Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P02794 (ferritin)
 17,525 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Follicles from rat and pig thyroid glands were isolated by digestion with collagenase. The epithelial cells of isolated follicles maintain their structural and functional polarity as shown by incorporation of 3H-leucine and autoradiography. To trace the fate of surface membrane, isolated follicles were opened, stimulated with thyrotropin and incubated for various time intervals with cationized ferritin (CF), uncharged dextran, native ferritin (NF), and latex spheres (0.5 mum in diameter) which were either pre-coated with CF or added together with CF. Uncharged dextran and native ferritin did not bind to the luminal cell membrane, were taken up in small amounts and accumulated in lysosomes; anionic NF was not found in Golgi cisternae in contrast to uncharged dextran which occassionally reached a few Golgi stacks. CF bound rapidly and in clusters to the luminal plasmalemma, preferentially to coated pits, was taken up by endocytosis, accumulated in lysosomes after 5 min and reached the Golgi cisternae after 30 min. Latex spheres were taken up by engulfment through fusion of microvilli and reached the lysosomes. CF particles coating the latex spheres may detach at this station and reach the Golgi cisternae. The findings show that the route of small tracers depends on the charge of the tracer, in agreement with results obtained by Farquhar [8]. Vesicles carrying NF can be traced to lysosomes only, whereas vesicles containing uncharged dextran or - more conspicuously -CF also fuse with Golgi membranes. Large tracers (latex beads) reach only the lysosomes, but CF taken up with them may move to Golgi cisternae.
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PMID:Membrane retrieval in epithelial cells of isolated thyroid follicles. 22 68

The surface saccharide composition of collagenase-dispersed pancreatic cells from adult guinea pig and rat glands was examined by using eight lectins and their ferritin conjugates: Concanavalin A (ConA); Lens culinaris (LCL); Lotus tetragonolobus (LTL); Ricinus communis agglutinins I and II (RCA I, RCA II); Soybean agglutinin (SBA); Ulex europeus lectin (UEL); and wheat germ agglutinin (WGA). Binding studies of iodinated lectins and lectin-ferritin conjugates both revealed one population of saturable, high-affinity receptor sites on the total cell population (approximately 95% acinar cells). Electron microscopy, however, revealed differences in lectin-ferritin binding to the plasmalemma of acinar, centroacinar, and endocrine cells. Whereas acinar cells bound heavily all lectin conjugates, endocrine and centroacinar cells were densely labeled only by ConA, LCL, WGA, and RCA I, and possessed few receptors for LTL, UEL, and SBA. Endocrine and centroacinar cells could be differentiated from each other by using RCA II, which binds to centroacinar cells but not to endocrine cells. Some RCA II receptors appeared to be glycolipids because they were extracted by ethanol and chloroform-methanol in contrast to WGA receptors which resisted solvent treatment but were partly removed by papain digestion. RCA I receptors were affected by neither treatment. The apparent absence of receptors for SBA on endocrine and centroacinar cells, and for RCA II on endocrine cells, was reversed by neuraminidase digestion, which suggested masking of lectin receptors by sialic acid. The absence of LTL and UEL receptors on endocrine and centroacinar cells was not reversed by neuraminidase. We suggest that the differential lectin-binding patterns observed on acinar, centroacinar, and endocrine cells from the adult pancreas surface-carbohydrate-developmental programs expressed during morphogenesis and cytodifferentiation of the gland.
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PMID:Distribution of cell surface saccharides on pancreatic cells. II. Lectin-labeling patterns on mature guinea pig and rat pancreatic cells. 42 54

The submandibular glands of 4-week-old rats were dissociated by a procedure involving digestions with collagenase and hyaluronidase, chelation of divalent cations and mechanical force. A suspension of single cells was obtained in low yield by centrifugation in a Ficoll-containing medium. Immediately after dissociation and after a culture period of 16-18 hr the dissociated cells were tested for agglutinability by concanavalin A (Con A). Using ferritin (tfer)-conjugated Con A the lectin binding by the isolated acinar cells was also studied. The dissociated cells were agglutinated by low concentrations of Con A and bound Fer-Con A molecules on their entire surface without any indication of polarization of the cell membrane. There was a considerable cell to cell variation in the amount of Fer-Con A binding which was, in general, sparse and patchy. The contact surfaces between agglutinated cells revealed a dense binding of Fer-Con A molecules irrespective of the types of cells participating in the agglutination reaction. Cells cultured for 16-18 hr were no longer agglutinated by Con A. As compared to the freshly dissociated cells the cultured acinar cells revealed a more uniform and denser binding of Fer-Con A molecules. Furthermore, there were more lectin molecules bound to the cell surface corresponding to the basal part of the cell, where the nucleus and most of the rough surface endoplasmic reticulum were located, than to the apical cell surface. It is suggested that the higher density of lectin-binding sites on the cell surface in the vicinity of the cisternae of the rough endoplasmic reticulum indicates insertion sites of newly synthesized membrane glycoproteins.
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PMID:Distribution of concanavalin A binding sites on the surface of dissociated rat submandibular gland acinar cells. 115 94

Dissociation of adult cardiac myocytes by collagenase perfusion techniques requires separation of the junctional contacts that link the cells physically, electrically and metabolically in the intact heart. Gap junctions, one of three types of intercellular junction present at the cardiac intercalated disc, are not split into their component membranes when myocytes are dissociated; they are ripped from the plasma membrane of one cell, to be retained by its neighbour. Partitioning of junctions in this way might be expected to constitute a serious threat to the ionic integrity of dissociated myocytes, but in practice, high yields of functionally intact cells, suitable for experimental studies, are routinely obtained. To explain this apparent paradox, repair mechanisms, operating to seal the membrane lesions caused by gap junction tearing, have been hypothesized, but evidence for their existence has previously been lacking. Using freeze-fracture electron microscopy, the present study identifies repair sites as smooth membrane domains that are continuous with the neighbouring plasma membrane, thus forming intact seals. That these structures are not chemically-induced artefacts is demonstrated by their presence in myocytes that were frozen directly from the living state. Subsarcolemmal vesicle clusters, detected in thin sections and freeze-fracture replicas, are associated with the smooth sealing domains. These structures may represent either rounded-up fragments of mechanically disrupted membrane or structures concerned with the synthesis of new lipid. From their freeze-fracture morphology, the sealing domains appear to be lipid-rich and protein-poor. Cytochemical studies using Ruthenium Red, cationized ferritin and lectins show in addition that they have a lower content of negatively-charged membrane components than the neighbouring plasma membrane, and that the carbohydrate residues normally associated with plasma membrane glycolipids and glycoproteins are absent.
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PMID:Integrity of the dissociated adult cardiac myocyte: gap junction tearing and the mechanism of plasma membrane resealing. 235 53

Interactions between macrophages and articular surfaces were studied in an in vitro model which has been described before. Either stimulated peritoneal macrophages or a purified population of bone marrow macrophages were incubated with mice femoral heads which were either untreated or were digested with collagenase, trypsin or hyaluronidase prior to incubation. Scanning electron microscopy (EM) examination showed that macrophages attached to the surface and in their vicinity tags and fibers were visible. Transmission EM was used after labeling the surfaces with cationized ferritin employed as a sensitive marker to define the integrity of the articular surface. Alterations of the surface of various degrees of intensity were seen in all the sections examined. No adhering macrophages were found, due probably to detachment of cells during tissue processing for transmission EM. Attachment of macrophages to the surface and alterations of the latter were seen also when hyaluronic acid was added to the incubation medium or when the surfaces had been treated with hyaluronidase before incubation.
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PMID:Interaction between macrophages and articular surfaces: an in vitro transmission and scanning electron microscopy study. 237 23

The presence, distribution and content of sialic acid on the cell surface in collagenase-dispersed acini obtained both from unstimulated as well as from in vivo isoproterenol-stimulated mouse parotid have been studied. To this end, sialic acid residues have been qualitatively and quantitatively analyzed by 1) cytochemical labeling by wheat germ agglutinin (WGA), 2) biochemical procedures and 3) isotopic labeling by [3H]WGA (WGA-N-[acetyl-3H]-acetylated). Electron microscopy revealed striking differences in the binding of ferritin-conjugated WGA at the basal, lateral and apical cell surface. Unstimulated acinar cells showed a heavy patch-distributed binding of ferritin-conjugate on the basal cell surface while it was homogeneous and very scarce on the lateral one and absent on the apical cell surface. During the first few hours after isoproterenol, the WGA binding sites at the basal cell surface became homogeneously distributed. This fact was coincident with a loss of about 60 to 70% both in the content of neuraminidase-releasable sialic acid and in the binding of [3H]WGA to the acinar surface. These findings suggest that the release of sialic acid as free residues, which has been involved in the isoproterenol-triggered cell proliferation-inducing mechanism in the mouse parotid, would occur at the glycocalyx corresponding to the basal plasma membrane of the acinar cells.
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PMID:Changes in the content and distribution of sialic acid on the basal surface of isoproterenol-stimulated mouse parotid acinar cells. 275

The effects of cross-linking agents on the resistance of the articular surface to digestion with clostridial collagenase were studied using a described in vitro system. Mouse femoral heads were treated with various concentrations of glutaraldehyde, with osmium tetraoxide and with dithiobis (succinimydil propionate), digested with the enzyme, labeled with cationized ferritin and examined by electron microscopy. Collagenase alone caused disruption of the articular surface with penetration of the large marker into the cartilage matrix. After treatment of the femoral heads with the cross-linking agents, no effects on the morphology and on the labeling of the articular surface and no penetration of the label into the cartilage matrix were observed. Increasing cross-linking at the articular surface might be a new route for therapeutic intervention. However, experiments would be needed to assess the effect of the procedure on the viability and nutrition of chondrocytes and on the functional properties of the tissue.
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PMID:In vitro protection of the articular surface by cross-linking agents. 285 26

The direct effects on the cartilage articular surface of three anti-inflammatory drugs (Diclofenac, Pirprofen and acetyl-salicylic acid) and of a polysulfated glycosaminoglycan (Arteparon), were studied using an in vitro system in which BALB-c mouse femoral heads were incubated with the drugs. After incubation and labeling of the negative charges of the articular surfaces with cationized ferritin, the femoral heads were examined by electron microscopy. In addition, the effect of the drugs on the aggressive action of collagenase on the articular surface was tested using the same in vitro system. Diclofenac, Pirprofen and the polysulfated glycosaminoglycan did not alter the structure or the charge properties of the surface. Acetyl salicylic acid produced a slight disruption of the articular surface. The drugs studied had no effect on the disruptive action of collagenase.
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PMID:Drug action on articular cartilage surface. An in vitro study using mouse femoral heads labeled with cationized ferritin. 295 42

Polycationic labels such as cationized ferritin and colloidal iron were used to evaluate the surface negative charges over the mandibular condyles of ICR mice. The effects of neuraminidase, hyaluronidase, pronase, and collagenase on the binding of cationized ferritin and colloidal iron particles to the condylar articular surface were also studied. The results of this study clearly indicate that the surface area of the cartilaginous condyle is negatively charged and that its composition consists mainly of a collagenous material embedded within a proteinaceous matrix. With age, a substantial decrease in the density of negative charges took place along the surface area and, in particular, in the context of sialic acid residues. It is, therefore, possible that the reduction in cartilage surface charge might be associated with the onset of osteoarthritic changes commonly seen in aging humans and experimental animals.
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PMID:Cartilage surface charge. A possible determinant in aging and osteoarthritic processes. 298 74

The role of collagen in ultrafiltration properties of the glomerular basement membrane (GBM) was tested after a single administration of bacterial collagenase, using native ferritin as a tracer which does not pass through the GBM under physiological conditions. Experiments were performed both in situ and with isolated kidneys. Increased permeability to ferritin occurs 6 hr following enzyme perfusion and becomes patent after 30 hr, numerous tracer molecules appearing in urinary space, without any readily observable changes either in distribution of fixed negative charges (as revealed by colloidal iron and polyethyleneimine) or in structural organization of the glomerulus. Selective permeability of the GBM is progressively restored so that ferritin is almost confined to capillary lumen one month after enzyme injection. We conclude that collagen plays an important part in restricting plasma protein filtration.
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PMID:Enhancement of glomerular permeability to anionic ferritin induced by kidney perfusion with collagenase. 298 77


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