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The effects of androgen deprivation and estrogen stimulation on rat coagulating gland were determined by immunohistochemistry and morphometric quantification of different tissue compartments. In castrated or estrogen-treated or estrogen-treated castrated animals, the reduction of the glandular lumen is the most obvious morphological alteration, which is accompanied by an increase in stromal tissue, especially within the lamina propria. Regressive changes occur most rapidly in castrated animals (already by the end of the first week), slower in estrogen-treated castrated animals, and still slower in estrogen-treated normal animals. In castrated animals, epithelium shows a reduction of rough endoplasmic reticulum, loss of secretory blebs, and a decrease of cell size and immunoreactivity for secretory transglutaminase. The reduction of glandular lumen results from an impressive increase in connective tissue of the lamina propria. Smooth muscle cells become atrophic in castrated animals, less so in estrogen-treated animals and in castrated estrogen-treated animals. A relative increase in thickness of the smooth muscle cell layer occurs in all experimental groups and is most obvious in estrogen-treated normal animals. The proportion of myofilament and intermediate filament proteins (smooth muscle-specific actin and desmin immunoreactivities) remains nearly unaltered in these cells after hormonal challenge. A redistribution of intermediate filaments occurs forming thicker bundles within the cells. No indication for increased mitotic activity of estrogenized smooth muscle cells has been found. After castration, and after estrogen treatment, the fibroblasts and the smooth muscle cells, respectively, appear responsible for the architectural changes within the coagulating gland. Reactions of the stroma are differentially regulated after estrogen treatment and androgen deprivation. No indication for increased biosynthetic activities of smooth muscle cells has been observed in any of the experimental conditions.
Anat Rec 1993 Feb
PMID:Effects of androgen deprivation and estrogen treatment on the structure and protein expression of the rat coagulating gland. 809 91

Cross-linking defects in hair cuticle have been observed in certain rare human disorders (trichothiodystrophy, transglutaminase-deficient lamellar ichthyosis). The hypothesis being investigated is that defective cross-linking in the cuticle or other parts of the fiber is a feature of some mouse mutants in which the hair is sparse or appears structurally unsound. Pelage hair samples from 13 mouse mutants displaying defective hair were extracted with sodium dodecyl sulfate and dithiothreitol at neutral pH and examined by transmission electron microscopy. All samples were indistinguishable after extraction from normal hair fibers in appearance of the medulla and cortex. In the cortex, keratins were completely extractable, but material remaining at the cell boundaries was clearly evident. Cells of the medulla were largely unextracted, containing distinct nuclei and amorphous material in the cytoplasm. In two samples (from mice with the matted/flaky tail and naked mutations) cells of the cuticle, which readily detached from the fiber when incubated at 100 degrees C, were more extensively extracted than normal. Defective cross-linking is thus observable in a minority of mouse hair mutants. The observed perturbation of cross-linking in the cuticle was not accompanied by visible perturbation in the cortex or medulla, indicating that different proteins participate in cross-linking in the different cell types.
Anat Rec 1999 02 01
PMID:Cross-linked features of mouse pelage hair resistant to detergent extraction. 997 8

Little is known about specific proteins involved in keratinization of the epidermis of snakes, which is composed of alternating beta- and alpha-keratin layers. Using immunological techniques (immunocytochemistry and immunoblotting), the present study reports the presence in snake epidermis of proteins with epitopes that cross-react with certain mammalian cornification proteins (loricrin, filaggrin, sciellin, transglutaminase) and chick beta-keratin. alpha-keratins were found in all epidermal layers except in the hard beta- and alpha-layers. beta-keratins were exclusively present in the oberhautchen and beta-layer. After extraction and electrophoresis, alpha-keratins of 40-67 kDa in molecular weights were found. Loricrin-like proteins recorded molecular weights of 33, 50, and 58 kDa; sciellin, 55 and 62 kDa; filaggrin-like, 52 and 65 kDa; and transglutaminase, 45, 50, and 56 kDa. These results suggest that alpha-layers of snake epidermis utilize proteins with common epitopes to those present during cornification of mammalian epidermis. The beta-keratin antibody on extracts from whole snake epidermis showed a strong cross-reactive band at 13-16 kDa. No cross-reactivity was seen using an antibody against feather beta-keratin, indicating absence of a common epitope between snake and feather keratins.
Anat Rec A Discov Mol Cell Evol Biol 2005 Feb
PMID:Immunolocalization and characterization of cornification proteins in snake epidermis. 1563 76