Human fetuin/alpha 2 HS glycoprotein in colloid and parenchymal cells in human fetal pituitary gland.

Abstract

An immunohistochemical study was undertaken, in an attempt to identify the acidic glycoprotein(s) present in colloid and in parenchymal cells in human fetal pituitary gland. As the colloid has been proposed to represent disintegrating cells, a series of antibodies against plasma glycoproteins and plasma proteins was applied; their presence intracellularly would generally be an indicator of plasma membrane leakage in dying parenchymal cells. In tissue sections from 9- to 20-week-old fetuses, the colloid showed prominent staining with an antibody to human fetuin/alpha 2 HS glycoprotein. Anti-alpha 2-HS glycoprotein labelled parenchymal cells in pars anterior and intermedia. Apart from a minor immunoreactivity for alpha 1 beta glycoprotein, no other plasma glycoprotein was seen in colloid or parenchymal cells. An antibody against bovine fetuin showed staining of the colloid and of some parenchymal cells in pars distalis and intermedia; the plasma and stroma of the pituitary gland were unstained. In contrast, the anti-human plasma protein antibodies all stained the stroma. The presence of alpha 2 HS glycoprotein in parenchymal cells and absence of other plasma glycoproteins imply integrity of the parenchymal cell plasma membrane. Thus, alpha 2 HS glycoprotein is either synthesized locally or taken up specifically in the parenchymal cells, which are proposed to participate in the formation of colloid. It is suggested that alpha 2 HS glycoprotein is part of a homeostatic system, which controls remodelling and physiological cell death during development.