Brain-specific expression of a novel human UDP-GalNAc :polypeptide N-acetylgalactosaminyltransferase (GalNAc-T9)

被引:62
|
作者
Toba, S
Tenno, M
Konishi, M
Mikami, T
Itoh, N
Kurosaka, A [1 ]
机构
[1] Kyoto Sangyo Univ, Fac Engn, Dept Biotechnol, Kita Ku, Kyoto 6038555, Japan
[2] Kyoto Univ, Grad Sch Pharmaceut Sci, Dept Biochem Genet, Sakyo Ku, Kyoto 6068501, Japan
关键词
N-acetylgalactosaminyltransferase; mucin; O-glycosylation; brain;
D O I
10.1016/S0167-4781(00)00180-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We isolated cDNA coding for the ninth of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-T9) from human brain by the polymerase chain reaction. The polypeptide encoded by GalNAc-T9 contained the structural features characteristic of GalNAc transferases, such as a GT1 motif. a Gal/GalNAc transferase motif, (QXW)(3) repeats, and conserved His, Cys, and acidic amino acid residues. Northern blot analysis revealed the mRNA expression of the enzyme to be confined to the brain. The brain-specific expression of GalNAc-T9 suggested that this isozyme catalyzes O-glycosylation in the brain. (C) 2000 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:264 / 268
页数:5
相关论文
共 50 条
  • [1] Cloning and expression of a brain-specific putative UDP-GalNAc:: Polypeptide N-acetylgalactosaminyltransferase gene
    Nakamura, N
    Toba, S
    Hirai, M
    Morishita, S
    Mikami, T
    Konishi, M
    Itoh, N
    Kurosaka, A
    BIOLOGICAL & PHARMACEUTICAL BULLETIN, 2005, 28 (03) : 429 - 433
  • [2] A scintillation proximity assay for UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
    Baker, CA
    Poorman, RA
    Kezdy, FJ
    Staples, DJ
    Smith, CW
    Elhammer, AP
    ANALYTICAL BIOCHEMISTRY, 1996, 239 (01) : 20 - 24
  • [3] A scintillation proximity assay for UDP-GalNAc:Polypeptide, N-acetylgalactosaminyltransferase
    Pharmacia and Upjohn, Inc., 301 Henrietta Street, Kalamazoo, MI 49001, United States
    Anal. Biochem., 1 (20-24):
  • [4] Identification of two cysteine residues involved in the binding of UDP-GalNAc to UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1(GalNAc-T1)
    Tenno, M
    Toba, S
    Kézdy, FJ
    Elhammer, ÅP
    Kurosaka, A
    EUROPEAN JOURNAL OF BIOCHEMISTRY, 2002, 269 (17): : 4308 - 4316
  • [5] Characterization of a UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase that displays glycopeptide N-acetylgalactosaminyltransferase activity
    Ten Hagen, KG
    Tetaert, D
    Hagen, FK
    Richet, C
    Beres, TM
    Gagnon, J
    Balys, MM
    VanWuyckhuyse, B
    Bedi, GS
    Degand, P
    Tabak, LA
    JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (39) : 27867 - 27874
  • [6] Characterization of a novel member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family.
    Ten Hagen, KG
    Bedi, GS
    Balys, MM
    Hagen, FK
    Van Wuyckhuyse, B
    Tabak, LA
    JOURNAL OF DENTAL RESEARCH, 2000, 79 : 390 - 390
  • [7] A UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase is essential for viability in Drosophila melanogaster
    Ten Hagen, KG
    Tran, DT
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (25) : 22616 - 22622
  • [8] Molecular cloning and characterization of a novel member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family, pp-GalNAc-T12
    Guo, JM
    Zhang, Y
    Cheng, LM
    Iwasaki, H
    Wang, H
    Kubota, T
    Tachibana, K
    Narimatsu, H
    FEBS LETTERS, 2002, 524 (1-3) : 211 - 218
  • [9] Organization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase gene and a related processed pseudogene
    Meurer, JA
    Drong, RF
    Homa, FL
    Slightom, JL
    Elhammer, AP
    GLYCOBIOLOGY, 1996, 6 (02) : 231 - 241
  • [10] Cloning and expression of a novel, tissue specifically expressed member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family
    Ten Hagen, BG
    Hagen, FK
    Balys, MM
    Beres, TM
    Van Wuyckhuyse, B
    Tabak, LA
    JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (42) : 27749 - 27754