Immunohistochemical Localization of ECE-1 in the Human Placenta

Placenta ◽  
2000 ◽  
Vol 21 (2-3) ◽  
pp. 226-233 ◽  
Author(s):  
Z. Ahmad ◽  
S.E. Reznik
Keyword(s):  
Human Placenta ◽  
Immunohistochemical Localization

scholarly journals Immunohistochemical Localization of Carboxypeptidases E and D in the Human Placenta and Umbilical Cord

1998 ◽  
Vol 46 (12) ◽  
pp. 1359-1367 ◽  
Author(s):  
Sandra E. Reznik ◽  
Carolyn M. Salafia ◽  
Janice M. Lage ◽  
Lloyd D. Fricker
Keyword(s):  
Umbilical Cord ◽  
Human Placenta ◽  
Immunohistochemical Localization

scholarly journals Ca2+-binding protein of the human placenta. Characterization, immunohistochemical localization and functional involvement in Ca2+ transport

1985 ◽  
Vol 227 (1) ◽  
pp. 317-326 ◽  
Author(s):  
R S Tuan
Keyword(s):  
Human Placenta ◽  
Binding Protein ◽  
Biochemical Properties ◽  
Immunohistochemical Localization ◽  
Chorionic Villi ◽  
Trophoblastic Cells ◽  
Functional Involvement ◽  
Microsomal Membranes ◽  
Specific Rabbit

The Ca2+-binding protein (HCaBP) of the human placenta was studied with respect to its biochemical properties, tissue and cellular distribution, and possible involvement in placental Ca2+ transport. Optimal Ca2+ binding by the HCaBP occurs at pH 7-8 and in 100 mM-Na+ and 3 mM-Ca2+. The HCaBP possesses at least 10 Ca2+-binding sites with a Kd of 5 × 10(-6) M ([Ca2+]). Highly specific rabbit-derived anti-HCaBP antibodies were used for HCaBP immunoquantification and immunohistochemistry, which revealed that the HCaBP is localized in the chorionic villi and is primarily associated with the trophoblastic cells of the placenta. In addition, an ‘in vitro’ cell-free assay system for Ca2+ uptake was constructed with microsomal membranes isolated from term placental tissues. Ca2+ uptake by the placental microsomal fraction exhibited characteristics indicative of active Ca2+ transport such as temperature-dependence, saturability and energetic requirement. In this system, preincubation of microsomal membranes with anti-HCaBP antibodies inhibited Ca2+ uptake, suggesting that the HCaBP is functionally involved in placental membrane Ca2+ uptake.

scholarly journals Immunoelectron microscopic localization of aromatase in human placenta and ovary using microwave fixation.

1990 ◽  
Vol 38 (10) ◽  
pp. 1427-1432 ◽  
Author(s):  
H Naganuma ◽  
H Ohtani ◽  
N Harada ◽  
H Nagura
Keyword(s):  
Light Microscopy ◽  
Human Placenta ◽  
Plasma Membranes ◽  
Present Report ◽  
Immunohistochemical Localization ◽  
Full Term ◽  
Electron Microscopic ◽  
Tissue Samples ◽  
Physiological Investigation ◽  
Microwave Fixation

In this study we investigated the immunohistochemical localization of a unique aromatase, a single protein of 51,000 daltons, in the human placenta and ovary at light and electron microscopic levels. Microwave fixation was adopted for the immunoelectron microscopic study because it is an excellent method for preserving antigenicity and subcellular structures in frozen sections. Tissue samples from four immature human placentas, four full-term human placentas, and two human ovaries fixed in 10% formalin were examined by light microscopy. In addition, tissues from three full-term human placentas and one immature human placenta fixed in 4% paraformaldehyde were examined by electron microscopy. By light microscopy, immunoreactivity for this aromatase was located in the syncytiotrophoblast and a part of the cytotrophoblast of the placenta and in the lutein and granulosa cells of the ovary. Immunoelectron microscopy revealed that the aromatase antigen was localized on the surface of the microvilli, the lateral plasma membrane, and in the endoplasmic reticulum (ER) in the syncytiotrophoblast of the placenta. The positive immunoreactivity in the syncytiotrophoblast ER is consistent with previous results using antibodies for other types of aromatase, whereas the reactivity on the microvilli has not been previously described. The present report describes the fine localization of this unique aromatase in placental and ovarian tissues; its localization on the plasma membranes requires further physiological investigation.

Immunohistochemical localization of serine-protease inhibitors in the human placenta

1994 ◽  
Vol 278 (2) ◽  
pp. 283-289
Author(s):  
Mario Castellucci ◽  
Thomas Theelen ◽  
Elena Pompili ◽  
Lorenzo Fumagalli ◽  
Gabriella De Renzis ◽  
...  
Keyword(s):  
Serine Protease ◽  
Protease Inhibitors ◽  
Human Placenta ◽  
Immunohistochemical Localization ◽  
Serine Protease Inhibitors

Immunohistochemical localization of heme oxygenase-1 and bilirubin/biopyrrin of heme metabolites as antioxidants in human placenta with preeclampsia

2019 ◽  
Vol 39 (1) ◽  
pp. 33-42 ◽  
Author(s):  
Michiko Miya ◽  
Aikou Okamoto ◽  
Takashi Nikaido ◽  
Rie Tachimoto-Kawaguchi ◽  
Tadao Tanaka
Keyword(s):  
Heme Oxygenase ◽  
Human Placenta ◽  
Immunohistochemical Localization ◽  
Heme Oxygenase 1
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