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Immunohistochemical localization of fibrillin in developing macaque and term human placentas and fetal membranes
Author(s) -
King Barry F.,
Blankenship Thomas N.
Publication year - 1997
Publication title -
microscopy research and technique
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.536
H-Index - 118
eISSN - 1097-0029
pISSN - 1059-910X
DOI - 10.1002/(sici)1097-0029(19970701/15)38:1/2<42::aid-jemt6>3.0.co;2-w
Subject(s) - staining , biology , cytotrophoblast , fibrillin , pathology , connective tissue , extracellular matrix , placenta , fetus , microbiology and biotechnology , medicine , pregnancy , genetics
The objective of this study was to examine the developmental appearance of the extracellular matrix glycoprotein fibrillin in macaque placentas and fetal membranes and to compare this distribution to that seen in term human placentas and fetal membranes. Standard immunoperoxidase methods were used on paraformaldehyde‐fixed, paraffin‐embedded tissues. At early gestational ages (26–30 days), fibrillin was found in cell columns and cytotrophoblastic shell, with weak staining in the villous stroma. Staining was abundant in the shell and columns at 53 days as well, and stronger staining was seen in the stroma of the chorionic plate and stem villi. Staining in the shell and remnants of the cell columns in later gestation continued to be positive, though variable. Generally, the strongest staining was present in the distal cytotrophoblastic shell. Stroma in the tips of anchoring villi was also strongly positive. Later in gestation, fibrillin was observed around the multilayered cytotrophoblast of the chorionic plate. Fibrillin was abundant in the stromal cores of human term placental villi. In early macaque amnion, fibrillin staining was abundant in a layer beneath the amniotic epithelium. Later in gestation, macaque chorioamnion staining was generally similar to human term chorioamnion staining, with the heaviest staining in portions of the compact and reticular layers. Fibrillin was sometimes localized in regions known to be rich in connective tissue microfibrils, but, in other regions known to have abundant microfibrils, fibrillin staining was weak. This suggests that some microfibrils in placenta may be composed predominantly of some other protein(s). The function of fibrillin in the various placental compartments is unknown at present. It may provide attachment points for cells while at the same time providing a strong, yet flexible, matrix to accommodate growth particularly in areas subject to shear stress. Microsc. Res. Tech. 38:42–51, 1997. © 1997 Wiley‐Liss, Inc.