デコリンのダーマタン硫酸鎖の配列化
Yanlei Yu1, Jiana Duan2, Franklin E Leach2
1School of Food Science and Biotechnology, Zhejiang Gongshang University , Hangzhou, Zhejiang 310018, China.
Journal of the American Chemical Society
|November 8, 2017
まとめ
研究者はデコリン プロテオグリカンの複雑な構造を決定した
科学分野:
- グリコミクス
- プロテオグリカン構造
- グリコサミノグリカン分析
背景:
- 特に複雑なプロテオグリカン (PG) については,グリコシライゼーションの制御は十分に理解されていません.
- PGsのグリコサミノグリカン (GAG) サイドチェーンは構造的に複雑です.
- 以前の研究では,ビクニンPGのコンドロイチン硫酸鎖を明らかにした.
研究 の 目的:
- デコリンPGの皮膚硫酸GAG鎖の複雑な構造を決定する.
- デコリンのGAGチェーン内の構造的モチーフを特定する
- 異なるGAGの構造的複雑さを比較する.
主な方法:
- 洗練された分離技術だ
- 構成分析とドメインマッピング
- 遺伝子アルゴリズムを使った マススペクトロメトリー
主要な成果:
- デコリン皮膚硫酸GAG鎖の構造モチーフは解明された.
- これは,目立つ構造的なモチーフを持つ第二の特定されたGAGです.
- デコリンのGAGの構造は,以前予想されたより少ない.
結論:
- デコリンの皮膚硫酸GAGの構造的決定は,GAGの複雑性に関する重要な洞察を提供します.
- 構造的モチーフを特定することで,GAGの変動性の理解が簡素化されます.
- この研究は,グリコミクスとプロテオグリカンの研究の分野を前進させています.
関連する概念動画
Desmosomes
7.9K
The term desmosome derives from the Greek words "desmo" and "soma" meaning "adhesion bodies." This structure was first observed during the late 1800s and described as small, dense nodules in the epidermis. Desmosomes are button-like structures that help form an interlinked network of intermediate filaments across the cells. These junctions are essential to hold cells together under mechanical stress and to maintain tissue integrity. Desmosomes are multi-protein...
7.9K
Glycosaminoglycans
7.2K
Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
7.2K
Laminins are the Adhesive Proteins of Basal Lamina
3.5K
Laminins are heterotrimeric proteins with high molecular mass found in the extracellular matrix. Each laminin molecule is composed of three chains, viz. alpha, beta, and gamma, coded by five, four, and three paralogous genes, respectively. Laminins are categories based on the compositions of the three chains.
In humans, the five forms of alpha chains are LAMA 1, LAMA 2, LAMA 3, LAMA 4, and LAMA 5. The four forms of beta chains are LAMB 1, LAMB 2, LAMB 3, and LAMB 4. The three forms of gamma...
In humans, the five forms of alpha chains are LAMA 1, LAMA 2, LAMA 3, LAMA 4, and LAMA 5. The four forms of beta chains are LAMB 1, LAMB 2, LAMB 3, and LAMB 4. The three forms of gamma...
3.5K
Oligosaccharide Assembly
3.7K
Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Multiple sugar molecules that may or may...
3.7K
Proteoglycans
4.9K
Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
4.9K
Type IV Collagen of Basal Lamina
3.1K
Type IV collagen is a 400 nm long, network-forming collagen that acts as a barrier between the epithelial and endothelial cells. Type IV collagen forms the backbone of the basement membrane by scaffolding with laminin, entactin, proteoglycans, and fibronectin. Apart from rendering structural support to the basement membrane, it also helps entail signaling potentials necessary for both pathological and physiological functions.
A type IV collagen molecule has six alpha chains which can...
A type IV collagen molecule has six alpha chains which can...
3.1K


