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Journal ArticleDOI

Protein absorption and transport by the guinea pig visceral yolk sac placenta.

01 Nov 1970-American Journal of Anatomy (Wiley Subscription Services, Inc., A Wiley Company)-Vol. 129, Iss: 3, pp 261-287
TL;DR: The cytological basis for protein transport across the guinea pig visceral yolk sac at 36–44 days of gestation was studied by means of electron microscopy following injection of horseradish peroxidase and ferritin and the pathways observed are consistent with those suggested by previous authors for the passage of maternal antibodies and serum proteins to the Guinea pig fetus.
Abstract: The cytological basis for protein transport across the guinea pig visceral yolk sac at 36–44 days of gestation was studied by means of electron microscopy following injection of horseradish peroxidase and ferritin. These results were compared with those obtained after administration of colloidal thorium dioxide. Distribution of the tracer molecules was studied at 2, 10, 20, 40, and 160 minutes after injection into the uterine lumen. All three tracer molecules were rapidly absorbed by endoderm cells. Although most of the protein appeared to be retained in droplets in endoderm cells, some protein was transmitted. Peroxidase was found to be rapidly transmitted across the yolk sac, ferritin somewhat more slowly, and colloidal thorium was not transmitted at all. Protein which had exited from the endoderm cells followed any of three pathways: (1) it crossed the visceral basement membrane and entered the vitelline capillaries; (2) it crossed the mesodermal compartment, crossed the mesothelial cells and entered the exocoelomic cavity; or (3) some of the protein was sequestered by macrophages in the splanchnic mesoderm. The pathways observed are consistent with those suggested by previous authors for the passage of maternal antibodies and serum proteins to the guinea pig fetus.
Citations
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Journal ArticleDOI
TL;DR: Observations indicate that nascent chylomicrons accumulate within Golgi vesicles as a pre-requisite to secretion and that secretion occurs by exocytosis resulting in the release of nascent chlyomicrons from secretory vesicle-membrane fusion.

176 citations

Journal ArticleDOI
01 May 2000-Placenta
TL;DR: Comparative studies will continue to be required to understand the functional role of IGFs and IGFBPs in each species, and to highlight the diversity in the expression of the IGF system among placentae of man and different laboratory animals, and even between closely related species.

176 citations

Journal ArticleDOI
TL;DR: The observations in the present study favor the premise that PGCs of the mouse do not originate in the endoderm, which was observed to mean that, although P GCs are set aside early in development as a distinct cell line, they also continue to become more specialized within time.

170 citations

Journal ArticleDOI
TL;DR: The data suggest that the Fc receptor of the yolk sac is isolated and that this receptor is structurally and functionally related to the F c receptor ofThe neonatal intestine.
Abstract: The yolk sac of the fetal rat and the proximal small intestine of the neonatal rat selectively transport maternal IgG. IgG-Fc receptors are thought to mediate transport across the epithelium of both tissues. We used a mouse mAb (MC-39) against the 45-54-kD component of the Fc receptor of the neonatal intestine to find an antigenically related protein that might function as an Fc receptor in fetal yolk sac. In immunoblots of yolk sac, MC-39 recognized a protein band with apparent molecular mass of 54-58 kD. MC-39 bound to the endoderm of yolk sac in immunofluorescence studies. In immunogold-labeling experiments MC-39 was associated mainly with small vesicles in the apical cytoplasm and in the region near the basolateral membrane of endodermal cells. The MC-39 cross-reactive protein and beta 2-microglobulin, a component of the intestinal Fc receptor, were copurified from detergent-solubilized yolk sac by an affinity purification that selected for proteins which, like the intestinal receptor, bound to IgG at pH 6.0 and eluted at pH 8.0. In summary, the data suggest that we have isolated the Fc receptor of the yolk sac and that this receptor is structurally and functionally related to the Fc receptor of the neonatal intestine. An unexpected finding is that, unlike the intestinal receptor which binds maternal IgG on the apical cell surface, the yolk sac receptor appears to bind IgG only within apical compartments which we suggest represent the endosomal complex.

156 citations


Cites background from "Protein absorption and transport by..."

  • ...Considerable biochemical (Williams et al., 1975) and morphological (Lambson, 1966; King and Enders, 1970; Slade, 1970; SeibeI, 1974) evidence indicates that a large amount of nonselective uptake occurs at the apical surface of endodermal cells where proteins appear to adsorb nonspecifically to a…...

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  • ...Considerable biochemical (Williams et al., 1975) and morphological (Lambson, 1966; King and Enders, 1970; Slade, 1970; SeibeI, 1974) evidence indicates that a large amount of nonselective uptake occurs at the apical surface of endodermal cells where proteins appear to adsorb nonspecifically to a characteristic dense coat on the luminal surface of apical invaginations....

    [...]

Journal ArticleDOI
TL;DR: By 24 hours after implantation, the two endo‐dermal derivatives have assumed widely diverse shapes and different types of associations and rates of replication, and are probably performing different functions.
Abstract: The initial differentiation of endoderm at the time of onset of implantation, and the subsequent rapid differentiation of visceral and parietal endoderm were studied in the rat and mouse. Transmission electron microscopy illustrates the reorientation and loosening of embryonic cell mass cells during implantation, as well as cytological evidence that endoderm cells have differentiated. Using scanning electron microscopy, parietal endoderm consists of individual stellate cells with numerous peripheral branching filopodia. As these cells migrate abembryonically, the rest of the embryonic cell mass becomes recom-pacted. The visceral endoderm proliferates and forms a columnar epithelium which has the cytological characteristic of an absorptive epithelium and is able to ingest exogenous proteins. Thus, by 24 hours after implantation, the two endo-dermal derivatives have assumed widely diverse shapes and different types of associations and rates of replication, and are probably performing different functions.

132 citations

References
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Journal ArticleDOI
TL;DR: The stain reported here differs from previous alkaline lead stains in that the chelating agent, citrate, is in sufficient excess to sequester all lead present, and is less likely to contaminate sections.
Abstract: Aqueous solutions of lead salts (1, 2) and saturated solutions of lead hydroxide (1) have been used as stains to enhance the electron-scattering properties of components of biological materials examined in the electron microscope. Saturated solutions of lead hydroxide (1), while staining more intensely than either lead acetate or monobasic lead acetate (l , 2), form insoluble lead carbonate upon exposure to air. The avoidance of such precipitates which contaminate surfaces of sections during staining has been the stimulus for the development of elaborate procedures for exclusion of air or carbon dioxide (3, 4). Several modifications of Watson's lead hydroxide stain (1) have recently appeared (5-7). All utilize relatively high pH (approximately 12) and one contains small amounts of tartrate (6), a relatively weak complexing agent (8), in addition to lead. These modified lead stains are less liable to contaminate the surface of the section with precipitated stain products. The stain reported here differs from previous alkaline lead stains in that the chelating agent, citrate, is in sufficient excess to sequester all lead present. Lead citrate, soluble in high concentrations in basic solutions, is a chelate compound with an apparent association constant (log Ka) between ligand and lead ion of 6.5 (9). Tissue binding sites, presumably organophosphates, and other anionic species present in biological components following fixation, dehydration, and plastic embedding apparently have a greater affinity for this cation than lead citrate inasmuch as cellular and extracellular structures in the section sequester lead from the staining solution. Alkaline lead citrate solutions are less likely to contaminate sections, as no precipitates form when droplets of fresh staining solution are exposed to air for periods of up to 30 minutes. The resultant staining of the sections is of high intensity in sections of Aralditeor Epon-embedded material. Cytoplasmic membranes, ribosomes, glycogen, and nuclear material are stained (Figs. 1 to 3). STAIN SOLUTION: Lead citrate is prepared by

24,137 citations

Journal ArticleDOI
TL;DR: The early stages of absorption of intravenously injected horseradish peroxidase in proximal tubules of mouse kidney were studied with a new ultrastructural cytochemical technique, which gives sharp localization and is sensitive to protein transport.
Abstract: The early stages of absorption of intravenously injected horseradish peroxidase in proximal tubules of mouse kidney were studied with a new ultrastructural cytochemical technique. In animals killed as early as 90 sec after injection, reaction product was found on the brushborder membranes and in the apical tubular invaginations. From the latter structures it was transported to the apical vacuoles, in which it was progressively concentrated to form protein absorption droplets. The method, which employs 3,3'-diaminobenzidine as oxidizable substrate, gives sharp localization and is sensitive. This system is advantageous in studying the early stages of renal tubular protein absorption, since small amounts of protein on membranes and in tubules and vesicles can be detected easily. The method also appears promising for studying protein transport in a variety of other cells and tissues.

6,495 citations

Journal ArticleDOI
TL;DR: Preliminary radioautographs, and certain morphological features of the fat body, ovary, and midgut, suggest that the midGut is the principal site of yolk protein synthesis in the mosquito.
Abstract: Yolk proteins are thought to enter certain eggs by a process akin to micropinocytosis but the detailed mechanism has not been previously depicted. In this study the formation of protein yolk was investigated in the mosquito Aedes aegypti L. Ovaries were fixed in phosphate-buffered osmium tetroxide, for electron microscopy, before and at intervals after a meal of blood. The deposition of protein yolk in the oocyte was correlated with a 15-fold increase in 140 mµ pit-like depressions on the oocyte surface. These pits form by invagination of the oocyte cell membrane. They have a 20 mµ bristle coat on their convex cytoplasmic side. They also show a layer of protein on their concave extracellular side which we propose accumulates by selective adsorption from the extraoocyte space. The pits, by pinching off from the cell membrane become bristle-coated vesicles which carry the adsorbed protein into the oocyte. These vesicles lose the coat and then fuse to form small crystalline yolk droplets, which subsequently coalesce to form the large proteid yolk bodies of the mature oocyte. Preliminary radioautographs, and certain morphological features of the fat body, ovary, and midgut, suggest that the midgut is the principal site of yolk protein synthesis in the mosquito.

1,284 citations

Journal ArticleDOI
TL;DR: The digestive cycle following reabsorption of hemoglobin by cells of the proximal convoluted tubules in mouse kidney and the uptake of ferritin by glomerular mesangial cells in the kidney of normal and nephrotic rats were investigated by electron microscopical histochemical procedures.
Abstract: The digestive cycle following reabsorption of hemoglobin by cells of the proximal convoluted tubules in mouse kidney and the uptake of ferritin by glomerular mesangial cells in the kidney of normal and nephrotic rats were investigated by electron microscopical histochemical procedures. Mouse kidneys, sampled at closely spaced time points between 1 to 48 hours after intraperitoneal injection of hemoglobin, and rat (normal and nephrotic) kidneys, sampled at 30 minutes, 2 hours, and 48 hours after intravenous injection of ferritin, were fixed in glutaraldehyde, cut at 50 µ on a freezing microtome, incubated for acid phosphatase and thiolacetate-esterase, and postfixed in OsO 4 . Satisfactory preservation of fine structure permitted the localization of the enzymatic reaction products on cell structures involved in uptake and digestion of exogenous proteins. The latter were identified either by their density (hemoglobin) or their molecular structure (ferritin). It was found that lysosomal enzymic activities and incorporated exogenous proteins occur together in the same membrane-bounded structures. In the cells of the proximal convolution, lytic activities become demonstrable within 1 hour after hemoglobin injection, appear first in apical vacuoles filled with hemoglobin, and persist in fully formed protein absorption droplets. At the end of the lytic cycle (∼48 hours post injection), the cells have an increased population of polymorphic bodies which exhibit lytic activities. In smaller numbers, identical bodies occur in controls. It is concluded that they represent remnants of previous digestive events. The means by which the resorptive vacuoles acquire hydrolytic activities remain unknown. Fusion of newly formed vacuoles with residual bodies was not seen, and hemoglobin incorporation into such bodies was only occasionally encountered. Acid phosphatase activity was found sometimes in the Golgi complex, but enzyme transport from the complex to the resorbing vacuoles could not be established. Autolytic vacuoles containing mitochondria or mitochondrial remnants were frequently found during the early stages of hemoglobin resorption, but no definite conclusions about the mechanism involved in the segregation of endogenous material were obtained. In nephrotic rats ferritin was segregated in membrane-bounded bodies mainly in the mesangial cells and to a lesser extent in epithelial and endothelial cells. Most of these sites were marked by the reaction products of acid phosphatase and organophosphorus-resistant esterase and therefore identified as lysosomes connected with the digestion of incorporated exogenous proteins.

422 citations