Document Detail

Immunocytochemical localization of annexins V and VI in human placentae of different gestational ages.
MedLine Citation:
PMID:  8012449     Owner:  NLM     Status:  MEDLINE    
The cellular and subcellular localization of annexins V and VI, two members of a superfamily of Ca(2+)-dependent phospholipid- and membrane-binding proteins, was investigated in chorionic villi of human placentae of different gestational ages by postembedding immunocytochemistry at the electron microscope level. All cell types of placental villi, i.e., the syncytiotrophoblast, Langhans cells, Hofbauer cells, fibroblasts, and capillary endothelial cells, appeared to express the two proteins, irrespective of the gestational age. By immunogold particle counts, annexin V was observed to be 2-3 times as much abundant as annexin VI. Syncytiotrophoblast cells appeared to contain the largest amounts and Langhans cells appeared to contain the least amounts of annexins V and VI, as judged by immunocytochemistry. The two proteins were found associated with plasma, Golgi, and vacuolar membranes, and with membranes of the endoplasmic reticulum, as well as diffusely in the cytoplasm. Annexin V appeared to be distributed in nearly equal proportions between cell membranes and the cytoplasm in stromal cells and to be about 30% associated with cell membranes in trophoblast cells, whereas annexin VI appeared almost equally distributed between cell membranes and the cytoplasm in trophoblast and stromal cells. Also, annexins V and VI appeared to be more abundant in trophoblast cells than in stromal cells. The present data strongly support the idea that placenta is a preferential site of annexin-regulated activities, and suggest that annexins V and VI are actively involved in the Ca(2+)-dependent regulation of membrane processes in trophoblast cells.
M G Rambotti; A Spreca; R Donato
Related Documents :
24220859 - A morphometric analysis of the phloem-unloading pathway in developing tobacco leaves.
12535069 - The bacterial linear motor of spiroplasma melliferum bc3: from single molecules to swim...
23666819 - Tuning scaffold mechanics by laminating native extracellular matrix membranes and effec...
23139869 - A functioning artificial secretory cell.
24519419 - Localization of cacna1s to on bipolar dendritic tips requires mglur6-related cascade el...
23612159 - Evaluation of intracellular lipid bodies in chlamydomonas reinhardtii strains by flow c...
6538879 - Intracellular control of axial shape in non-uniform neurites: a serial electron microsc...
7259639 - Haemagglutinins and lysins in plants and their application in characterising human and ...
19596699 - Identification and localization of the bilitranslocase homologue in white grape berries...
Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Cellular & molecular biology research     Volume:  39     ISSN:  0968-8773     ISO Abbreviation:  Cell. Mol. Biol. Res.     Publication Date:  1993  
Date Detail:
Created Date:  1994-07-28     Completed Date:  1994-07-28     Revised Date:  2012-02-27    
Medline Journal Info:
Nlm Unique ID:  9316986     Medline TA:  Cell Mol Biol Res     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  579-88     Citation Subset:  IM    
Department of Experimental Medicine and Biochemical Sciences, University of Perugia, Italy.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Annexin A5 / analysis*
Annexin A6 / analysis*
Calcium / metabolism
Chorionic Villi / chemistry*
Gestational Age
Membrane Proteins / analysis
Pregnancy Proteins / analysis*
Subcellular Fractions / chemistry
Trophoblasts / chemistry
Grant Support
Reg. No./Substance:
0/Annexin A5; 0/Annexin A6; 0/Membrane Proteins; 0/Pregnancy Proteins; 7440-70-2/Calcium

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  INO2, a regulatory gene in yeast phospholipid biosynthesis, affects nuclear segregation and bud patt...
Next Document:  Endotoxin alters the expression of extracellular matrix proteins by cultured endothelial cells.