関連する実験動画
Updated: Jul 6, 2026

10:37
Observing and Quantifying Fibroblast-mediated Fibrin Gel Compaction
Published on: January 16, 2014
フィブリン5は,生体内で弾性繊維の発達に不可欠なエラスティン結合タンパク質です
Hiromi Yanagisawa1, Elaine C Davis, Barry C Starcher
1Department of Molecular Biology, University of Texas Southwestern Medical Center at Dallas, Texas 75390, USA. hyanagisawa@aol.com
Nature
|January 24, 2002
まとめ
フィブリン5は,組織弾性および適切な臓器発達に不可欠な弾性繊維の組織化に不可欠です. マウスの体内には存在していないため,ヒトのカティスラキサ症候群に似た重度の結合組織疾患を引き起こす.
科学分野:
- バイオケミストリー バイオケミストリー
- 発達生物学 発達生物学とは
- 細胞生物学 細胞生物学
背景:
- 細胞外弾性繊維は,組織の弾性を提供し,細胞シグナル伝達を通じて臓器の改造に影響を与えます.
- 弾性繊維の形成には,トポエラスティン単体組立,クロスリンク,マトリックス組織が含まれ,その基礎となるメカニズムはほとんど不明です.
- フィブリン-5 (EVEC/DANCE) は,弾性繊維が豊富な組織に存在する細胞外マトリックスタンパク質です.
研究 の 目的:
- 弾性繊維の形成と組織におけるフィブリン5の役割を調査する.
- フィブリン5が弾性繊維の構造と機能に寄与する分子メカニズムを解明する.
主な方法:
- フィブリン-5のカルシウム依存性,エラスティン結合タンパク質の特徴.
- 弾性繊維におけるフィブリン-5のインビボ局所化研究.
- フィブリン-5ノックアウト (フィブリン-5-/-) マウスのフェノタイプ分析.
主要な成果:
- フィブリン5は,カルシウムに依存した方法でエラスティンを結合し,弾性繊維に局所化します.
- フィブリン5ノックアウトマウスは,組織化されていない弾性繊維によって特徴づけられる重度のエラスティノパシーを示します.
- 主要なフェノタイプには,肌のゆるさ,血管異常,肺エムフィセマトスがあり,ヒトのカティスラキサ症候群を反映しています.
結論:
- フィブリン5は,弾性繊維を組織化し,細胞に固定するための重要な支架タンパク質として機能します.
- フィブリン-5のRGDモチーフは細胞インテグリン結合を介し,EGFのリピートはエラスティンを結合する.
- フィブリン5は,組織の完全性を維持し,結合組織疾患の予防に不可欠です.
関連する概念動画
Structural Protein Function
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to form...
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to form...
Fibril-associated Collagen
Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
Elastin is Responsible for Tissue Elasticity
Elastic fiber contains the protein elastin along with lesser amounts of other proteins and glycoproteins. The main property of elastin is that it will return to its original shape after being stretched or compressed. Elastic fibers are prominent in elastic tissues found in skin and the elastic ligaments of the vertebral column.
Ligaments and tendons are made of dense regular connective tissue, but in ligaments not all fibers are parallel. Dense regular elastic tissue contains elastin fibers and...
Ligaments and tendons are made of dense regular connective tissue, but in ligaments not all fibers are parallel. Dense regular elastic tissue contains elastin fibers and...
Fibronectins Connect Cells with ECM
Fibronectin is an adhesive glycoprotein present in the extracellular matrix of embryogenic and adult tissue. These molecules primarily aid in regulating cell motility and attachment. A fibronectin molecule is composed of two identical polypeptide chains attached to each other by a pair of disulfide bonds at the C-terminal.
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...
Type IV Collagen of Basal Lamina
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 exist in...
A type IV collagen molecule has six alpha chains which can exist in...
Fibrous Proteins
Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...

