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Replication of 15 loci involved in human plasma protein N-glycosylation in 4802 samples from four cohorts. / Sharapov, Sodbo Zh; Shadrina, Alexandra S.; Tsepilov, Yakov A. et al.

In: Glycobiology, Vol. 31, No. 2, 01.02.2021, p. 82-88.

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

Harvard

Sharapov, SZ, Shadrina, AS, Tsepilov, YA, Elgaeva, EE, Tiys, ES, Feoktistova, SG, Zaytseva, OO, Vuckovic, F, Cuadrat, R, Jäger, S, Wittenbecher, C, Karssen, LC, Timofeeva, M, Tillin, T, Trbojević-Akmačić, I, Štambuk, T, Rudman, N, Krištić, J, Šimunović, J, Momčilović, A, Vilaj, M, Jurić, J, Slana, A, Gudelj, I, Klarić, T, Puljak, L, Skelin, A, Kadić, AJ, Van Zundert, J, Chaturvedi, N, Campbell, H, Dunlop, M, Farrington, SM, Doherty, M, Dagostino, C, Gieger, C, Allegri, M, Williams, F, Schulze, MB, Lauc, G & Aulchenko, YS 2021, 'Replication of 15 loci involved in human plasma protein N-glycosylation in 4802 samples from four cohorts', Glycobiology, vol. 31, no. 2, pp. 82-88. https://doi.org/10.1093/glycob/cwaa053

APA

Sharapov, S. Z., Shadrina, A. S., Tsepilov, Y. A., Elgaeva, E. E., Tiys, E. S., Feoktistova, S. G., Zaytseva, O. O., Vuckovic, F., Cuadrat, R., Jäger, S., Wittenbecher, C., Karssen, L. C., Timofeeva, M., Tillin, T., Trbojević-Akmačić, I., Štambuk, T., Rudman, N., Krištić, J., Šimunović, J., ... Aulchenko, Y. S. (2021). Replication of 15 loci involved in human plasma protein N-glycosylation in 4802 samples from four cohorts. Glycobiology, 31(2), 82-88. https://doi.org/10.1093/glycob/cwaa053

Vancouver

Sharapov SZ, Shadrina AS, Tsepilov YA, Elgaeva EE, Tiys ES, Feoktistova SG et al. Replication of 15 loci involved in human plasma protein N-glycosylation in 4802 samples from four cohorts. Glycobiology. 2021 Feb 1;31(2):82-88. doi: 10.1093/glycob/cwaa053

Author

Sharapov, Sodbo Zh ; Shadrina, Alexandra S. ; Tsepilov, Yakov A. et al. / Replication of 15 loci involved in human plasma protein N-glycosylation in 4802 samples from four cohorts. In: Glycobiology. 2021 ; Vol. 31, No. 2. pp. 82-88.

BibTeX

@article{264dad500ebc4069872dce6c91acecc8,
title = "Replication of 15 loci involved in human plasma protein N-glycosylation in 4802 samples from four cohorts",
abstract = "Human protein glycosylation is a complex process, and its in vivo regulation is poorly understood. Changes in glycosylation patterns are associated with many human diseases and conditions. Understanding the biological determinants of protein glycome provides a basis for future diagnostic and therapeutic applications. Genome-wide association studies (GWAS) allow to study biology via a hypothesis-free search of loci and genetic variants associated with a trait of interest. Sixteen loci were identified by three previous GWAS of human plasma proteome N-glycosylation. However, the possibility that some of these loci are false positives needs to be eliminated by replication studies, which have been limited so far. Here, we use the largest set of samples so far (4802 individuals) to replicate the previously identified loci. For all but one locus, the expected replication power exceeded 95%. Of the 16 loci reported previously, 15 were replicated in our study. For the remaining locus (near the KREMEN1 gene), the replication power was low, and hence, replication results were inconclusive. The very high replication rate highlights the general robustness of the GWAS findings as well as the high standards adopted by the community that studies genetic regulation of protein glycosylation. The 15 replicated loci present a good target for further functional studies. Among these, eight loci contain genes encoding glycosyltransferases: MGAT5, B3GAT1, FUT8, FUT6, ST6GAL1, B4GALT1, ST3GAL4 and MGAT3. The remaining seven loci offer starting points for further functional follow-up investigation into molecules and mechanisms that regulate human protein N-glycosylation in vivo.",
keywords = "genetic association study, glycosylation, locus, replication, total plasma N-glycome",
author = "Sharapov, {Sodbo Zh} and Shadrina, {Alexandra S.} and Tsepilov, {Yakov A.} and Elgaeva, {Elizaveta E.} and Tiys, {Evgeny S.} and Feoktistova, {Sofya G.} and Zaytseva, {Olga O.} and Frano Vuckovic and Rafael Cuadrat and Susanne J{\"a}ger and Clemens Wittenbecher and Karssen, {Lennart C.} and Maria Timofeeva and Therese Tillin and Irena Trbojevi{\'c}-Akma{\v c}i{\'c} and Tamara {\v S}tambuk and Najda Rudman and Jasminka Kri{\v s}ti{\'c} and Jelena {\v S}imunovi{\'c} and Ana Mom{\v c}ilovi{\'c} and Marija Vilaj and Julija Juri{\'c} and Anita Slana and Ivan Gudelj and Thomas Klari{\'c} and Livia Puljak and Andrea Skelin and Kadi{\'c}, {Antonia Jeli{\v c}i{\'c}} and {Van Zundert}, Jan and Nishi Chaturvedi and Harry Campbell and Malcolm Dunlop and Farrington, {Susan M.} and Margaret Doherty and Concetta Dagostino and Christian Gieger and Massimo Allegri and Frances Williams and Schulze, {Matthias B.} and Gordan Lauc and Aulchenko, {Yurii S.}",
note = "Publisher Copyright: {\textcopyright} 2020 The Author(s).",
year = "2021",
month = feb,
day = "1",
doi = "10.1093/glycob/cwaa053",
language = "English",
volume = "31",
pages = "82--88",
journal = "Glycobiology",
issn = "0959-6658",
publisher = "Oxford University Press",
number = "2",

}

RIS

TY - JOUR

T1 - Replication of 15 loci involved in human plasma protein N-glycosylation in 4802 samples from four cohorts

AU - Sharapov, Sodbo Zh

AU - Shadrina, Alexandra S.

AU - Tsepilov, Yakov A.

AU - Elgaeva, Elizaveta E.

AU - Tiys, Evgeny S.

AU - Feoktistova, Sofya G.

AU - Zaytseva, Olga O.

AU - Vuckovic, Frano

AU - Cuadrat, Rafael

AU - Jäger, Susanne

AU - Wittenbecher, Clemens

AU - Karssen, Lennart C.

AU - Timofeeva, Maria

AU - Tillin, Therese

AU - Trbojević-Akmačić, Irena

AU - Štambuk, Tamara

AU - Rudman, Najda

AU - Krištić, Jasminka

AU - Šimunović, Jelena

AU - Momčilović, Ana

AU - Vilaj, Marija

AU - Jurić, Julija

AU - Slana, Anita

AU - Gudelj, Ivan

AU - Klarić, Thomas

AU - Puljak, Livia

AU - Skelin, Andrea

AU - Kadić, Antonia Jeličić

AU - Van Zundert, Jan

AU - Chaturvedi, Nishi

AU - Campbell, Harry

AU - Dunlop, Malcolm

AU - Farrington, Susan M.

AU - Doherty, Margaret

AU - Dagostino, Concetta

AU - Gieger, Christian

AU - Allegri, Massimo

AU - Williams, Frances

AU - Schulze, Matthias B.

AU - Lauc, Gordan

AU - Aulchenko, Yurii S.

N1 - Publisher Copyright: © 2020 The Author(s).

PY - 2021/2/1

Y1 - 2021/2/1

N2 - Human protein glycosylation is a complex process, and its in vivo regulation is poorly understood. Changes in glycosylation patterns are associated with many human diseases and conditions. Understanding the biological determinants of protein glycome provides a basis for future diagnostic and therapeutic applications. Genome-wide association studies (GWAS) allow to study biology via a hypothesis-free search of loci and genetic variants associated with a trait of interest. Sixteen loci were identified by three previous GWAS of human plasma proteome N-glycosylation. However, the possibility that some of these loci are false positives needs to be eliminated by replication studies, which have been limited so far. Here, we use the largest set of samples so far (4802 individuals) to replicate the previously identified loci. For all but one locus, the expected replication power exceeded 95%. Of the 16 loci reported previously, 15 were replicated in our study. For the remaining locus (near the KREMEN1 gene), the replication power was low, and hence, replication results were inconclusive. The very high replication rate highlights the general robustness of the GWAS findings as well as the high standards adopted by the community that studies genetic regulation of protein glycosylation. The 15 replicated loci present a good target for further functional studies. Among these, eight loci contain genes encoding glycosyltransferases: MGAT5, B3GAT1, FUT8, FUT6, ST6GAL1, B4GALT1, ST3GAL4 and MGAT3. The remaining seven loci offer starting points for further functional follow-up investigation into molecules and mechanisms that regulate human protein N-glycosylation in vivo.

AB - Human protein glycosylation is a complex process, and its in vivo regulation is poorly understood. Changes in glycosylation patterns are associated with many human diseases and conditions. Understanding the biological determinants of protein glycome provides a basis for future diagnostic and therapeutic applications. Genome-wide association studies (GWAS) allow to study biology via a hypothesis-free search of loci and genetic variants associated with a trait of interest. Sixteen loci were identified by three previous GWAS of human plasma proteome N-glycosylation. However, the possibility that some of these loci are false positives needs to be eliminated by replication studies, which have been limited so far. Here, we use the largest set of samples so far (4802 individuals) to replicate the previously identified loci. For all but one locus, the expected replication power exceeded 95%. Of the 16 loci reported previously, 15 were replicated in our study. For the remaining locus (near the KREMEN1 gene), the replication power was low, and hence, replication results were inconclusive. The very high replication rate highlights the general robustness of the GWAS findings as well as the high standards adopted by the community that studies genetic regulation of protein glycosylation. The 15 replicated loci present a good target for further functional studies. Among these, eight loci contain genes encoding glycosyltransferases: MGAT5, B3GAT1, FUT8, FUT6, ST6GAL1, B4GALT1, ST3GAL4 and MGAT3. The remaining seven loci offer starting points for further functional follow-up investigation into molecules and mechanisms that regulate human protein N-glycosylation in vivo.

KW - genetic association study

KW - glycosylation

KW - locus

KW - replication

KW - total plasma N-glycome

UR - http://www.scopus.com/inward/record.url?scp=85102095032&partnerID=8YFLogxK

U2 - 10.1093/glycob/cwaa053

DO - 10.1093/glycob/cwaa053

M3 - Article

C2 - 32521004

AN - SCOPUS:85102095032

VL - 31

SP - 82

EP - 88

JO - Glycobiology

JF - Glycobiology

SN - 0959-6658

IS - 2

ER -

ID: 28013088