cDNA cloning and expression of a novel human UDP-N-acetyl-α-D- galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-T3
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cDNA cloning and expression of a novel human UDP-N-acetyl-α-D- galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-T3. / Bennett, Eric Paul; Hassan, Helle; Clausen, Henrik.
I: Journal of Biological Chemistry, Bind 271, Nr. 29, 05.08.1996, s. 17006-17012.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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T1 - cDNA cloning and expression of a novel human UDP-N-acetyl-α-D- galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-T3
AU - Bennett, Eric Paul
AU - Hassan, Helle
AU - Clausen, Henrik
PY - 1996/8/5
Y1 - 1996/8/5
N2 - The glycosylation of serine and threonine residues during mucin-type O- linked protein glycosylation is carried out by a family of UDP- GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferase). Previously two members, GalNAc-T1 and -T2, have been isolated and the genes cloned and characterized. Here we report the cDNA cloning and expression of a novel GalNAc-transferase termed GalNAc-T3. The gene was isolated and cloned based on the identification of a GalNAc-transferase motif (61 amino acids) that is shared between GalNAc-T1 and -T2 as well as a homologous Caenorhabditis elegans gene. The cDNA sequence has a 633-amino acid coding region indicating a protein of 72.5 kDa with a type II domain structure. The overall amino acid sequence similarity with GalNAc-T1 and -T2 is approximately 45%; 12 cysteine residues that are shared between GalNAc-T1 and -T2 are also found in GalNAc-T3. GalNAc-T3 was expressed as a soluble protein without the hydrophobic transmembrane domain in insect cells using a Baculo- virus vector, and the expressed GalNAc-transferase activity showed substrate specificity different from that previously reported for GalNAc-T1 and -T2. Northern analysis of human organs revealed a very restricted expression pattern of GalNAc-T3.
AB - The glycosylation of serine and threonine residues during mucin-type O- linked protein glycosylation is carried out by a family of UDP- GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferase). Previously two members, GalNAc-T1 and -T2, have been isolated and the genes cloned and characterized. Here we report the cDNA cloning and expression of a novel GalNAc-transferase termed GalNAc-T3. The gene was isolated and cloned based on the identification of a GalNAc-transferase motif (61 amino acids) that is shared between GalNAc-T1 and -T2 as well as a homologous Caenorhabditis elegans gene. The cDNA sequence has a 633-amino acid coding region indicating a protein of 72.5 kDa with a type II domain structure. The overall amino acid sequence similarity with GalNAc-T1 and -T2 is approximately 45%; 12 cysteine residues that are shared between GalNAc-T1 and -T2 are also found in GalNAc-T3. GalNAc-T3 was expressed as a soluble protein without the hydrophobic transmembrane domain in insect cells using a Baculo- virus vector, and the expressed GalNAc-transferase activity showed substrate specificity different from that previously reported for GalNAc-T1 and -T2. Northern analysis of human organs revealed a very restricted expression pattern of GalNAc-T3.
UR - http://www.scopus.com/inward/record.url?scp=0030035111&partnerID=8YFLogxK
U2 - 10.1074/jbc.271.29.17006
DO - 10.1074/jbc.271.29.17006
M3 - Journal article
C2 - 8663203
AN - SCOPUS:0030035111
VL - 271
SP - 17006
EP - 17012
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 29
ER -
ID: 221854878