Related Experiment Video
Updated: Aug 14, 2026
08:49
Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes
Published on: March 14, 2021
Phospholipid transfer protein activity in two cholestatic patients
Eliana Cotta de Faria1, Adriana Celeste Gebrin, Wilson Nadruz Júnior
1Department of Internal Medicine, Lipids Laboratory and Experimental Medicine and Surgery Center, Faculdade de Ciências Médicas, Universidade Estadual de Campinas, Campinas, São Paulo, Brazil. cotta@fcm.unicamp.br
Sao Paulo Medical Journal = Revista Paulista De Medicina
|November 16, 2004
Summary
Plasma phospholipid transfer protein activity may decrease in cholestasis due to altered high-density lipoprotein composition and competition from lipoprotein X. This impacts lipid metabolism and cholesterol transport.
Area of Science:
- Lipidology
- Biochemistry
- Clinical Chemistry
Background:
- Plasma phospholipid transfer protein (PLTP) facilitates phospholipid transfer between lipoproteins, crucial for high-density lipoprotein (HDL) remodeling.
- This process generates lipid-poor apolipoprotein AI (apoAI) particles, efficient acceptors of cellular cholesterol.
Observation:
- Two cholestatic patients with severe hypercholesterolemia and lipoprotein X exhibited reduced PLTP activity.
- Low HDL cholesterol and high serum phospholipid levels were noted in one patient.
Findings:
- PLTP activity was near the lower limit of the reference interval in cholestatic patients.
- Cholestasis may reduce PLTP activity due to increased phospholipid content in HDL and competition from lipoprotein X.
Implications:
- Reduced PLTP activity in cholestasis could impair reverse cholesterol transport.
- Understanding PLTP's role in cholestasis may offer new therapeutic targets for lipid disorders.
More Related Videos
Related Concept Videos
01:35Asymmetric Lipid Bilayer
Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...
01:42Phosphoinositides and PIPs
Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
01:27Synthesis of Phosphatidylcholine in the ER Membrane
The ER synthesizes lipids for building cell membranes and performing cellular functions such as energy storage and signaling. The lipid synthesis machinery embedded in the ER membrane primarily collects all reactants from the cytosol. Following synthesis, the secretory pathway and the ER contact sites distribute these lipids to other cellular organelles. Additionally, the energy-rich triacylglycerides are transported from the ER via lipid droplets.
The major components of all eukaryotic cell...
The major components of all eukaryotic cell...
01:19Membrane Asymmetry Regulating Transporters
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...
01:26Effect of Hepatic Disease on Pharmacokinetics: Drug Dosing and Hepatic Blood Flow
Chronic liver disease significantly impacts drug metabolism due to alterations in hepatic blood flow and enzyme accessibility. This disruption affects the body's pharmacokinetics—the movement and processing of drugs within the system. Key enzymes crucial for metabolizing medications become less accessible, changing how drugs are processed and utilized. Furthermore, liver disease influences the synthesis of plasma proteins, such as albumin and globulins, which play critical roles in drug binding...
01:25Blood Studies for Cardiovascular System III: Serum Lipid Profile
Understanding serum lipids is crucial for maintaining cardiovascular health and preventing heart disease and stroke.
Serum lipids are fats and fatty substances in the blood and are crucial for various bodily functions, including energy storage, cellular structure, and hormone production. Serum lipids consist of cholesterol, triglycerides, and phospholipids.
Cholesterol is a soft, fat-like substance found in all body cells. It is crucial for producing hormones, vitamin D, and substances that aid...
Serum lipids are fats and fatty substances in the blood and are crucial for various bodily functions, including energy storage, cellular structure, and hormone production. Serum lipids consist of cholesterol, triglycerides, and phospholipids.
Cholesterol is a soft, fat-like substance found in all body cells. It is crucial for producing hormones, vitamin D, and substances that aid...