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Dipeptide transport in brush-border membrane vesicles isolated from normal term human placenta
American Journal of Obstetrics and Gynecology
|September 1, 1985
Summary
Human placenta transports glycylsarcosine, a dipeptide, intact via a sodium-independent system. This study identifies a novel dipeptide transport system in the human placenta, crucial for nutrient transfer.
Area of Science:
- Obstetrics and Gynecology
- Human Physiology
- Biochemistry
Background:
- The human placenta facilitates nutrient and waste exchange between mother and fetus.
- Understanding placental transport mechanisms is vital for fetal development and health.
Purpose of the Study:
- To investigate the transport of the dipeptide glycylsarcosine across the human placental brush-border membrane.
- To characterize the properties of this transport system.
Main Methods:
- Isolation of brush-border membrane vesicles from normal term human placentas.
- Assay of glycylsarcosine uptake into these vesicles.
- Investigation of transport kinetics and substrate specificity.
Main Results:
- Glycylsarcosine was transported intact and resisted hydrolysis by placental vesicles.
- Transport was sodium-independent and appeared to follow a concentration gradient.
- Other dipeptides inhibited glycylsarcosine transport, while amino acids did not.
Conclusions:
- The human placenta possesses a distinct dipeptide transport system.
- This system is separate from amino acid transporters.
- This finding represents the first evidence of a specific dipeptide transporter in the human placenta.