インテグリン結合ペプチドと成長因子の組み合わせは,電子ビームで製造されたパターンの細胞粘着を促進します
Christopher M Kolodziej1, Sung Hye Kim, Rebecca M Broyer
1Department of Chemistry and Biochemistry and the California NanoSystems Institute, University of California, Los Angeles, 607 Charles E. Young Drive South, Los Angeles, California 90095, USA.
Journal of the American Chemical Society
|December 1, 2011
まとめ
この研究では,電子ビームリトグラフィーとクリック化学を使用して細胞結合ペプチドと成長因子で細胞粘着を精密に制御し,組織工学のアプリケーションのための細胞相互作用を強化するバイオマテリアルをパターン化しています.
科学分野:
- バイオマテリアル科学 バイオマテリアル科学
- 組織工学は,組織工学である.
- 細胞生物学 細胞生物学
背景:
- エンジニアリング・スキャフォルドの細胞粘着を制御することは,バイオマテリアルと組織工学にとって極めて重要です.
- 細胞の行動を導くために,正確にパターン化されたバイオマテリアルの表面が必要である.
研究 の 目的:
- 細胞粘着リガンドと成長因子を組み合わせたパターン化されたバイオマテリアル表面を製造する.
- 人間の動脈内皮細胞の粘着と形態学に対するこれらのパターン化された表面の影響を調査する.
主な方法:
- 電子ビームリトグラフィを用いたミクロンサイズのポリエチレングリコール (PEG) ハイドロゲルの製造.
- オキシム結合形成によるアルギニン・グリシン・アスパルティック酸 (RGD) ペプチドの導入.
- 静電相互作用を用いた基礎線維細胞成長因子 (bFGF) の不動化.
主要な成果:
- 人間の静脈内皮細胞は,RGDとRGD/bFGFのパターンの表面に焦点粘着複合体を形成した.
- 細胞は,bFGFとRGDの両方が存在したときに,より大きな面積を示した.
- 制御されたマイクロ環境の中で焦点粘着の拘束が実証されています.
結論:
- 電子ビームリトグラフィーは,クリック化学と組み合わせて,細胞粘着の正確な制御を可能にします.
- 粘着性パターンの内にある成長因子を固定することで,細胞と物質の相互作用に好影響を与える.
- このアプローチは,高度な組織工学とバイオマテリアルデザインの大きな可能性を秘めています.
関連する概念動画
01:10Integrins
Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
01:17Intracellular Signaling Affects Focal Adhesions
Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Some...
01:03Anchoring Junctions
Anchoring junctions are multiprotein complexes that help cells connect to other cells and the extracellular matrix. Anchoring junctions are present on the lateral and basal surfaces of cells, providing strong and flexible connections. Focal adhesions are often formed due to cell interactions with the ECM substrata, which initiate signal transduction via kinase cascades and other mechanisms. Together, they provide stability and tissue integrity. There are three types of anchoring junctions:...
01:24Overview of Cell-Matrix Interactions
The extracellular matrix or ECM holds cells together to form a tissue and allows the cells within the tissue to communicate. ECM comprises proteins such as fibronectin, collagen, laminin, etc. The most abundant protein in this space is collagen. Collagen fibers are interwoven with carbohydrate-containing protein molecules called proteoglycans. ECM allows cell migration and provides a structural scaffold at cell adhesion that anchors the cell when the extracellular matrix proteins interact with...
01:15Activation of Integrins
Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
01:25Fibronectins 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...