フェニララニンは膜の透過性を増加させる
Russell Perkins1, Veronica Vaida1
1University of Colorado Boulder , 215 UCB, Boulder, Colorado 80309, United States.
Journal of the American Chemical Society
|October 3, 2017
まとめ
アミノ酸フェニララニンは生体膜の透過性を高める. この発見は,フェニルケトヌーリアの有害な症状を説明する可能性があります.フェニララニンの高いレベルを引き起こす遺伝的疾患です.
科学分野:
- 生物化学
- 細胞生物学
- 神経科学
背景:
- 生物学的な膜は 化学成分の分布を制御することで 細胞のプロセスを制御します
- 膜の透過性は,代謝 (電子伝達) と神経細胞機能 (信号伝達) に不可欠である.
研究 の 目的:
- アミノ酸フェニララニンの生物学的膜透過性への影響を調査する.
- フェニララニン誘発の透過性変化とフェニルケトヌーリアの症状の間の潜在的な関連を調べる.
主な方法:
- この研究では,フェニララニンの存在下で膜の透過性を測定する実験が行われた可能性が高い.
- フェニララニンの膜特性への影響の分析
主要な成果:
- フェニララニンは生体膜の透過性を高めることが判明した.
- この増加は,フェニララニンの高い状態で観察された有害作用の潜在的なメカニズムです.
結論:
- フェニララニンのレベルが上昇すると,透過性が増加し,膜機能が変化する可能性があります.
- このメカニズムは,フェニルケトヌーリアの病理生理学への洞察を提供します.
関連する概念動画
Bioavailability Enhancement: Drug Permeability Enhancement
248
Body:After oral administration, poor permeability often limits the rate at which drugs are absorbed through the intestinal epithelium. Enhancing drug permeability is crucial for effective therapy, and several strategies have been developed to overcome this challenge.One effective strategy involves the use of lipid-based formulations. These formulations enhance dissolution and solubility, targeting physiological mechanisms to increase drug absorption. This includes stimulating bile salt...
248
Protein Diffusion in the Membrane
6.0K
Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
6.0K
Membrane Fluidity
17.0K
Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
Mosaic nature of the membrane
The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is...
Mosaic nature of the membrane
The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is...
17.0K
Membrane Fluidity
176.7K
Cell membranes are composed of phospholipids, proteins, and carbohydrates loosely attached to one another through chemical interactions. Molecules are generally able to move about in the plane of the membrane, giving the membrane its flexible nature called fluidity. Two other features of the membrane contribute to membrane fluidity: the chemical structure of the phospholipids and the presence of cholesterol in the membrane.
176.7K
Membrane Asymmetry Regulating Transporters
7.5K
Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
7.5K
Multi-pass Transmembrane Proteins and β-barrels
6.7K
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
6.7K


