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  • 1
    Electronic Resource
    Electronic Resource
    Na+-dependent glucose transporter SGLT1 is localized in the apical plasma membrane upon completion of tight junction formation in MDCK cells (1996)
    Springer
    Histochemistry and cell biology 106 (1996), S. 529-533 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  SGLT1, an isoform of Na+-dependent glucose transporters, is localized at the apical plasma membrane in the epithelial cells of the small intestine and the kidney. In the present study we examined its location in SGLT1 cDNA-transfected MDCK cells, which form an epithelial sheet connected by tight junctions in culture. Formation of tight junctions was monitored by staining for occludin, an integral tight junction protein. In the cells demarcated by an uninterrupted occludin meshwork, SGLT1 was specifically localized at the apical plasma membrane, showing that SGLT1 has a signal to accomplish this restricted localization. In the cells with little or no occludin accumulation in the tight junction, however, SGLT1 was present along the entire aspect of the plasma membrane. Similar distribution of SGLT1 was observed in the cells as long as the occludin meshwork remained incomplete. These observations sugget that apical localization of SGLT1 occurs upon the completion of the uninterrupted meshwork of tight junctions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004180050073
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  • 2
    Electronic Resource
    Electronic Resource
    Differential localization of organic cation transporters rOCT1 and rOCT2 in the basolateral membrane of rat kidney proximal tubules (2000)
    Springer
    Histochemistry and cell biology 114 (2000), S. 175-180 
    Details
    ISSN: 1432-119X
    Keywords: Organic cation transporter rOCT1 rOCT2 Kidney Proximal tubule
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Organic cation transporters play an important role in the secretion of cationic drugs as well as endogenous cationic metabolites in the renal tubules. Immunoblotting showed the presence of organic cation transporter proteins, rOCT1 and rOCT2, in the rat kidney. By immunofluorescence microscopy, rOCT1 was shown to be concentrated in the proximal tubules in the renal cortex. rOCT2, on the other hand, was rich in the proximal tubules in the outer stripe of the outer medulla. Confocal microscopy revealed that both rOCT1 and rOCT2 were localized to the basolateral membranes of these tubule cells. These findings directly show that rOCT1 and rOCT2 are basolateral membrane proteins and are differentially distributed along the proximal tubules.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004180000186
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  • 3
    Electronic Resource
    Electronic Resource
    Interactions between large organic cations and cation exchange membranes (1986)
    Springer
    Journal of applied electrochemistry 16 (1986), S. 41-52 
    Details
    ISSN: 1572-8838
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Electrical Engineering, Measurement and Control Technology
    Notes: Abstract Interactions between cation exchange membranes and large organic cations have been studied; namely (1) adsorption and electrodialytic desorption of cationic surface active agents, and (2) change in transport properties of the membranes by adsorption. N-dodecyl pyridyl compounds, such as N-dodecyl pyridinium bromide (C12-Py), N-dodecyl dipyridyl bromide (C12-Dipy) and N-dodecyl tripyridyl bromide (C12-Tripy) were used for the adsorption and electrodialytic desorption; and for the study on the change in transport properties of membranes, N-dodecyl pyridinium chloride, C12-Py, C12-Dipy, C12-Tripy and hexadecyl trimethylammonium chloride were used. It was confirmed that the higher the molecular weight of the cation the longer the time required to reach adsorption equilibrium, and that the amount of adsorption exceeded the ion-exchange capacity of the membrane. After equilibrium was attained, electrodialytic desorption from the membranes was difficult. The adsorption or ion-exchange of large organic cations was effective to the permselectivity of the cation exchange membrane to the sodium ion in electrodialysis of a solution of sodium chloride and calcium chloride. The relationship between the permselectivity and the properties of the cations was examined.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01015982
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  • 4
    Electronic Resource
    Electronic Resource
    Detection of a glycosphingolipid antigen in bladder cancer cells with monoclonal antibody MRG-1 (1995)
    Springer
    Journal of molecular histology 27 (1995), S. 247-252 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The monoclonal antibody MRG-1 has been evaluated for the immunohistochemical detection of the type 3 chain of blood group A in human normal bladder epithelium and bladder tumours. Light microscope examination of paraffin sections demonstrated that this antigen was present in normal epithelium and superficial bladder tumour in patients with blood group A or AB, but was absent in the invasive type of bladder tumour. In normal epithelium, the plasma membrane was positive for this antigen, and the cytoplasm was diffusely stained. In superficial transitional cell carcinoma, the plasma membrane was negative, whereas the cytoplasm was intensely stained in the perinuclear region. This pattern was different from that observed for type 1 and 2 group A antigen, which was recognized mainly at the plasma membrane. However, in superficial transitional cell carcinoma, the staining was also seen on the plasma membrane. The pattern of the localization of this antigen in this carcinoma was influenced by the treatment of organic solvents. Electron microscopical observations confirmed that this antigen was localized on the plasma membrane and also in the Golgi apparatus of the superficial tumour. These results proved that the type 3 chain of blood group A is present in human bladder epithelium and low grade tumours in correspondence with the blood type, but disappears in tumours with high malignant potential. However, its expression is independent of the expressions of the other subtypes which have been studied. Furthermore, the changes in the staining pattern caused by pretreatment with organic solvents suggested possible differences in the microenvironment of the glycolipids containing this type of sugar chain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00177592
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  • 5
    Electronic Resource
    Electronic Resource
    Detection of a glycosphingolipid antigen in bladder cancer cells with monoclonal antibody MRG-1 (1995)
    Springer
    Journal of molecular histology 27 (1995), S. 247-252 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The monoclonal antibody MRG-1 has been evaluated for the immunohistochemical detection of the type 3 chain of blood group A in human normal bladder epithelium and bladder tumours. Light microscope examination of paraffin sections demonstrated that this antigen was present in normal epithelium and superficial bladder tumour in patients with blood group A or AB, but was absent in the invasive type of bladder tumour. In normal epithelium, the plasma membrane was positive for this antigen, and the cytoplasm was diffusely stained. In superficial transitional cell carcinoma, the plasma membrane was negative, whereas the cytoplasm was intensely stained in the perinuclear region. This pattern was different from that observed for type 1 and 2 group A antigen, which was recognized mainly at the plasma membrane. However, in superficial transitional cell carcinoma, the staining was also seen on the plasma membrane. The pattern of the localization of this antigen in this carcinoma was influenced by the treatment of organic solvents. Electron microscopical observations confirmed that this antigen was localized on the plasma membrane and also in the Golgi apparatus of the superficial tumour. These results proved that the type 3 chain of blood group A is present in human bladder epithelium and low grade tumours in correspondence with the blood type, but disappears in tumours with high malignant potential. However, its expression is independent of the expressions of the other subtypes which have been studied. Furthermore, the changes in the staining pattern caused by pretreatment with organic solvents suggested possible differences in the microenvironment of the glycolipids containing this type of sugar chain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02389892
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  • 6
    Electronic Resource
    Electronic Resource
    Immunohistochemical localization of Na+-dependent glucose transporter in the rat digestive tract (1995)
    Springer
    Journal of molecular histology 27 (1995), S. 420-426 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Glucose is actively absorbed in the intestine by the action of the Na+-dependent glucose transporter. Using an antibody against the rabbit intestinal Na+-dependent glucose transporter (SGLT1), we examined the localization of SGLT1 immunohistochemically along the rat digestive tract (oesophagus, stomach, duodenum, jejunum, ileum, colon and rectum). SGLT1 was detected in the small intestine (duodenum, jejunum and ileum), but not in the oesophagus, stomach, colon or rectum. SGLT1 was localized at the brush border of the absorptive epithelium cells in the small intestine. Electron microscopical examination showed that SGLT1 was localized at the apical plasma membrane of the absorptive epithelial cells. SGLT1 was not detected at the basolateral plasma membrane. Along the crypt-villus axis, all the absorptive epithelial cells in the villus were positive for SGLT1, whose amount increased from the bottom of the villus to its tip. On the other hand, cells in the crypts exhibited little or no staining for SGLT1. Goblet cells scattered throughout the intestinal epithelium were negative for SGLT1. These observations show that SGLT1 is specific to the apical plasma membrane of differentiated absorptive epithelial cells in the small intestine, and suggest that active uptake of glucose occurs mainly in the absorptive epithelial cells in the small intestine.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00179568
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  • 7
    Electronic Resource
    Electronic Resource
    Immunohistochemical localization of Na+-dependent glucose transporter in the rat digestive tract (1995)
    Springer
    Journal of molecular histology 27 (1995), S. 420-426 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Glucose is actively absorbed in the intestine by the action of the Na+-dependent glucose transporter. Using an antibody against the rabbit intestinal Na+-dependent glucose transporter (SGLT1), we examined the localization of SGLT1 immunohistochemically along the rat digestive tract (oesophagus, stomach, duodenum, jejunum, ileum, colon and rectum). SGLT1 was detected in the small intestine (duodenum, jejunum and ileum), but not in the oesophagus, stomach, colon or rectum. SGLT1 was localized at the brush border of the absorptive epithelium cells in the small intestine. Electron microscopical examination showed that SGLT1 was localized at the apical plasma membrane of the absorptive epithelial cells. SGLT1 was not detected at the basolateral plasma membrane. Along the crypt-villus axis, all the absorptive epithelial cells in the villus were positive for SGLT1, whose amount increased from the bottom of the villus to its tip. On the other hand, cells in the crypts exhibited little or no staining for SGLT1. Goblet cells scattered throughout the intestinal epithelium were negative for SGLT1. These observations show that SGLT1 is specific to the apical plasma membrane of differentiated absorptive epithelial cells in the small intestine, and suggest that active uptake of glucose occurs mainly in the absorptive epithelial cells in the small intestine.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02389029
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  • 8
    Electronic Resource
    Electronic Resource
    Immunohistochemical expression of glucose transporter-1 in human penile proliferative lesions (1997)
    Springer
    Journal of molecular histology 29 (1997), S. 273-278 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Glucose transporters (GLUTs) are a family of membrane proteins responsible for the transport of glucose across cellular membranes. In terms of their mRNA levels, they have been reported to be expressed in some human tumours. However, the immunohistochemical localization of GLUTs in human urogenital lesions has rarely been studied. This study was performed to evaluate the expression of GLUT1 in penile proliferative lesions (18 cases of penile carcinoma and 13 cases of condyloma acuminatum). Using an isoform-specific anti-GLUT1 antibody, formalin-fixed paraffin-embedded sections were stained by the avidin--biotin complex method. In all cases of penile carcinoma, GLUT1 staining was diffusely recognized on the cell membrane of the carcinoma cells in the mainly infiltrating areas. However, the inner areas of the tumour were more weakly and focally stained. The intensity of staining for the penile carcinoma (staining score = 2.8 ± 0.6) was stronger than that for condyloma acuminatum and that for adjacent non-proliferative areas. All cases of condyloma acuminatum showed a diffuse staining on the cell membrane in the basal and intermediate layers (staining score = 2.4 ± 0.5). Non-proliferative (histologically normal) glans areas adjacent to the above lesions expressed the weakest GLUT1 staining only in the stratum basale (staining score = 1.8 ± 0.5). These three areas showed significantly different staining scores from each other (p 0.01). In conclusion, GLUT1 is expressed dominantly in penile proliferative lesions, especially in infiltrating areas of penile carcinoma
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026466229242
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  • 9
    Electronic Resource
    Electronic Resource
    Immunohistochemical localization of Na+-dependent glucose transporter in rat jejunum (1992)
    Springer
    Cell & tissue research 267 (1992), S. 3-9 
    Details
    ISSN: 1432-0878
    Keywords: Jejunum ; Na+-dependent active glucose transporter ; Absorptive epithelial cell ; Crypt-villus axis ; Plasma membrane ; Golgi apparatus ; Rat (Sprague-Dawley)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Glucose is actively absorbed via a Na+-dependent active glucose transporter (Na-GT) in the small intestine. We raised a polyclonal antibody against the peptide corresponding to amino acids 564–575 of rabbit intestinal Na-GT, and localized it immunohistochemically in the rat jejunum. By means of immunofluorescence staining, Na-GT was located at the brush border of the absorptive epithelial cells of the intestinal villi. Electron-microscopic examination showed that Na-GT was localized at the plasma membrane of the apical microvilli of these cells. Little Na-GT was found at the basolateral plasma membrane. Along the crypt-villus axis, all of the absorptive epithelial cells in the villus were positive for Na-GT. In addition to the brush border staining, the supranuclear positive staining, which was shown to be the Golgi apparatus by use of electron microscopy, was seen in cells located between the base to the middle of the villus. Cells in crypts exhibited little or no staining for Na-GT. Goblet cells scattered in the intestinal epithelium were negative for Na-GT staining. These observations show that Na-GT is specific to the apical plasma membrane of the absorptive epithelial cells, and that the onset of Na-GT synthesis may occur near the crypt-villus junction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00318685
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  • 10
    Electronic Resource
    Electronic Resource
    Immunolocalization of GLUT1 and connexin 26 in the rat placenta (1996)
    Springer
    Cell & tissue research 285 (1996), S. 83-89 
    Details
    ISSN: 1432-0878
    Keywords: Key words: Glucose transporter ; GLUT1 ; Connexin 26 ; Gap junctions ; Placenta ; Syncytiotrophoblast ; Rat (Wistar)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Interhemal membrane in the rat placenta is composed of three trophoblastic layers and endothelial cells. GLUT1, an isoform of the facilitated-diffusion glucose transporter, is abundant in the cells of the placental barrier, i.e., syncytiotrophoblastic layers I and II. GLUT1 is localized at the plasma membranes of the maternal-blood side of syncytiotrophoblastic layer I, and of the fetal-blood side of syncytiotrophoblastic layer II. Double-immunofluorescence microscopy has shown that connexin 26 is present between these GLUT1-positive sites, i.e., between syncytiotrophoblastic layers I and II. Immunogold electron microscopy has revealed that connexin 26 is localized in the gap junctions connecting the two layers. Connexin 26 in these layers therefore makes them functionally a single syncytial layer for the transfer of small molecules such as glucose in the rat placental barrier. These results suggest that glucose transfer in the rat placental barrier is carried out as follows: GLUT1 is used for the entry of glucose into the cytoplasm of syncytiotrophoblastic layer I, connexin 26 for the transfer of glucose from syncytiotrophoblastic layer I to syncytiotrophoblastic layer II, and GLUT1 for the exit of glucose to the fetal circulation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004410050623
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