Site-specific protein O-glycosylation modulates proprotein processing - Deciphering specific functions of the large polypeptide GalNAc-transferase gene family

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Standard

Site-specific protein O-glycosylation modulates proprotein processing - Deciphering specific functions of the large polypeptide GalNAc-transferase gene family. / Schjoldager, Katrine Ter-Borch Gram; Clausen, Henrik.

I: BBA General Subjects, Bind 1820, Nr. 12, 09.2012, s. 2079-94.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Schjoldager, KT-BG & Clausen, H 2012, 'Site-specific protein O-glycosylation modulates proprotein processing - Deciphering specific functions of the large polypeptide GalNAc-transferase gene family', BBA General Subjects, bind 1820, nr. 12, s. 2079-94. https://doi.org/10.1016/j.bbagen.2012.09.014

APA

Schjoldager, K. T-B. G., & Clausen, H. (2012). Site-specific protein O-glycosylation modulates proprotein processing - Deciphering specific functions of the large polypeptide GalNAc-transferase gene family. BBA General Subjects, 1820(12), 2079-94. https://doi.org/10.1016/j.bbagen.2012.09.014

Vancouver

Schjoldager KT-BG, Clausen H. Site-specific protein O-glycosylation modulates proprotein processing - Deciphering specific functions of the large polypeptide GalNAc-transferase gene family. BBA General Subjects. 2012 sep.;1820(12):2079-94. https://doi.org/10.1016/j.bbagen.2012.09.014

Author

Schjoldager, Katrine Ter-Borch Gram ; Clausen, Henrik. / Site-specific protein O-glycosylation modulates proprotein processing - Deciphering specific functions of the large polypeptide GalNAc-transferase gene family. I: BBA General Subjects. 2012 ; Bind 1820, Nr. 12. s. 2079-94.

Bibtex

@article{8512269ecd774436b3f1a0bfece1560d,
title = "Site-specific protein O-glycosylation modulates proprotein processing - Deciphering specific functions of the large polypeptide GalNAc-transferase gene family",
abstract = "Posttranslational modifications (PTMs) greatly expand the function and regulation of proteins, and glycosylation is the most abundant and diverse PTM. Of the many different types of protein glycosylation, one is quite unique; GalNAc-type (or mucin-type) O-glycosylation, where biosynthesis is initiated in the Golgi by up to twenty distinct UDP-N-acetyl-a-d-galactosamine:polypeptide N-acetylgalactosaminyltransferases (GalNAc-Ts). These GalNAc-Ts are differentially expressed in cells and have different (although partly overlapping) substrate specificities, which provide for both unique functions and considerable redundancy. Recently we have begun to uncover human diseases associated with deficiencies in GalNAc-T genes (GALNTs). Thus deficiencies in individual GALNTs produce cell and protein specific effects and subtle distinct phenotypes such as hyperphosphatemia with hyperostosis (GALNT3) and dysregulated lipid metabolism (GALNT2). These phenotypes appear to be caused by deficient site-specific O-glycosylation that co-regulates proprotein convertase (PC) processing of FGF23 and ANGPTL3, respectively.",
author = "Schjoldager, {Katrine Ter-Borch Gram} and Henrik Clausen",
note = "Copyright {\textcopyright} 2012 Elsevier B.V. All rights reserved.",
year = "2012",
month = sep,
doi = "10.1016/j.bbagen.2012.09.014",
language = "English",
volume = "1820",
pages = "2079--94",
journal = "B B A - General Subjects",
issn = "0304-4165",
publisher = "Elsevier",
number = "12",

}

RIS

TY - JOUR

T1 - Site-specific protein O-glycosylation modulates proprotein processing - Deciphering specific functions of the large polypeptide GalNAc-transferase gene family

AU - Schjoldager, Katrine Ter-Borch Gram

AU - Clausen, Henrik

N1 - Copyright © 2012 Elsevier B.V. All rights reserved.

PY - 2012/9

Y1 - 2012/9

N2 - Posttranslational modifications (PTMs) greatly expand the function and regulation of proteins, and glycosylation is the most abundant and diverse PTM. Of the many different types of protein glycosylation, one is quite unique; GalNAc-type (or mucin-type) O-glycosylation, where biosynthesis is initiated in the Golgi by up to twenty distinct UDP-N-acetyl-a-d-galactosamine:polypeptide N-acetylgalactosaminyltransferases (GalNAc-Ts). These GalNAc-Ts are differentially expressed in cells and have different (although partly overlapping) substrate specificities, which provide for both unique functions and considerable redundancy. Recently we have begun to uncover human diseases associated with deficiencies in GalNAc-T genes (GALNTs). Thus deficiencies in individual GALNTs produce cell and protein specific effects and subtle distinct phenotypes such as hyperphosphatemia with hyperostosis (GALNT3) and dysregulated lipid metabolism (GALNT2). These phenotypes appear to be caused by deficient site-specific O-glycosylation that co-regulates proprotein convertase (PC) processing of FGF23 and ANGPTL3, respectively.

AB - Posttranslational modifications (PTMs) greatly expand the function and regulation of proteins, and glycosylation is the most abundant and diverse PTM. Of the many different types of protein glycosylation, one is quite unique; GalNAc-type (or mucin-type) O-glycosylation, where biosynthesis is initiated in the Golgi by up to twenty distinct UDP-N-acetyl-a-d-galactosamine:polypeptide N-acetylgalactosaminyltransferases (GalNAc-Ts). These GalNAc-Ts are differentially expressed in cells and have different (although partly overlapping) substrate specificities, which provide for both unique functions and considerable redundancy. Recently we have begun to uncover human diseases associated with deficiencies in GalNAc-T genes (GALNTs). Thus deficiencies in individual GALNTs produce cell and protein specific effects and subtle distinct phenotypes such as hyperphosphatemia with hyperostosis (GALNT3) and dysregulated lipid metabolism (GALNT2). These phenotypes appear to be caused by deficient site-specific O-glycosylation that co-regulates proprotein convertase (PC) processing of FGF23 and ANGPTL3, respectively.

U2 - 10.1016/j.bbagen.2012.09.014

DO - 10.1016/j.bbagen.2012.09.014

M3 - Journal article

C2 - 23022508

VL - 1820

SP - 2079

EP - 2094

JO - B B A - General Subjects

JF - B B A - General Subjects

SN - 0304-4165

IS - 12

ER -

ID: 41808802