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  • 1
    Electronic Resource
    Electronic Resource
    IRON SOLUBILITY FROM SEAFOODS WITH ADDED IRON AND ORGANIC ACIDS UNDER SIMULATED GASTROINTESTINAL CONDITIONS (1997)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food quality 20 (1997), S. 0 
    Details
    ISSN: 1745-4557
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Iron absorption from foods is dependent on the type of food consumed and other factors such as ligands which may have enhancing or inhibiting effects on iron absorption. In this study, iron (Fe2+ or Fe3+) and two organic acids (ascorbate and citrate) were added to three seafood surimis (scallops, prawns, and cod) and then subjected to simulated gastrointestinal conditions (pH 2, 4, and 6) to evaluate iron solubility. Soluble iron decreased with increasing pH in all samples and control. In cod, a combination of ascorbic and citric acid (1:2) was most effective to increase soluble iron; however, in scallops and prawns citric acid alone was best. After sequential pH and enzyme treatments, it was found that the effectiveness of iron solubilization depended primarily upon the type of seafood present and to a lesser extent the oxidation state of the iron salt.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4557.1997.tb00467.x
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  • 2
    Electronic Resource
    Electronic Resource
    Marked Spatial Genetic Structure in Three Populations of a Weedy Fern, Pteris multifida Poir., and Reestimation of Its Selfing Rate (1997)
    Oxford, UK : Blackwell Publishing Ltd
    Plant species biology 12 (1997), S. 0 
    Details
    ISSN: 1442-1984
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Allozyme markers were used to characterize spatial genetic structure for the weedy fern Pteris multifida within three populations growing on the man made stone walls. Even visually distinct genetic substructures were observed in all the examined populations. Spatial autocorrelation analysis using Moran's /indicated that the patch size of P. multifida was as small as 4–9 m. Estimation of outcrossing rate is known to be severely biased downwards if the presence of spatial genetic structure is ignored. Mating system of this fern species was reported as mixed (mean selfing rate: 0.435). However, fixation indexes calculated in small patches less than 3–10 m wide were not significantly different from Hardy-Weinberg equilibrium and thus P. multifida's mating system was considered to be outcrossing.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1442-1984.1997.tb00161.x
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  • 3
    Electronic Resource
    Electronic Resource
    Connexin 43 and the glucose transporter, GLUT1, in the ciliary body of the rat (1996)
    Springer
    Histochemistry and cell biology 106 (1996), S. 209-214 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  To investigate the relationship between the gap junction protein connexin 43 and the glucose transporter GLUT1, their localization was visualized by double-immunofluorescence microscopy using frozen sections as well as immunogold staining of ultrathin frozen sections. In pigmented epithelial cells, most of the GLUT1 was localized along the plasma membrane facing the blood vessels, whereas in non-pigmented epithelial cells, it was present along the plasma membrane facing the aqueous humor. Connexin 43 was abundant in the ciliary body and localized mainly in the gap junctions connecting the pigmented and non-pigmented epithelial cells. Localization of GLUT1 and connexin 43 in the blood-aqueous barrier suggests that GLUT1, connexin 43, and GLUT1 disposed in this order could be a machinery responsible for the transport of glucose across the blood-aqueous barrier.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004180050033
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  • 4
    Electronic Resource
    Electronic Resource
    Colocalization of tight junction proteins, occludin and ZO-1, and glucose transporter GLUT1 in cells of the blood-ocular barrier in the mouse eye (1998)
    Springer
    Histochemistry and cell biology 110 (1998), S. 543-551 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  The facilitative glucose transporter GLUT1 is abundant in cells of the blood-ocular barrier and serves as a glucose transport mechanism in the barrier. To see the relationship between the glucose transfer function and junctional proteins in the barrier, we examined the localization of GLUT1 and the tight junction proteins, occludin and ZO-1, in the mouse eye. Their localization in the retina, ciliary body, and iris was visualized by double-immunofluorescence microscopy and immunogold electron microscopy. Occludin and ZO-1 were colocalized at tight junctions of the cells of the barrier: retinal pigment epithelial cells, non-pigmented epithelial cells of the ciliary body, and endothelial cells of GLUT1-positive blood vessels. Occludin was restricted to these cells of the barrier. ZO-1 was found, in addition, in sites not functioning as a barrier: the outer limiting membrane in the retina, in the cell border between pigmented and non-pigmented epithelial cells in the ciliary body, and GLUT1-negative blood vessels. These observations show that localization of occludin is restricted to tight junctions of cells of the barrier, whereas ZO-1 is more widely distributed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004180050316
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  • 5
    Electronic Resource
    Electronic Resource
    Reductions in the bilateral parietal and occipital cerebral blood flow and metabolism in a patient with Marchiafava-Bignami disease (1999)
    Springer
    Journal of neurology 246 (1999), S. 607-608 
    Details
    ISSN: 1432-1459
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004150050412
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  • 6
    Electronic Resource
    Electronic Resource
    A case of cranial meningocele associated with Joubert syndrome (1996)
    Springer
    Child's nervous system 12 (1996), S. 280-282 
    Details
    ISSN: 1433-0350
    Keywords: Joubert syndrome ; Cranial meningocele ; MRI
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Joubert syndrome was first reported in 1969 as a rare, recessive autosomal syndrome associated with neuropathological abnormalities of the cerebellum and brain stem, partial or complete aplasia of the cerebellar vermis, and presenting with episodic hyperpnea and apnea, oculomotor abnormalities, and psychomotor retardation. Having experienced one case of this syndrome with associated cranial meningocele, we report the clinical course, MRI features, and surgical findings, and discuss the relevant literature.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00261812
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  • 7
    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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  • 8
    Electronic Resource
    Electronic Resource
    Aquaporin-5 (AQP5), a water channel protein, in the rat salivary and lacrimal glands: immunolocalization and effect of secretory stimulation (1999)
    Springer
    Cell & tissue research 295 (1999), S. 513-521 
    Details
    ISSN: 1432-0878
    Keywords: Key words Water channel protein ; Aquaporin ; AQP5 ; Rat ; Salivary glands ; Immunolocalization ; Secretory stimulation ; Rat (Wistar)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Aquaporin-5 (AQP5) is a water channel protein and is considered to play an important role in water movement across the plasma membrane. We raised anti-AQP5 antibody and examined the localization of AQP5 protein in rat salivary and lacrimal glands by immunofluorescence microscopy. AQP5 was found in secretory acinar cells of submandibular, parotid, and sublingual glands, where it was restricted to apical membranes including intercellular secretory canaliculi. In the submandibular gland, abundant AQP5 was also found additionally at the apical membrane of intercalated duct cells. Upon stimulation by isoproterenol, apical staining for AQP5 in parotid acinar cells tended to appear as clusters of dots. These results suggest that AQP5 is one of the candidate molecules responsible for the water movement in the salivary glands.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004410051257
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  • 9
    Electronic Resource
    Electronic Resource
    Peptide Transporter in the Rat Small Intestine: Ultrastructural Localization and the Effect of Starvation and Administration of Amino Acids (1999)
    Springer
    Journal of molecular histology 31 (1999), S. 169-174 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Peptide transporter-1 is a H+/peptide cotransporter responsible for the uptake of small peptides and peptide-like drugs, and is present in the absorptive epithelial cells of the villi in the small intestine (duodenum, jejunum, and ileum). It has been localized to the apical microvillous plasma membrane of the absorptive epithelial cells of the rat small intestine using the immunogold electron microscopic technique. Digital image analysis of the jejunum revealed that the transporter protein was abundant at the tip of the villus and that the amount decreased from the tip of the villus to its base. The effect of dietary administration of amino acids and starvation on the expression of PepT1 in the jejunum was examined by immunoblotting and image analysis of immunofluorescence. Starvation markedly increased the amount of peptide transporter present, whereas dietary administration of amino acids reduced it. The gradient of the transporter protein along the crypt-villus axis was maintained under either condition. These observations show that it is specific to the microvillous plasma membrane and that its expression is regulated by the nutritional condition.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1003515413550
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