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J. Biol. Chem., Vol. 279, Issue 53, 55271-55276, December 31, 2004

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Human Placenta Secretes Apolipoprotein B-100-containing Lipoproteins^*

Eva M. Madsen, Marie L. S. Lindegaard, Claus B. Andersen, Peter Damm¶, and Lars B. Nielsen||

From the Departments of Clinical Biochemistry and Pathology and ^¶Clinic of Obstetrics, Rigshospitalet, University of Copenhagen, DK-2100 Copenhagen, Denmark

Supply of lipids from the mother is essential for fetal growth and development. In mice, disruption of yolk sac cell secretion of apolipoprotein (apo) B-containing lipoproteins results in embryonic lethality. In humans, the yolk sac is vestigial. Nutritional functions are instead established very early during pregnancy in the placenta. To examine whether the human placenta produces lipoproteins, we examined apoB and microsomal triglyceride transfer protein (MTP) mRNA expression in placental biopsies. ApoB and MTP are mandatory for assembly and secretion of apoB-containing lipoproteins. Both genes were expressed in placenta and microsomal extracts from human placenta contained triglyceride transfer activity, indicating expression of bioactive MTP. To detect lipoprotein secretion, biopsies from term placentas were placed in medium with [³⁵S]methionine and [³⁵S]cysteine for 3–24 h. Upon sucrose gradient ultracentrifugation of the labeled medium, fractions were analyzed by apoB-immunoprecipitation. ³⁵S-labeled apoB-100 was recovered in d 1.02–1.04 g/ml particles (i.e. similar to the density of plasma low density lipoproteins). Electron microscopy of negatively stained lipoproteins secreted from placental tissue showed spherical particles with a diameter of 47 ± 10 nm. These results demonstrate that human placenta expresses both apoB and MTP and consequently synthesize and secrete apoB-100-containing lipoproteins. Placental lipoprotein formation constitutes a novel pathway of lipid transfer from the mother to the developing fetus.

Received for publication, October 6, 2004

^* The study was supported by the Danish Medical Research Council (22-03-0087). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^|| To whom correspondence should be addressed: Department of Clinical Biochemistry KB3011, Rigshospitalet, University of Copenhagen, Blegdamsvej 9, DK-2100 Copenhagen, Denmark. Tel.: 45-3545-3011; Fax: 45-3545-2524; E-mail: larsbo{at}rh.dk.

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