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Detection and verification of glycosylation patterns of glycoproteins from clinical specimens using lectin microarrays and lectin-based immunosorbent assays

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Detection and verification of glycosylation patterns of glycoproteins from clinical specimens using lectin microarrays and lectin-based immunosorbent assays. / Li, Yan; Tao, Sheng Ce; Bova, G. Steven; Liu, Alvin Y.; Chan, Daniel W.; Zhu, Heng; Zhang, Hui.

In: Analytical Chemistry, Vol. 83, No. 22, 15.11.2011, p. 8509-8516.

Research output: Contribution to journalArticleScientificpeer-review

Harvard

Li, Y, Tao, SC, Bova, GS, Liu, AY, Chan, DW, Zhu, H & Zhang, H 2011, 'Detection and verification of glycosylation patterns of glycoproteins from clinical specimens using lectin microarrays and lectin-based immunosorbent assays', Analytical Chemistry, vol. 83, no. 22, pp. 8509-8516. https://doi.org/10.1021/ac201452f

APA

Li, Y., Tao, S. C., Bova, G. S., Liu, A. Y., Chan, D. W., Zhu, H., & Zhang, H. (2011). Detection and verification of glycosylation patterns of glycoproteins from clinical specimens using lectin microarrays and lectin-based immunosorbent assays. Analytical Chemistry, 83(22), 8509-8516. https://doi.org/10.1021/ac201452f

Vancouver

Author

Li, Yan ; Tao, Sheng Ce ; Bova, G. Steven ; Liu, Alvin Y. ; Chan, Daniel W. ; Zhu, Heng ; Zhang, Hui. / Detection and verification of glycosylation patterns of glycoproteins from clinical specimens using lectin microarrays and lectin-based immunosorbent assays. In: Analytical Chemistry. 2011 ; Vol. 83, No. 22. pp. 8509-8516.

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@article{7e6b6621cc114fb9bcc61c62da2a6edd,
title = "Detection and verification of glycosylation patterns of glycoproteins from clinical specimens using lectin microarrays and lectin-based immunosorbent assays",
abstract = "Aberrant glycosylation is a fundamental characteristic of progression of diseases such as cancer. Therefore, characterization of glycosylation patterns of proteins from disease tissues may identify changes specific to the disease development and improve diagnostic performance. Thus, analysis strategies with sufficient sensitivity for evaluation of glycosylation patterns in clinical specimens are needed. Here, we describe an analytical strategy for detection and verification of glycosylation patterns. It is based on a two-phase platform including a pattern discovery phase to identify the glycosylation changes using high-density lectin microarrays and a verification phase by developing lectin-based immunosorbent assays using the identified lectins. We evaluated the analytical performance of the platform using the glycoprotein standard and found that the lectin microarray could detect specific bindings of glycoprotein to lectins at the nanogram level and the lectin-based immunosorbent assay could be used for verification of protein glycosylation. We then applied the approach to the analysis of glycosylation patterns of two glycoproteins, which are highly expressed in prostate cancer in our prior studies, prostate specific antigen (PSA) and membrane metallo-endopeptidase (MME), from aggressive (AC) and nonaggressive prostate cancer (NAC) tissues. The observed differences in glycosylation patterns of PSA and MME may represent a significant clinical importance and could be used to develop multiplex assays for diagnosis of aggressive prostate cancer.",
author = "Yan Li and Tao, {Sheng Ce} and Bova, {G. Steven} and Liu, {Alvin Y.} and Chan, {Daniel W.} and Heng Zhu and Hui Zhang",
year = "2011",
month = "11",
day = "15",
doi = "10.1021/ac201452f",
language = "English",
volume = "83",
pages = "8509--8516",
journal = "Analytical Chemistry",
issn = "0003-2700",
publisher = "AMER CHEMICAL SOC",
number = "22",

}

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TY - JOUR

T1 - Detection and verification of glycosylation patterns of glycoproteins from clinical specimens using lectin microarrays and lectin-based immunosorbent assays

AU - Li, Yan

AU - Tao, Sheng Ce

AU - Bova, G. Steven

AU - Liu, Alvin Y.

AU - Chan, Daniel W.

AU - Zhu, Heng

AU - Zhang, Hui

PY - 2011/11/15

Y1 - 2011/11/15

N2 - Aberrant glycosylation is a fundamental characteristic of progression of diseases such as cancer. Therefore, characterization of glycosylation patterns of proteins from disease tissues may identify changes specific to the disease development and improve diagnostic performance. Thus, analysis strategies with sufficient sensitivity for evaluation of glycosylation patterns in clinical specimens are needed. Here, we describe an analytical strategy for detection and verification of glycosylation patterns. It is based on a two-phase platform including a pattern discovery phase to identify the glycosylation changes using high-density lectin microarrays and a verification phase by developing lectin-based immunosorbent assays using the identified lectins. We evaluated the analytical performance of the platform using the glycoprotein standard and found that the lectin microarray could detect specific bindings of glycoprotein to lectins at the nanogram level and the lectin-based immunosorbent assay could be used for verification of protein glycosylation. We then applied the approach to the analysis of glycosylation patterns of two glycoproteins, which are highly expressed in prostate cancer in our prior studies, prostate specific antigen (PSA) and membrane metallo-endopeptidase (MME), from aggressive (AC) and nonaggressive prostate cancer (NAC) tissues. The observed differences in glycosylation patterns of PSA and MME may represent a significant clinical importance and could be used to develop multiplex assays for diagnosis of aggressive prostate cancer.

AB - Aberrant glycosylation is a fundamental characteristic of progression of diseases such as cancer. Therefore, characterization of glycosylation patterns of proteins from disease tissues may identify changes specific to the disease development and improve diagnostic performance. Thus, analysis strategies with sufficient sensitivity for evaluation of glycosylation patterns in clinical specimens are needed. Here, we describe an analytical strategy for detection and verification of glycosylation patterns. It is based on a two-phase platform including a pattern discovery phase to identify the glycosylation changes using high-density lectin microarrays and a verification phase by developing lectin-based immunosorbent assays using the identified lectins. We evaluated the analytical performance of the platform using the glycoprotein standard and found that the lectin microarray could detect specific bindings of glycoprotein to lectins at the nanogram level and the lectin-based immunosorbent assay could be used for verification of protein glycosylation. We then applied the approach to the analysis of glycosylation patterns of two glycoproteins, which are highly expressed in prostate cancer in our prior studies, prostate specific antigen (PSA) and membrane metallo-endopeptidase (MME), from aggressive (AC) and nonaggressive prostate cancer (NAC) tissues. The observed differences in glycosylation patterns of PSA and MME may represent a significant clinical importance and could be used to develop multiplex assays for diagnosis of aggressive prostate cancer.

UR - http://www.scopus.com/inward/record.url?scp=81255146498&partnerID=8YFLogxK

U2 - 10.1021/ac201452f

DO - 10.1021/ac201452f

M3 - Article

VL - 83

SP - 8509

EP - 8516

JO - Analytical Chemistry

JF - Analytical Chemistry

SN - 0003-2700

IS - 22

ER -