Dipeptide transport in brush-border membrane vesicles isolated from normal term human placenta

Malliga E. Ganapathy; Virendra B. Mahesh; Lawrence D. Devoe; Frederick H. Leibach; Vadivel Ganapathy

doi:10.1016/0002-9378(85)90600-3

Dipeptide transport in brush-border membrane vesicles isolated from normal term human placenta

Malliga E. Ganapathy, Virendra B. Mahesh, Lawrence D. Devoe, Frederick H. Leibach, Vadivel Ganapathy

Maternal/Fetal Medicine

Research output: Contribution to journal › Article › peer-review

32 Scopus citations

Abstract

We studied the transport of glycylsarcosine by the brush-border membrane vesicles isolated from normal term human placentas. This dipeptide resisted hydrolysis by placental membrane vesicles and was transported intact into an osmotically responsive intravesicular space. The transport process was Na⁺-independent and probably occurred down a concentration gradient. Many peptides inhibited the transport of glycylsarcosine whereas amino acids had no effect. These results demonstrate, for the first time, the presence of a dipeptide transport system in the human placenta.

Original language	English (US)
Pages (from-to)	83-86
Number of pages	4
Journal	American journal of obstetrics and gynecology
Volume	153
Issue number	1
DOIs	https://doi.org/10.1016/0002-9378(85)90600-3
State	Published - Sep 1 1985

Keywords

Dipeptide transport
Na independence
brush-border vesicle
human placenta

ASJC Scopus subject areas

Obstetrics and Gynecology

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10.1016/0002-9378(85)90600-3

Cite this

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title = "Dipeptide transport in brush-border membrane vesicles isolated from normal term human placenta",

abstract = "We studied the transport of glycylsarcosine by the brush-border membrane vesicles isolated from normal term human placentas. This dipeptide resisted hydrolysis by placental membrane vesicles and was transported intact into an osmotically responsive intravesicular space. The transport process was Na+-independent and probably occurred down a concentration gradient. Many peptides inhibited the transport of glycylsarcosine whereas amino acids had no effect. These results demonstrate, for the first time, the presence of a dipeptide transport system in the human placenta.",

keywords = "Dipeptide transport, Na independence, brush-border vesicle, human placenta",

author = "Ganapathy, {Malliga E.} and Mahesh, {Virendra B.} and Devoe, {Lawrence D.} and Leibach, {Frederick H.} and Vadivel Ganapathy",

note = "Funding Information: From the Departments of Endocrinology, Obstetrics and Gynecology, and Cell and Molecular Biology, Medical College of Georgia. This study was supported by National Institutes of Health Grant AM 28389 to F. H. L. This is contribution No. 0887 from the Department of Cell and Mo-lecular Biology, Medical College of Georgia, Augusta, Georgia. Reprint requests: V. Ganapathy, Ph.D., Department of Cell and Mo-lecular Biology, Medical College of Georgia, Augusta, GA 30912.",

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AU - Ganapathy, Malliga E.

AU - Mahesh, Virendra B.

AU - Devoe, Lawrence D.

AU - Leibach, Frederick H.

AU - Ganapathy, Vadivel

N1 - Funding Information: From the Departments of Endocrinology, Obstetrics and Gynecology, and Cell and Molecular Biology, Medical College of Georgia. This study was supported by National Institutes of Health Grant AM 28389 to F. H. L. This is contribution No. 0887 from the Department of Cell and Mo-lecular Biology, Medical College of Georgia, Augusta, Georgia. Reprint requests: V. Ganapathy, Ph.D., Department of Cell and Mo-lecular Biology, Medical College of Georgia, Augusta, GA 30912.

PY - 1985/9/1

Y1 - 1985/9/1

N2 - We studied the transport of glycylsarcosine by the brush-border membrane vesicles isolated from normal term human placentas. This dipeptide resisted hydrolysis by placental membrane vesicles and was transported intact into an osmotically responsive intravesicular space. The transport process was Na+-independent and probably occurred down a concentration gradient. Many peptides inhibited the transport of glycylsarcosine whereas amino acids had no effect. These results demonstrate, for the first time, the presence of a dipeptide transport system in the human placenta.

AB - We studied the transport of glycylsarcosine by the brush-border membrane vesicles isolated from normal term human placentas. This dipeptide resisted hydrolysis by placental membrane vesicles and was transported intact into an osmotically responsive intravesicular space. The transport process was Na+-independent and probably occurred down a concentration gradient. Many peptides inhibited the transport of glycylsarcosine whereas amino acids had no effect. These results demonstrate, for the first time, the presence of a dipeptide transport system in the human placenta.

KW - Dipeptide transport

KW - Na independence

KW - brush-border vesicle

KW - human placenta

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Dipeptide transport in brush-border membrane vesicles isolated from normal term human placenta

Abstract

Keywords

ASJC Scopus subject areas

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