeling of Sialidase with a Biotin-Conjugated Phenylaminodiazirine Derivative of 2,3-Didehydro-2-deoxy-N-acetylneuraminic Acid

Kannappan

Ando

Furuhata

et al. 2008

Biological & Pharmaceutical Bulletin

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A biotin-conjugated photoactivatable phenylaminodiazirine derivative of 2,3-didehydro-2-deoxy-N-acetylneuraminic acid (DANA) was synthesized to identify sialidase. The free carboxylic group and N-acetyl substituent of sialic acid, which are important for recognition and enzymatic activity of sialidase, were conserved by the photolabeling compound as confirmed using analytical methods. The synthesized compound and DANA competitively inhibited starfish sialidase with a K i value of 7.6 m mM and 4.6 m mM, respectively. Photo incorporation of the labeling compound to sialidase increased with irradiation time; 90% photo incorporation was achieved with more than 10-min irradiation, and labeling was completely inhibited by the addition of a competitive inhibitor. Starfish sialidase purified using high-performance gel filtration chromatography was subjected to photoaffinity labeling. A 50-kDa band was revealed to contain the sialidase active site by the photolabeling compound, and labeling was completely hindered in presence of the competitive inhibitor. Labeling specificity was ensured by the addition of the heat-deactivated standard protein chymotrypsinogen A to the reaction mixture.

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confidence: 70%

Photoaffinity Labeling of Sialidase with a Biotin-Conjugated Phenylaminodiazirine Derivative of 2,3-Didehydro-2-deoxy-N-acetylneuraminic Acid

Kannappan

Ando

Furuhata

et al. 2008

Biological & Pharmaceutical Bulletin

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“…Table 1 summarizes the deduced amino acid sequences of a-GalNAcase I and a-GalNAcase II and compares with the corresponding sequences from human and chicken a-GalNAcases. 10,20) Analysis of sequences revealed 80% homology between a-GalNAcase I Fig. 1.…”

Section: Resultsmentioning

confidence: 98%

“…However, subsequent kinetic, inhibitor, immunologic and gene mapping studies demonstrated that a-galactosidases A and B were genetically distinct lysosomal enzymes with different substrate specificities and a-galactosidase B was in reality an a-GalNAcase. 10,11) Thus far, a-GalNAcases purified from different animal tissues including human, bovine, porcine, earthworm, snail, gastropod Turbo cornutus, limpet Patella vulgata and skipjack, all exhibited the a-galactosidase activity. 1,[12][13][14] a-GalNAcases without a-galactosidase activity have been found only in Clostridium perfringens.…”

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confidence: 99%

Chemical and Immunological Characterization of the Two .ALPHA.-N-Acetylgalactosaminidases from Squid Liver

Sadik

Itoh-Nashida

et al. 2009

Biological & Pharmaceutical Bulletin

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a-N-Acetylgalactosaminidase (a-GalNAcase) [EC 3.2.1.49] is a lysosomal exoglycosidase that cleaves a-linked N-acetylgalactosaminyl (a-GalNAc) units from glycoconjugates. Its physiological substrates presumably are glycopeptides and glycoproteins containing O-glycosidic core structures, and oligosaccharides, glycoproteins and glycosphingolipids bearing blood group A determinants or Forsmann haptens.1) The ability of a-GalNAcase to cleave a wide variety of substrate suggests that this enzyme plays a significant role in the metabolism of glycoconjugates. Mutation in the a-GalNAcase gene identified in patients with Schindler disease 2) and Kanzaki disease 3) have been shown to impair the enzymatic activity, resulting in the accumulation of undegraded glycoconjugates in lysosome. 4,5) Despite the physiological importance, a-GalNAcase has received much attention recent time for its ability to convert blood group O antigen, the universal donor blood type, from blood group A antigen. a-GalNAcase, therefore, can be used to process human blood to produce type O.6,7) Furthermore, a-GalNAcase is a tool of choice for elucidating the biological functions of the complex glycoconjugates having a-linked N-acetylgalactosaminyl units.a-GalNAcase, soon after its isolation from human tissue, was thought to be an isoenzyme of a-galactosidase for its weak a-galactosidase activity and thereafter called also agalactosidase B.8,9) The two enzymes had similar physicochemical properties, a subunit molecular mass of 48 kDa, homodimeric structure and a similar amino acid composition. However, subsequent kinetic, inhibitor, immunologic and gene mapping studies demonstrated that a-galactosidases A and B were genetically distinct lysosomal enzymes with different substrate specificities and a-galactosidase B was in reality an a-GalNAcase.10,11) Thus far, a-GalNAcases purified from different animal tissues including human, bovine, porcine, earthworm, snail, gastropod Turbo cornutus, limpet Patella vulgata and skipjack, all exhibited the a-galactosidase activity.1,12-14) a-GalNAcases without a-galactosidase activity have been found only in Clostridium perfringens. 15)During work on the glycosidases, we first discovered the occurence of two different a-GalNAcases, a-GalNAcase I and a-GalNAcase II, in the squid liver based on the enzymatic properties.16) a-GalNAcase I appeared to be a typical a-GalNAcase as it exhibited an inherent a-galactosidase activity and broader substrate specificity. 16,17) It was able to hydrolyze the artificial substrates p-nitrophenyl-a-N-galactosaminide and p-nitrophenyl-a-D-galactoside and natural substrates asialo bovine submaxillary mucin (ABSM), Forssman glycolipid, human ovarian cyst A-glycoprotein, blood group A-type ghosts, ceramide trihexoside (CTH) and oligosccharides melibiose, raffinose, stachyose, and amethyl-galactoside, indicating its specificity for a-N-galactosaminyl and a-galactosyl moiety. Moreover, the enzyme was heat stable and its enzymatic activity was inhibited by Nacetylgalactosamine and galactose....

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“…The human a-GalNAc was also accidentally found as one of the five major bands during purification of placental sialidases [22]. In this species, a-GalNAc seemed to be synthesized as a 65 kDa glycosylated precursor, which is processed to a mature 48 kDa isoform [20].…”

Section: Discussionmentioning

confidence: 99%

Characterization of pregnancy-associated glycoproteins extracted from zebu (Bos indicus) placentas removed at different gestational periods

et al. 2002

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-In the present work, two biochemical approaches were used to characterize PAGs isolated from Bos indicus fetal cotyledons removed at different gestational ages. The first procedure included acidic and ammonium sulfate precipitations, anion and cation exchange chromatographies and the second included pepstatin-agarose affinity chromatography. A bovine PAG radioimmunoassay was used to monitor the immunoreactivity throughout the isolation procedures. The most immunoreactive fractions issued from cation exchange and affinity chromatographies were analyzed by SDS-PAGE and Western blotting, before transfer to a polyvinylidene difluoride (PVDF) membrane for NH 2 -microsequence determination. Use SDS-PAGE and Western blotting, different isoforms of PAG with apparent molecular masses of 51 to 69 kDa and isoelectric points varying from 4.4 to 6.7 were identified in the placentas from different gestational ages. N-terminal microsequencing (10 to 25 aa long) indicates the expression of one single terminal amino acid sequence in the Bos indicus placenta, which is 100% identical to the bovine PAG-1. pregnancy-associated glycoprotein / purification / zebu / placenta / N-terminal microsequencing Reprod. Nutr. Dev. 42 (2002) 227-241 227

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Molecular cloning of a full-length cDNA for human α-N-acetylgalactosaminidase (α-galactosidase B)

Cited by 30 publications

References 17 publications

Photoaffinity Labeling of Sialidase with a Biotin-Conjugated Phenylaminodiazirine Derivative of 2,3-Didehydro-2-deoxy-N-acetylneuraminic Acid

Photoaffinity Labeling of Sialidase with a Biotin-Conjugated Phenylaminodiazirine Derivative of 2,3-Didehydro-2-deoxy-N-acetylneuraminic Acid

Chemical and Immunological Characterization of the Two .ALPHA.-N-Acetylgalactosaminidases from Squid Liver

Characterization of pregnancy-associated glycoproteins extracted from zebu (Bos indicus) placentas removed at different gestational periods

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