Gene/Protein Disease Symptom Drug Enzyme Compound
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Following intravenous injection, cytochrome c traverses the capillary endothelium of the rat choroid plexus and permeates the perivascular space and the extracellular space between epithelial cells. The tracer is incorporated into pinocytotic vesicles adjacent to the lateral and basal plasmalemmas. Thereafter, cytochrome c is incorporated into multivesicular and dense bodies. Tracerladen vesicles were not found to fuse with the apical plasmalemma and cytochrome c was not discharged into the cerebral ventricles. Acid phosphatase activity of the choroidal epithelium after the administration of cytochrome c was greatly increased and localized in the same intracellular sites shown for cytochrome c. These data suggest that cytochrome c and possibly other proteins that penetrate the choroidal stroma are taken up by the choroidal epithelium and subsequently degraded in lysosomal vesicles. This heterolytic mechanism may be an important means for preventing the entry of certain substances such as proteins into CSF and subsequently into nervous tissue.
Anat Rec 1975 Apr
PMID:The blood-brain barrier of the rat choroid plexus. 16 40

We previously reported that the pulmonary intravascular macrophages (PIMs) of sheep, goat, and calf lung contained a heparin and a lipolytic lipase sensitive surface coat by using tannic acid as a component of paraformaldehyde-glutaraldehyde-based fixative. The implication of this sensitivity was that the surface coat was predominantly comprised of lipoprotein-like substance. In this study we report that monastral blue (MB) used as a vascular tracer interacted with the coat globules and lost its original particulate appearance. Its precise localization in the PIMs was in combination with altered macromolecules of the surface coat in the form of lipid droplets, which conformed to the conventional view of neutral lipids. In contrast, pigment particles examined in their native state resembled metallic particles as electron-dense elliptical rods. The lipid droplets were subsequently internalized through endocytic route and found their access into the lysosomal compartments of PIMs at the electron microscopic level. Lamellar bodies (LLBs) arose from the lysosomal matrix after the entry of lipid droplets in the secondary lysosomes. Acid phosphatase activity was located in secondary lysosomes as well as in endosomes. These observations suggest that coat granules of the PIMs acted as a carrier of exogenous MB particles to deliver the complex to the lysosomal compartment where partial digestion lead to the formation of lamellar bodies. The implications of MB (cationic dye) as a vascular tracer for studying phagocytic index of PIMs in the light of their coat and the rapid development of LLBs are discussed. It is proposed that MB by initially combining with the surface coat provokes mobilization of intracellular lipid pools. In this way metabolism of vasoactive lipid in the PIMs is stimulated to influence the dynamics of pulmonary circulation in the calves.
Anat Rec 1992 Oct
PMID:In vivo monastral blue-induced lamellar-bodies in lysosomes of pulmonary intravascular macrophages (PIMs) of bovine lung: implications of the surface coat. 141 8

M cells are specialized epithelial cells over lymphoid follicles in Peyer's patches which take up viruses, bacteria, and antigenic macromolecules from the intestinal lumen. Unlike ordinary enterocytes which sequester pinocytosed material in lysosomes, M cells transport such material across the epithelium to antigen-processing areas in lymphoid follicle domes, suggesting a difference in lysosomal activity or a different route for movement of endocytic vesicles. Ileal Peyer's patches in rats were examined by electron microscopy to identify lysosomes by acid phosphatase activity. Acid phosphatase was found in dense bodies in enterocytes but not in M cells. Stereological analysis showed the volume fraction occupied by dense bodies in M cells to be 16 times less than in enterocytes (P less than .0005), even though the volume fractions of cytoplasm occupied by mitochondria in M cells and enterocytes were not significantly different. The small volume fraction of dense bodies and the absence of acid phosphatase activity in M cells thus correlate with absence of lysosomal degradation of luminal microorganisms during transport into lymphoid follicles by M cells and may provide not only a complete array of microbial antigens for initiation of immune responses, but also a route through the mucosal barrier for microorganisms which can evade local containment mechanisms.
Anat Rec 1986 Dec
PMID:Morphometric and cytochemical analysis of lysosomes in rat Peyer's patch follicle epithelium: their reduction in volume fraction and acid phosphatase content in M cells compared to adjacent enterocytes. 379 99

Little information is available concerning enzyme activity in primordial germ cells (PGCs) of the early chick embryo. The present study is designed to examine the disposition of alkaline and acid phosphatase activity in the PGCs during their migration into the developing gonads of the early chick embryo. White Leghorn chick embryos were sacrificed at daily intervals from 1 to 6 days of incubation. Following sacrifice the embryos were fixed, dehydrated, and embedded in glycol methacrylate (GMA). Alkaline and acid phosphatases were demonstrated by the simultaneous diazo-coupling method. The embryonic tissues at the different ages were examined for PGCs and the histochemical reactions for alkaline and acid phosphatases in these cells evaluated. Acid phosphatase activity did not appear within PGCs until 3 days of incubation, and then in only a few PGCs in the active phase of their migration in the dorsal mesentery, suggesting that there is no large wave of degeneration of these cells during migration. Alkaline phosphatase activity was observed as early as 2 days of incubation in PGCs during the passive phase of their migration in extraembryonic blood vessels. Alkaline phosphatase-positive PGCs in the active phase of migration were also found in the dorsal mesentery; however, the cellular localization of this enzyme differed from that observed in the passively migrating PCGs, indicating that there are alterations in the metabolic activities of these cells during the active and passive phases of migration.
Anat Rec 1982 Mar
PMID:Acid and alkaline phosphatase activity in migrating primordial germ cells of the early chick embryo. 707 83

Resorption of uncalcified cartilage in the embryonic chick femur appears to be mediated by two types of mononuclear cells. One cell type lies flattened and adherent along the surface of the cartilage matrix into which it extends cellular processes. Cytological characteristics of a large, euchromatic nucleus containing a nucleolus, and cytoplasm containing moderate to extensive amounts of rough endoplasmic reticulum indicate that these are protein synthetic cells. Macrophages, characterized by a pleomorphic shape and cytoplasm containing numerous mitochondria and vesicles, comprise the second cell type. These may be seen lying in contact with cartilage matrix, but are more likely located in the nonhematopoietic marrow adjacent to resorbing cartilage, where they establish close cellular associations with protein synthetic cells. Alkaline and acid phosphatase histochemical studies differentiate these two cellular types. Marrow alkaline phosphatase activity is restricted to the cartilage-marrow interface from which it diffuses a short distance into cartilage matrix, but does not diffuse into nearby marrow. Intracellular alkaline phosphatase is present only in protein synthetic cells that line the surface of cartilage, and thus appears to be produced by these cells. Acid phosphatase positive macrophages are scattered throughout the marrow, but are found in greatest concentrations in the region of cartilage resorption. They are rarely in direct contact with cartilage, and there is no evidence that acid phosphatase is released from these cells. The relative localizations and the presence of cellular interactions of these two cell types suggests that protein synthetic cells may be of fibroblastic origin, and may play a primary role in cartilage degradation, while macrophages, in keeping with biochemical evidence, play an adjunct or possibly a regulative role.
Anat Rec 1982 Apr
PMID:The cellular organization of fibroblastic cells and macrophages at regions of uncalcified cartilage resorption in the embryonic chick femur as revealed by alkaline and acid phosphatase histochemistry. 707 91

Ultrastructural and cytochemical methods were utilized to study the human Fallopian tube fimbrial epithelium during the different stages of the menstrual cycle. Alkaline phosphatase reaction product was located along the apical and lateral plasma membranes of the secretory cells only, regardless of the stage of the cycle. The ciliated cells were almost devoid of any reaction product at all stages of the cycle. Acid phosphatase reaction product depicted the lysosomes. These appeared as electron-dense bodies, of almost equal numbers in the ciliated and the secretory cells at all stages of the cycle. Thus the number of lysosomes did not vary appreciable during the different stages of the menstrual cycle. Many lipid droplets were found in both cells; these were rimmed by acid phosphatase reaction product, and some were partially enveloped by electron-dense bodies containing acid phosphatase deposits. Acid phosphatase deposits were also found on the inner face of Golgi vesicles.
Anat Rec 1982 May
PMID:Ultrastructural localization of alkaline and acid phosphatases in the human fallopian tube epithelium during the menstrual cycle. 710 26

An ultrastructural cytochemical study of acid phosphatase activity in the antimesometrial decidua on days 9-11 of pregnancy was performed in fed and acutely fasted mice. Specimens were fixed in a buffered mixture of paraformaldehyde and glutaraldehyde and were incubated in a buffered medium containing sodium beta-glycerophosphate and cerium chloride for ultrastructural localization of acid phosphatase activity. Fed and fasted animals showed extracellular acid phosphatase reaction product in the decidual-trophoblast interface, in the region of loosely and tightly packed, mature decidual cells, and in the region of predecidual cells. Reaction product was absent in the region of nondecidualized stromal cells. Extracellular acid phosphatase activity was more conspicuous in the region of mature decidual cells in fasted mice than in fed mice, and it was apparently similar in the region of predecidual cells in both fed and fasted mice. Acid phosphatase reaction product was also observed in lysosomes in all cells studied. Because acid phosphatase activity reflects the presence of lysosomal hydrolases in general, our results suggest that there is matrix degradation by lysosomal enzymes in both fed and fasted mice. These events may be part of the process of tissue remodeling in regions of predecidual cells and mature decidual cells. However, it is also possible that, in the region of mature decidual cells, breakdown of matrix constituents is a mechanism to provide nutrients for the growing fetus. This mechanism is probably enhanced in fasted mice.
Anat Rec 1998 09
PMID:Demonstration of extracellular acid phosphatase activity in the involuting, antimesometrial decidua in fed and acutely fasted mice by combined cytochemistry and electron microscopy. 973 39