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Structural Heterogeneity of Glycoform of Alpha-1 Acid Glycoprotein in Alcoholic Cirrhosis Patients

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Biochemical Roles of Eukaryotic Cell Surface Macromolecules

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 842))

Abstract

Altered glycosylation of serum proteins has been reported in different pathologic conditions. Changes in glycosylation of serum proteins in disease state have been extensively used for the development of noninvasive sensitive clinical tests for diagnostic purposes. The aim of the present research was to monitor the changes of glycoform of serum alpha1-acid glycoprotein (AGP) in alcoholic liver cirrhosis (ALC) patients which could be predicted as serological marker for diagnosis. AGP was isolated from the albumin depleted pooled sera of ALC patients as well as controls by monoclonal anti-AGP affinity column. The altered glycoforms of AGP was determined by HPLC mapping followed by mass spectrometry and GALAXY database search. N-glycans released from AGP by hydrazinolysis were labeled with 2-aminopyridine and separated by three successive HPLC columns, viz., DEAE, ODS and amide silica. Significant decrease of sialylation level was observed by HPLC in ALC patients group with respect to controls. The binding of SNA with AGP was found to be less in patients group than control by ELISA and lectin blotting using Sambucus nigra agglutinin (SNA). This variation of N-linked glycoforms and decreased level of sialic acid in AGP could be valuable for the diagnosis of ALC besides clinical examination and routine laboratory investigation that could be helpful for treatment strategy.

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Abbreviations

2-PA:

2-Aminopyridine

AAT:

Alpha-1 antitrypsin

ACT:

Alpha-1 antichymotrypsin

AGP:

Alpha1-acid glycoprotein

ALC:

Alcoholic liver cirrhosis

ALT:

Alanine aminotransferase

AST:

Aspartate aminotransferase

CDT:

Carbohydrate-deficient transferrin

DEAE:

Diethylaminoethyl

GU:

Glucose unit

Hp:

Haptoglobin

ODS:

Octadecyl silica

SNA:

Sambucus nigra agglutinin

Tf:

Transferrin

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Acknowledgements

The authors sincerely thank Prof. Y. K. Chawla, Department of Hepatology, Post Graduate Institute of Medical Education and Research, Chandigarh, India for providing patients’ sera. This study was supported in part by Grants from IMS for IMS visiting Professor from abroad and the Japan Society for the Promotion of Science (JSPS) Invitational Training Program for Advanced Japanese Research Institutes. BPC and GM gratefully acknowledge the research grant (52/22/2008-BMS) provided by the Indian Council of Medical Research, New Delhi.

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Authors and Affiliations

  1. Department of Natural Sciences, West Bengal University of Technology, Salt Lake, Kolkata, 700064, India

    Goutam Mandal & Bishnu Pada Chatterjee

  2. Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-diri, Mizuho-ku, Nagoya, 4678603, Japan

    Hirokazu Yagi & Koichi Kato

  3. Institute for Molecular Science and Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, Okazaki Institute for Integrative Biosciences, 5-1 Higashiyama, Myodaiji, Okazaki, 444-8787, Japan

    Koichi Kato

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  1. Goutam Mandal
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  2. Hirokazu Yagi
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  4. Bishnu Pada Chatterjee
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Correspondence to Bishnu Pada Chatterjee .

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Editors and Affiliations

  1. Crystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, Kolkata, India

    Abhijit Chakrabarti

  2. Molecular Biophysics Unit, Indian Institute of Science, Bengaluru, India

    Avadhesha Surolia

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Mandal, G., Yagi, H., Kato, K., Chatterjee, B.P. (2015). Structural Heterogeneity of Glycoform of Alpha-1 Acid Glycoprotein in Alcoholic Cirrhosis Patients. In: Chakrabarti, A., Surolia, A. (eds) Biochemical Roles of Eukaryotic Cell Surface Macromolecules. Advances in Experimental Medicine and Biology, vol 842. Springer, Cham. https://doi.org/10.1007/978-3-319-11280-0_24

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