Increased content of annexin II (p36) and p11 in human placenta brush-border membrane vesicles during syncytiotrophoblast maturation and differentiation

被引:29
作者
KaczanBourgois, D
Salles, JP
Hullin, F
Fauvel, J
Moisand, A
DugaNeulat, I
Berrebi, A
Campistron, G
Chap, H
机构
[1] HOP PURPAN,INSERM U326,TOULOUSE,FRANCE
[2] CNRS,PHARMACOL & TOXICOL FONDAMENTALES LAB,TOULOUSE,FRANCE
[3] HOP PURPAN,ANAT PATHOL LAB,TOULOUSE,FRANCE
[4] HOP LA GRAVE,DEPT OBSTET GYNECOL,TOULOUSE,FRANCE
[5] UNIV TOULOUSE 3,FAC PHARMACEUT SCI,SERV PHYSIOL,F-31062 TOULOUSE,FRANCE
关键词
D O I
10.1016/S0143-4004(96)80017-8
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
Annexins are a group of proteins abundant in placental membranes a here they may play diverse functional roles. Annexins are expressed in high levels in mature placenta but little is known about their presence at very early stages of gestation and later. We used the model of brush-border membrane vesicles (BBMV) at different stages of gestation to assess precise localization of some of these proteins in syncytiotrophoblast apical membrane and to determine their appearance along the maturation process of placenta. Here rue describe annexins type I, II, IV, V and VI which are present all along gestation in BBMV. Annexin II (p36) is present with the S100 like calcium-binding protein p11 in BBMV, where they can constitute heterotetrameric forms of annexin II linked to cytoskeleton structures. No variation of annexins I, IV and VI content was observed in BBMV along pregnancy. Annexin V undergoes significant decrease after 12th week, which could be related to local anticoagulant activity. Levels of annexin II and p11 increased progressively during gestation suggesting that heterotetrameric forms of annexin II play a role in the differentiation process of placenta and in function of the mature microvilli. (C) 1996 W. B. Saunders Company Ltd
引用
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页码:669 / 676
页数:8
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