Polypeptide n-acetylgalactosaminyltransferase-associated phenotypes in mammals

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Polypeptide n-acetylgalactosaminyltransferase-associated phenotypes in mammals. / Kato, Kentaro; Hansen, Lars; Clausen, Henrik.

In: Molecules, Vol. 26, No. 18, 5504, 2021.

Research output: Contribution to journal › Review › Research › peer-review

Harvard

Kato, K, Hansen, L & Clausen, H 2021, 'Polypeptide n-acetylgalactosaminyltransferase-associated phenotypes in mammals', Molecules, vol. 26, no. 18, 5504. https://doi.org/10.3390/molecules26185504

APA

Kato, K., Hansen, L., & Clausen, H. (2021). Polypeptide n-acetylgalactosaminyltransferase-associated phenotypes in mammals. Molecules, 26(18), [5504]. https://doi.org/10.3390/molecules26185504

Vancouver

Kato K, Hansen L, Clausen H. Polypeptide n-acetylgalactosaminyltransferase-associated phenotypes in mammals. Molecules. 2021;26(18). 5504. https://doi.org/10.3390/molecules26185504

Author

Kato, Kentaro ; Hansen, Lars ; Clausen, Henrik. / Polypeptide n-acetylgalactosaminyltransferase-associated phenotypes in mammals. In: Molecules. 2021 ; Vol. 26, No. 18.

Bibtex

@article{8dcd292b03c04a47b60b669ef5c83eda,

title = "Polypeptide n-acetylgalactosaminyltransferase-associated phenotypes in mammals",

abstract = "Mucin-type O-glycosylation involves the attachment of glycans to an initial O-linked N-acetylgalactosamine (GalNAc) on serine and threonine residues on proteins. This process in mammals is initiated and regulated by a large family of 20 UDP-GalNAc: polypeptide N-acetylgalactosaminyl transferases (GalNAc-Ts) (EC 2.4.1.41). The enzymes are encoded by a large gene family (GALNTs). Two of these genes, GALNT2 and GALNT3, are known as monogenic autosomal recessive inherited disease genes with well characterized phenotypes, whereas a broad spectrum of phenotypes is associated with the remaining 18 genes. Until recently, the overlapping functionality of the 20 members of the enzyme family has hindered characterizing the specific biological roles of individual enzymes. However, recent evidence suggests that these enzymes do not have full functional redundancy and may serve specific purposes that are found in the different phenotypes described. Here, we summarize the current knowledge of GALNT and associated phenotypes.",

keywords = "GalNAc-T, GALNT, O-glycosylation, Polypeptide N-acetylgalactosaminyltransferase, UDP-GalNAc: polypeptide N-acetylgala ctosaminyltransferase",

author = "Kentaro Kato and Lars Hansen and Henrik Clausen",

note = "Publisher Copyright: {\textcopyright} 2021 by the authors. Licensee MDPI, Basel, Switzerland.",

year = "2021",

doi = "10.3390/molecules26185504",

language = "English",

volume = "26",

journal = "Molecules",

issn = "1420-3049",

publisher = "M D P I AG",

number = "18",

}

RIS

TY - JOUR

T1 - Polypeptide n-acetylgalactosaminyltransferase-associated phenotypes in mammals

AU - Kato, Kentaro

AU - Hansen, Lars

AU - Clausen, Henrik

PY - 2021

Y1 - 2021

N2 - Mucin-type O-glycosylation involves the attachment of glycans to an initial O-linked N-acetylgalactosamine (GalNAc) on serine and threonine residues on proteins. This process in mammals is initiated and regulated by a large family of 20 UDP-GalNAc: polypeptide N-acetylgalactosaminyl transferases (GalNAc-Ts) (EC 2.4.1.41). The enzymes are encoded by a large gene family (GALNTs). Two of these genes, GALNT2 and GALNT3, are known as monogenic autosomal recessive inherited disease genes with well characterized phenotypes, whereas a broad spectrum of phenotypes is associated with the remaining 18 genes. Until recently, the overlapping functionality of the 20 members of the enzyme family has hindered characterizing the specific biological roles of individual enzymes. However, recent evidence suggests that these enzymes do not have full functional redundancy and may serve specific purposes that are found in the different phenotypes described. Here, we summarize the current knowledge of GALNT and associated phenotypes.

AB - Mucin-type O-glycosylation involves the attachment of glycans to an initial O-linked N-acetylgalactosamine (GalNAc) on serine and threonine residues on proteins. This process in mammals is initiated and regulated by a large family of 20 UDP-GalNAc: polypeptide N-acetylgalactosaminyl transferases (GalNAc-Ts) (EC 2.4.1.41). The enzymes are encoded by a large gene family (GALNTs). Two of these genes, GALNT2 and GALNT3, are known as monogenic autosomal recessive inherited disease genes with well characterized phenotypes, whereas a broad spectrum of phenotypes is associated with the remaining 18 genes. Until recently, the overlapping functionality of the 20 members of the enzyme family has hindered characterizing the specific biological roles of individual enzymes. However, recent evidence suggests that these enzymes do not have full functional redundancy and may serve specific purposes that are found in the different phenotypes described. Here, we summarize the current knowledge of GALNT and associated phenotypes.

KW - GalNAc-T

KW - GALNT

KW - O-glycosylation

KW - Polypeptide N-acetylgalactosaminyltransferase

KW - UDP-GalNAc: polypeptide N-acetylgala ctosaminyltransferase

U2 - 10.3390/molecules26185504

DO - 10.3390/molecules26185504

M3 - Review

C2 - 34576978

AN - SCOPUS:85114953314

VL - 26

JO - Molecules

JF - Molecules

SN - 1420-3049

IS - 18

M1 - 5504

ER -

ID: 280112763