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Microsomal esterification of retinol in human liver
Acta Medica Scandinavica
|January 1, 1984
Summary
Acyl CoA: retinol acyl transferase (ARAT) facilitates retinol esterification in various tissues. This study confirms ARAT activity in human liver microsomes, indicating its physiological significance in vitamin A metabolism.
Area of Science:
- Biochemistry
- Cell Biology
- Human Physiology
Background:
- Retinol esterification is crucial for vitamin A storage and transport.
- Acyl CoA: retinol acyl transferase (ARAT) has been identified as the key enzyme in various species and tissues.
- Previous research indicated ARAT activity in rat and human small intestine, but its role in human liver was less defined.
Purpose of the Study:
- To investigate and confirm the presence and activity of Acyl CoA: retinol acyl transferase (ARAT) in human liver microsomes.
- To assess the physiological relevance of ARAT in human liver based on its enzymatic activity.
Main Methods:
- Microsomal fractions were isolated from human liver tissue.
- Enzyme assays were performed to measure the rate of retinyl ester formation.
- Incubation conditions were optimized to determine maximal enzyme activity.
Main Results:
- ARAT activity was successfully demonstrated in human liver microsomes.
- The measured rate of retinyl ester formation by ARAT was 0.37 +/- 0.31 nmole ester formed per mg microsomal protein per minute.
- This activity level suggests a significant role for the enzyme in vivo.
Conclusions:
- Acyl CoA: retinol acyl transferase (ARAT) is enzymatically active in human liver microsomes.
- The demonstrated ARAT activity supports its physiological importance in human liver vitamin A metabolism.
- Further research can explore the specific functions and regulation of ARAT in the human liver.