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Microsomal triglyceride transfer protein expression in mouse intestine
Larry L Swift1, Aneta Jovanovska, Bharati Kakkad
1Department of Pathology, Vanderbilt University School of Medicine, 1161 21st Avenue South, Nashville, Tennessee, TN 37232-2561, USA. larry.swift@vanderbilt.edu
Histochemistry and Cell Biology
|May 14, 2005
Summary
Microsomal triglyceride transfer protein (MTP) and cellular retinol binding protein II (CRBPII) share similar expression patterns in the mouse small intestine, but differ from apolipoprotein B (apoB) and apoA-I. Diet influences MTP and CRBPII but not apoB/apoA-I expression.
Area of Science:
- Gastroenterology
- Molecular Biology
- Nutritional Science
Background:
- Microsomal triglyceride transfer protein (MTP) and cellular retinol binding protein II (CRBPII) are crucial for lipid absorption and transport.
- Apolipoprotein B (apoB) and apolipoprotein A-I (apoA-I) are key structural proteins involved in lipoprotein assembly and metabolism.
Purpose of the Study:
- To compare the expression patterns and regulation of MTP and CRBPII with apoB and apoA-I throughout the mouse small intestine.
- To investigate the impact of a Western diet on the expression of these proteins in different intestinal segments.
Main Methods:
- Immunohistochemical and biochemical analyses were employed to quantify protein expression.
- Expression levels were assessed along the entire length of the small intestine in mice under control and Western diet conditions.
Main Results:
- MTP and CRBPII exhibited similar expression patterns, with peak levels in the proximal intestine and a significant decrease distally.
- ApoB and apoA-I also showed peak expression in the proximal intestine, with higher residual expression in distal segments compared to MTP/CRBPII.
- A Western diet increased distal MTP and CRBPII expression, while apoB and apoA-I expression remained unaffected.
Conclusions:
- The expression and regulation of MTP and CRBPII are similar to each other but distinct from apoB and apoA-I.
- MTP expression is not directly coordinated with apoB expression, despite their shared role in chylomicron formation.