Association of PAT proteins with lipid storage droplets in term fetal membranes

被引:7
作者
Ackerman, W. E.
Robinson, J. M.
Kniss, D. A. [1 ]
机构
[1] Ohio State Univ, Coll Med, Dept Obstet & Gynecol, Div Maternal Fetal Med, Columbus, OH 43210 USA
[2] Ohio State Univ, Coll Med, Lab Perinatal Res, Columbus, OH 43210 USA
[3] Ohio State Univ, Coll Med, Dept Physiol & Cell Biol, Columbus, OH 43210 USA
[4] Ohio State Univ, Coll Med, Biomed Engn Ctr, Columbus, OH 43210 USA
关键词
lipid storage droplets; placental membranes; perilipin; tail-interacting protein of 47 kilodaltons; adipose differentiation-related protein;
D O I
10.1016/j.placenta.2006.06.009
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
As depots for neutral lipids, lipid storage droplets (LDs) accumulate with advancing gestation within the fetal membranes. Little is currently known about the proteins associated with the LDs of these cells. The PAT family [perilipin, adipose differentiation-related protein (ADRP), and tail-interacting protein of 47 kilodaltons (TIP47)] represents a unique group of proteins thought to contribute to LD formation and function. We examined the association of each of the PAT proteins with LDs of term fetal membranes. We found that large LDs of amnion epithelial cells were reactive for neutral lipid stains and simultaneously encoated with ADRP and TIP47, but not perilipin. Within the remaining cell types, LDs were frequently co-labeled with antibodies recognizing ADRP and TIP47; however, in cells harboring only small LDs, the majority of TIP47 labeling was cytoplasmic. Structures labeled with perilipin antibodies were present only in chorion laeve trophoblasts. Gene and protein expression analyses suggested this to be a small molecular weight perilipin isoform, such as that seen in steroidogenic cells. We conclude that LDs are heterogeneous among differing cell types of the fetal membranes. Subclassification of LDs based on associated proteins suggests that these organelles may serve specialized functions within individual cells. (c) 2006 Elsevier Ltd. All rights reserved.
引用
收藏
页码:465 / 476
页数:12
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