Gene/Protein Disease Symptom Drug Enzyme Compound
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The epithelium of the guinea pig yolk sac is involved in the selective transport of macromolecules to the fetus. We studied the compartments involved in sorting and transepithelial transport of protein tracers and the effect of lowered temperature (18 degrees C) on these events. Explants of yolk sac were incubated with a mixture of cationized ferritin (CF) and horseradish peroxidase (HRP, Sigma type VI). At 4 degrees C, both tracers were bound to the cell surface and binding of an HRP-gold complex was shown to be inhibited by mannan. At 37 degrees C and 18 degrees C, both tracers were taken up into tubules and vesicles in the apical cytoplasm. Usually the tubules contained a mixture of tracers, but they often showed a polarized distribution with CF and HRP at opposite ends. The vesicles also contained mixtures of the tracers, but some contained only one. In addition, there were some irregularly shaped vacuoles composed of saccules that contained either a mixture, HRP alone, or CF alone. These results suggest that these adsorbed ligands are binding to unique microdomains of the endocytic complex. After 20 min at 37 degrees C coated vesicles 100 nm in diameter were located in the apical cytoplasm and coated vesicles of the same size were located at the lateral cell membrane. Usually they contained only HRP or CF, although occasional mixtures were seen. At 18 degrees C, HRP was transported across the cells in 100 nm vesicles. However, transport of CF was completely inhibited at the lower temperature.(ABSTRACT TRUNCATED AT 250 WORDS)
Anat Rec 1986 Sep
PMID:Sorting and transepithelial transport of adsorbed protein tracers: effects of temperature. 376

Endocytosis from apical and basolateral cell membranes of mouse blastocyst trophectoderm was examined morphologically by using unconjugated horseradish peroxidase (HRP, fluid phase marker), cationized ferritin (membrane marker, bound ionically), and protein A-HRP conjugate (membrane marker, identifying antigens recognised by antimouse species serum). The markers were applied in single and double labelling procedures designed to reveal the derivation, sorting site, and fate of all the major endocytic pathways. Endocytosis at the apical surface led to the obligate fusion of labelled elements with prelysosomal endosomes prior to the redistribution of membrane into lysosomal, transcellular, or recycling pathways, and to the passage of internalised fluid into lysosomes only. Complementary routes appear to operate following endocytosis at the basolateral domain. Thus, endocytic trafficking within the trophectoderm, regulated by "sorting" mechanisms localised at the endosome compartment, may be responsible for the maintenance of polarised membrane domains. The polarised transcellular pathway involving obligatory endosome fusion is present in cleavage-stage, peripheral 16-cell blastomeres prior to zonular tight junction formation. Nocodazole treatment to depolymerize microtubules in many cases induced a bypass of the endosomal sorting compartment during transcytosis, indicating that microtubules contribute to the spatial organization of endocytic membrane traffic.
Anat Rec 1986 Dec
PMID:Endocytic traffic in trophectoderm and polarised blastomeres of the mouse preimplantation embryo. 379 97

The carbohydrate histochemistry of the rabbit oviduct has been examined by the use of four lectins conjugated with horseradish peroxidase as histochemical reagents. Each lectin gave a very distinct typical pattern of binding, but for each lectin there was no difference between the distribution of binding sites in ampulla and isthmus. Wheat germ lectin bound exclusively with the connective tissue of the oviduct folds; winged pea lectin was detected only in the ciliated cells; peanut lectin binding sites were visualized in the secretory cells; the binding reactivity of soybean lectin was limited to the basal part of the cilia. Although it is very difficult at present to correlate the distribution of lectin binding sites with the function of the positive cells, some hypotheses have been advanced.
Anat Rec 1985 Mar
PMID:Distribution of lectin binding sites in rabbit oviduct. 383 62

Discovery of components of the renin-angiotensin system (RAS) in the adenohypophysis of several species has prompted speculation concerning the location and possible function of a pituitary RAS. Although both renin and angiotensin II have been localized within the rat adenohypophysis, their colocalization has not been previously demonstrated within the same cells. In the present study, immunohistochemical staining by the avidin-biotin-peroxidase complex technique was used to demonstrate the coexistence of renin and angiotensin II in adenohypophyseal cells identified morphologically and immunocytochemically as gonadotrophs. These results support the existence of an adenohypophyseal RAS, at least part of which is under intracellular control. The influence of this system on control of fluid balance, blood pressure, and the secretion of other hypophyseal hormones is discussed.
Anat Rec 1985 Jun
PMID:The renin-angiotensin system in the rat anterior pituitary: colocalization of renin and angiotensin II in gonadotrophs. 391 37

Paraffin sections of normal human kidney were stained with a battery of ten lectin-horseradish peroxidase conjugates. Staining of proximal tubules revealed a relatively uniform distribution of glycoconjugates having bi- and/or triantennary N-linked sugar chains as well as terminal beta-galactose and alpha-fucose in all cells. In contrast, terminal alpha- and beta-galactose and alpha-fucose were localized in only some cells of the thin limbs, whereas N-linked sugar chains and terminal alpha-N-acetylgalactosamine occurred in all cells. In the ascending thick limbs, terminal alpha-N-acetylgalactosamine was found in some cells and N-linked sugar chains and terminal beta-galactose were present in all cells. The distal convoluted tubules contained N-linked oligosaccharides and terminal beta-galactose in all cells. Terminal alpha-N-acetylgalactosamine was found in some but not all profiles of distal convoluted tubules in a few kidneys. In the initial (connecting) segment of cortical collecting ducts, cells varied in their content of glycogen and glycoconjugates with terminal alpha- and beta-galactose, alpha-fucose and alpha-N-acetylgalactosamine, but cells in this segment evidenced uniform localization of N-linked sugar chains. A similar distribution of sugars occurred in the medullary ray segment of cortical collecting ducts, except for terminal beta-galactose which was present in all cells. In the medullary collecting ducts, there was also considerable cell-to-cell variation in the content and distribution of glycogen and glycoconjugates having N-linked sugar chains, terminal alpha-galactose, alpha-fucose, alpha-N-acetylgalactosamine, and the disaccharide galactose-(beta 1----3)-N-acetylgalactosamine. The content and distribution of glycoconjugates in the nephron varied only slightly between kidneys from different individuals, but individual variability was extensive in the collecting ducts. The reasons for these individual differences have not been determined, however. Cellular heterogeneity of glycosubstances within the different regions of the human kidney correlates with similar findings in other mammals and implies diverse functional roles for the various types of complex carbohydrates in the kidney.
Anat Rec 1985 Apr
PMID:Heterogeneous distribution of glycoconjugates in human kidney tubules. 399 86

Neurotensin-like immunoreactivity was localized in nerve fibers and terminals of hamster adrenal medulla at light and electron microscopy using the peroxidase-antiperoxidase method. Numerous varicose neurotensin-immunoreactive nerves and terminals were found among nonlabeled cell groups situated peripherally in the adrenal medulla. Combined formaldehyde-glutaraldehyde (Faglu) fluorescence and immunohistochemistry of the same vibratome section showed that only norepinephrine cells were innervated by neurotensin-immunoreactive nerves. All norepinephrine cells seemed to be innervated by neurotensin-immunoreactive nerves. Neurotensin-immunoreactive nerves disappeared after extrinsic denervation of the adrenal gland. By electron microscopy numerous neurotensin-immunoreactive terminals were seen to make synaptic contacts with norepinephrine cells and with autonomic ganglion cells present in small numbers among norepinephrine cells. In the terminals neurotensin-like immunoreactivity was localized mainly in large dense-cored vesicles, but some precipitates were also associated with small vesicles, diffusely scattered in the axoplasm. The present findings suggest that in the hamster adrenal medulla part of the nerve terminals arising from splanchnic nerves contain neurotensin-like peptide. The functional significance of these nerves in the hamster adrenal medulla remains to be elucidated.
Anat Rec 1985 Apr
PMID:Immunohistochemical localization of neurotensin in hamster adrenal medulla. 399 96

Ciliated cells of the ductuli efferentes show at their apex a discrete endocytic apparatus composed of small vesicles connected to or subjacent to the apical plasma membrane, small apical membranous tubules, and pale multivesicular bodies. Deeper in the cytoplasm, there are acid phosphatase-positive denser, multivesicular bodies and secondary lysosomes showing an electron-dense cortex and a crystalline, paler stained core. Cationic ferritin and concanavalin A-ferritin used to demonstrate adsorptive endocytosis, when injected into the rete testis, rapidly reached the lumen of the ductuli efferentes. At 1 min after injection, these tracers were seen bound to the apical plasma membrane of ciliated cells and within small endocytic vesicles and by 5 min in narrow apical tubules. At 15 and 30 min after injection, the tracers appeared in pale multivesicular bodies while at 1 hr they were found within dense multivesicular bodies. At 2 hr and longer time intervals these tracers accumulated within secondary lysosomes. Native ferritin, concanavalin A-ferritin in the presence of alpha-methyl-D-mannoside, and horseradish peroxidase or albumin-colloidal gold complexes were used to analyze fluid-phase endocytosis. At various intervals following their injection into the rete testis, these tracers presented a distribution identical in all respects to that described for cationic ferritin and concanavalin A-ferritin. In the present work, none of the above tracers were transported to the abluminal aspect of the ciliated cells. These cells, like the nonciliated epithelial cells of the ductuli efferentes are thus involved in adsorptive as well as in fluid-phase endocytosis.
Anat Rec 1985 Mar
PMID:Fluid-phase and adsorptive endocytosis in ciliated epithelial cells of the rat ductuli efferentes. 403 43

The fine topological relationship between sinus-lining endothelial cells (SLE) and vessel-lining endothelial cells (VLE) at the opening portion of sinusoids into central or interlobular veins of rat liver was studied by a comparison of morphological and functional properties of both types of cells. Three minutes after intravenous injection of formalin-denatured albumin conjugated with horseradish peroxidase (HRP-FDA), liver was perfused with fixative. Chopped sections of the liver (50 micron thick) were incubated in diaminobenzidine-H2O2 medium, followed by processing for electron microscopy. The HRP-FDA was localized in endocytotic vesicles and vacuoles of the SLE and Kupffer cells but not of the VLE lining interlobular or central veins or interlobular arteries. In the opening portion of the sinusoids into these veins, the attenuated cytoplasmic extensions of the SLE containing positive vesicles were in direct contact with squamous process of the VLE having no positive vesicles. The contact was mediated by overlapping junctions. No intermediate cell type between the SLE and VLE in this region or other portions was noted. The results indicate that the habitat of the SLE is exactly isolated from that of the VLE in rat liver and at the transitional portion from sinusoids to veins or arteries they are directly connected with each other by overlapping junctions.
Anat Rec 1985 May
PMID:Functional differences between sinusoidal endothelial cells and interlobular or central vein endothelium in rat liver. 407 45

The structure of the sinus walls in the popliteal lymph node of the rabbit was studied with the electron microscope. In the marginal sinus, the endothelial cells are connected by gap junctions, puncta adherentia, and surface specializations characterized by focal approximation of the adjoining membranes without fusion. They possess large numbers of simple and compound uncoated invaginations of the plasma membrane that are closed by a diaphragm with a central thickening. The tissue strands that straddle the lumen of the sinus consist of a fibrous core containing both collagen and elastic fibers, surrounded by endothelial cells identical to those composing the outer sinus wall. Cortical sinuses that run independently of the trabeculae were identified by exploiting the fact that their endothelial cells accumulate lymph-borne ferritin, and their lumen is outlined by horseradish peroxidase administered intravenously. They are lined by a flattened, continuous endothelium and lack luminal strands. The walls of the medullary sinuses consist of endothelial cells and macrophages. The endothelial cells are interconnected by specialized junctions and contain fewer plasmalemmal vesicles than in the cortex; furthermore, dense granules are present in their cytoplasm. Macrophages adhere to the surface of the endothelial cells; typically, none of the junctional specializations that characterize the interface between endothelial cells connect endothelial cells to macrophages. However, at points along the contact region with the endothelium, the plasmalemma of the macrophage is decorated by an attachment plaque of fluffy cytoplasmic material. Sinus endothelial cells slowly accumulate lymph-borne ferritin like vascular endothelial cells elsewhere in the body, whereas macrophages contain both ferritin and engulfed erythrocytes.
Anat Rec 1985 Aug
PMID:Structure of the sinus-lining cells in the popliteal lymph node of the rabbit. 407 55

A 10,000-dalton calcium-binding protein (10-kd CaBP) has been described in the placentae and yolk sacs of rats and mice. This protein is similar or identical to vitamin D-dependent intestinal CaBP and these proteins have been implicated in the molecular mechanisms of intestinal calcium absorption and transplacental calcium transport. Using an antiserum to the purified 10-kd rat intestinal CaBP, the localization of CaBP in the 16-17-day mouse yolk sac and placenta was studied immunocytochemically with peroxidase-antiperoxidase labelling and quantified by radial immunodiffusion. A high concentration of immunolabelling was observed in the endodermal cells of the intraplacental yolk sac lining the sinuses of Duval. The columnar endodermal cells lining one side of the endodermal sinuses adjacent to fetal vessels contained most of the immunoreactive label. Quantitation by radial immunodiffusion demonstrated a 5.5-fold higher concentration of CaBP in the portion of the placenta containing most of the intraplacental yolk sac than in the maternal half of the placenta. This demonstration of a 10-kd CaBP within the intraplacental yolk sac suggests this protein functions to facilitate placental calcium transport and is the first study which directly supports the hypothesis of a functional role for the sinuses of Duval in calcium transport.
Anat Rec 1985 Dec
PMID:Immunochemical localization of vitamin D-dependent calcium-binding protein in mouse placenta and yolk sac. 408 32


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