Publication:
Glycosylation of Type I Collagen

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Issued Date

2019

Resource Type

Book Chapter

File Type

application/pdf

ISSN

10643745

DOI

10.1007/978-1-4939-9055-9_9

Other identifier(s)

2-s2.0-85068192939

Rights Holder(s)

Scopus

Bibliographic Citation

Methods in Molecular Biology. Vol 1934, (2019), p.127-144

Suggested Citation

Yamauchi M., Sricholpech M., Terajima M., Tomer K.B., Perdivara I. Glycosylation of Type I Collagen. Methods in Molecular Biology. Vol 1934, (2019), p.127-144. doi:10.1007/978-1-4939-9055-9_9 Retrieved from: https://hdl.handle.net/20.500.14740/5727

Title

Glycosylation of Type I Collagen

Author(s)

Yamauchi M.
 Sricholpech M.
 Terajima M.
 Tomer K.B.
 Perdivara I.

Abstract

Fibrillar type I collagen is the most abundant structural protein in most tissues and organs. One of the unique and functionally important characteristics of collagen is sequential posttranslational modifications of lysine (Lys) residues. In the endoplasmic reticulum, hydroxylation of specific Lys occurs producing 5-hydroxylysine (Hyl). Then, to the 5-hydroxyl group of Hyl, a single galactose unit can be attached to form galactosyl-Hyl (Gal-Hyl) and further glucose can be added to Gal-Hyl to form glucosylgalactosyl-Hyl (GlcGal-Hyl). These are the only two O-linked glycosides found in mature type I collagen. It has been shown that this modification is critically involved in a number of biological and pathological processes likely through its regulatory roles in collagen fibrillogenesis, intermolecular cross-linking, and collagen-cell interaction. Recently, with the advances in molecular/cell biology and analytical chemistry, the molecular mechanisms of collagen glycosylation have been gradually deciphered, and the type and extent of glycosylation at the specific molecular loci can now be quantitatively analyzed. In this chapter, we describe quantitative analysis of collagen glycosylation by high-performance liquid chromatography (HPLC) and semiquantitative, site-specific analysis by HPLC-tandem mass spectrometry. © 2019, Springer Science+Business Media, LLC, part of Springer Nature.

Subject(s)

Collagen type 1
 Galactose
 Glucose
 Hydroxyl group
 Hydroxylysine
 Lysine
 Structural protein
 Amino acid
 Collagen type 1
 Amino acid analysis
 Cell culture
 Cell function
 Collagen synthesis
 Controlled study
 Endoplasmic reticulum
 Enzyme activity
 High performance liquid chromatography
 Human
 Hydroxylation
 Liquid chromatography-mass spectrometry
 Protein cross linking
 Protein degradation
 Protein glycosylation
 Protein hydrolysis
 Protein processing
 Protein purification
 Quantitative analysis
 Tandem mass spectrometry
 Cell line
 Chemistry
 Glycosylation
 Hydrolysis
 Liquid chromatography
 Mass spectrometry
 Metabolism
 Protein domain
 Amino Acids
 Cell Line
 Chromatography, High Pressure Liquid
 Chromatography, Liquid
 Collagen Type I
 Glycosylation
 Hydrolysis
 Hydroxylysine
 Mass Spectrometry
 Protein Domains
 Protein Processing, Post-Translational

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URI

https://hdl.handle.net/20.500.14740/5727

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Scopus: Year 1983-2021

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