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Plasma membrane fatty acid-binding protein (FABPpm) is exclusively located in the maternal facing membranes of the human placenta.
- Source :
-
FEBS letters [FEBS Lett] 1995 Nov 20; Vol. 375 (3), pp. 227-30. - Publication Year :
- 1995
-
Abstract
- We reported earlier the presence of a 40 kDa plasma membrane fatty acid-binding protein (FABPpm) in human placenta. This protein is thought to be involved in the sequestration of unesterified free fatty acids bound to albumin from the maternal plasma for delivery to the fetus. However, its location in human placental syncytiotrophoblasts is not known. These cells are bipolar; one side facing maternal circulation (microvillous membranes), and the other side facing fetal circulation (basal membranes). Therefore, it is important to resolve the location of this protein in trophoblast membranes in order to understand fatty acid transport and metabolism in human placenta. Isolated plasma membranes vesicles were prepared respectively from the maternal facing microvillous and fetal facing surface of the human full-term placental syncytiotrophoblast. Using these membrane preparations, fatty acid binding activity, the polyacrylamide gel electrophoresis radiobinding assay for FABPpm, and Western blot analysis of FABPpm were carried out to determine the location of this protein in these membranes. Based on the above studies we conclude that the FABPpm is located exclusively in the microvillous membranes. Since FABPpm may be responsible for FFA uptake, its location in the microvillous membranes favours the unidirectional flow of maternal FFA to the fetus.
- Subjects :
- Autoradiography
Binding Sites
Blotting, Western
Carbon Radioisotopes
Carrier Proteins analysis
Carrier Proteins isolation & purification
Cell Membrane metabolism
Dihydroalprenolol metabolism
Fatty Acid-Binding Protein 7
Fatty Acid-Binding Proteins
Female
Fetus
Humans
Linoleic Acid
Linoleic Acids metabolism
Molecular Weight
Myelin P2 Protein analysis
Myelin P2 Protein isolation & purification
Oleic Acid
Oleic Acids metabolism
Pregnancy
Trophoblasts metabolism
Carrier Proteins metabolism
Myelin P2 Protein metabolism
Neoplasm Proteins
Placenta metabolism
Tumor Suppressor Proteins
Subjects
Details
- Language :
- English
- ISSN :
- 0014-5793
- Volume :
- 375
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 7498505
- Full Text :
- https://doi.org/10.1016/0014-5793(95)01216-2