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  • Escherichia coli  (6)
  • Rat (Wistar)  (5)
  • Springer  (11)
  • Wiley-Blackwell
  • 1
    Electronic Resource
    Electronic Resource
    Mechanism of Na+/proline symport inEscherichia coli: Reappraisal of the effect of cation binding to the Na+/proline symport carrier (1990)
    Springer
    The journal of membrane biology 114 (1990), S. 143-151 
    Details
    ISSN: 1432-1424
    Keywords: proline carrier ; Na+-symport ; proline binding ; Escherichia coli ; transport model
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The proton and sodium ion dependences of the proline binding and transport activities of the proline carrier inEscherichia coli were investigated in detail. The binding activity in cytoplasmic membrane vesicles from a carrier over-producing strain (PT21/pTMP5) was absolutely dependent on the presence of Na+, but did not necessarily require protonation of the carrier, in contrast to the model previously reported (Mogi, T., Anraku, Y. 1984.J. Biol. Chem. 259:7797–7801). Based on this and previous observations, we propose a modified model of the proline binding reaction of the proline carrier, in which a proton is supposed to be a regulatory factor for the binding activity. The apparent Michaelis constant of proline (Kt) of the transport activity of cytoplasmic membrane vesicles from the wild typeE. coli strain driven by a respiratory substrate, ascorbate, showed dependence on a low concentration of sodium ion. The Michaelis constant of sodium ion for transport (Kt Na) was estimated to be 25 μm. The proline transport activities in membrane vesicles and intact cells were modulated by H+ concentration, the inhibitory effect of protons (pK a ≈6) being similar to that observed previously (Mogi, T., Anraku, Y. 1984.J. Biol. Chem. 259:7802–7806). Based on these observations and the modified model of substrate binding to the proline carrier, a model of the proline/Na+ symport mechanism is proposed, in which a proton is postulated to be a regulatory factor of the transport activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01869095
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  • 2
    Electronic Resource
    Electronic Resource
    Rat intestinal galactoside-binding lectin L-36 functions as a structural protein in the superficial squamous cells of the esophageal epithelium (1995)
    Springer
    Cell & tissue research 281 (1995), S. 77-83 
    Details
    ISSN: 1432-0878
    Keywords: Key words: Esophagus ; Epithelial cells ; Intestinal lectin ; L-36 ; RI-H fragment ; Immunocytochemistry ; Rat (Wistar)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Using an affinity purified antibody raised against the RI-H fragment of rat intestinal lectin L-36, the latter protein has been identified within the esophageal epithelium by means of ultracryotomy followed by immunogold labeling. The epithelium consists of 4 morphologically distinct cell-types, namely, the basal, spiny, granular and squamous cells, and each of these exhibits a different immunolabeling pattern. The basal cells form a layer on the basal lamina, and in these a diffuse cytoplasmic staining is observed. This basal cell layer is overlaid by spiny cells that extend many cell processes into wide intercellular spaces. In these cells, immunogold particles are found only on small granular inclusions consisting of an electron-lucent homogeneous substance. The granular cells form a third layer over the spiny cells, and are characterized by a number of large granular inclusions with an electron-dense core rimmed by a less electron-dense substance. Immunogold labeling is found on these granules, both on the core and peripheral region. Squamous cell-types constitute the most superficial layer of the epithelium. They are without granular inclusions, and immunogold labeling is confined to the cytoplasmic surface of the thickened plasma membrane. These findings suggest that L-36 is produced in the basal cells as free cytosolic protein, then becomes progressively aggregated into the granular inclusions of the spiny and granular cells, and is eventually transferred onto the cytoplasmic surface of the squamous cell plasma membrane where it may interact with complementary glycoconjugate(s) located at this site. The membrane lining substance thus formed may play a role in stabilizing the squamous cell membranes, thereby maintaining the structural integrity of the epithelium against mechanical stress coming from the esophageal lumen.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00307960
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  • 3
    Electronic Resource
    Electronic Resource
    Immunohistochemical localization of 14 kDa β-galactoside-binding lectin in various organs of rat (1990)
    Springer
    Cell & tissue research 259 (1990), S. 43-49 
    Details
    ISSN: 1432-0878
    Keywords: Lectin ; Smooth muscle cells ; Immunohistochemistry ; Rat (Wistar)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Immunohistochemical localization of 14 kDa β-galactoside-binding lectin in various organs of adult rat was achieved using a monospecific antibody raised against lectin purified from rat lung. The antibody-stained cells were formed into small aggregates, thin fascicles, or thick bundles in the walls of blood vessels, gastrointestinal tracts and urogenital organs. From the patterns of distribution, as well as their organization, these immunoreactive cells were regarded as smooth muscle cells. This was confirmed by a double immunofluorescence study using a mixture of anti 14 kDa lectin and anti α-smooth muscle-specific actin antibodies. Strong 14 kDa lectin immunoreactivity was seen in the pericellular matrix of smooth muscle cells in intact organs as well as in detergent-treated organs from which all cellular components were extracted. From these findings, it is suggested that the 14 kDa lectin may be externalized by smooth muscle cells into their pericellular matrix and participate in the crosslinking of the complementary glycoconjugate(s) localized at that site. The macromolecular complex of glycoconjugates thus formed around smooth muscle cells may play a role in anchoring smooth muscle cells to the pericellular connective tissue thereby permitting the force of muscle contraction to be efficiently transmitted to the surrounding connective tissue proper.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00571428
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  • 4
    Electronic Resource
    Electronic Resource
    Rat intestinal galactoside-binding lectin L-36 functions as a structural protein in the superficial squamous cells of the esophageal epithelium (1995)
    Springer
    Cell & tissue research 281 (1995), S. 77-83 
    Details
    ISSN: 1432-0878
    Keywords: Esophagus ; Epithelial cells ; Intestinal lectin, L-36 ; RI-H fragment ; Immunocytochemistry ; Rat (Wistar)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Using an affinity purified antibody raised against the RI-H fragment of rat intestinal lectin L-36, the latter protein has been identified within the esophageal epithelium by means of ultracryotomy followed by immunogold labeling. The epithelium consists of 4 morphologically distinct cell-types, namely, the basal, spiny, granular and squamous cells, and each of these exhibits a different immunolabeling pattern. The basal cells form a layer on the basal lamina, and in these a diffuse cytoplasmic staining is observed. This basal cell layer is overlaid by spiny cells that extend many cell processes into wide intercellular spaces. In these cells, immunogold particles are found only on small granular inclusions consisting of an electron-lucent homogeneous substance. The granular cells from a third layer over the spiny cells, and are characterized by a number of large granular inclusions with an electron-dense core rimmed by a less electron-dense substance. Immunogold labeling is found on these granules, both on the core and peripheral region. Squamous cell-types constitute the most superficial layer of the epithelium. They are without granular inclusions, and immunogold labeling is confined to the cytoplasmic surface of the thickened plasma membrane. These findings suggest that L-36 is produced in the basal cells as free cytosolic protein, then becomes progressively aggregated into the granular inclusions of the spiny and granular cells, and is eventually transferred onto the cytoplasmic surface of the squamous cell plasma membrane where it may interact with complementary glycoconjugate(s) located at this site. The membrane lining substance thus formed may play a role in stabilizing the squamous cell membranes, thereby maintaining the structural integrity of the epithelium against mechanical stress coming from the esophageal lumen.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00307960
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  • 5
    Electronic Resource
    Electronic Resource
    Target-specific innervation by autonomic and sensory nerve fibers in hairy fetal skin transplanted into the anterior eye chamber of adult rat (1991)
    Springer
    Cell & tissue research 266 (1991), S. 259-263 
    Details
    ISSN: 1432-0878
    Keywords: Hairy skin tissue fetal ; Transplantation ; Anterior eye chamber ; Immunohistochemistry ; Rat (Wistar)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Pieces of hairy skin tissue of fetal rat were transplanted into the anterior eye chamber of adult rats. The ability of autonomic and sensory nerve fibers from the host iris to innervate the grafted skin tissue was immunohistochemically and enzyme-histochemically examined using antisera against tyrosine hydroxylase (TH), substance P (SP), calcitonin gene-related peptide (CGRP) and vasoactive intestinal peptide (VIP), and a reaction medium for acetylcholinesterase (AchE). The grafted tissue was successfully implanted and connected with the host iris. Epidermis, dermis, subcutaneous tissue, hairs, hair follicles, sebaceous glands, and piloerector muscles developed in the graft. Two weeks after transplantation, TH-, SP-, and CGRP-immunoreactive fibers were observed in association with the blood vessels in the graft. Four weeks after transplantation, TH-immunoreactive fibers were distributed in the piloerector muscles, whereas SP-and CGRP-immunoreactive fibers were present around the hair follicles. VIP-immunoreactive and AchE-positive fibers were restricted to the host iris at all survival times. These results suggest that the outgrowth of autonomic and sensory nerve fibers from the host iris show target specificity for the grafted skin tissue.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00318181
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  • 6
    Electronic Resource
    Electronic Resource
    Immunolocalization of 67 kDa elastin-binding protein in perinatal rat lungs (1992)
    Springer
    Cell & tissue research 268 (1992), S. 277-281 
    Details
    ISSN: 1432-0878
    Keywords: Lung ; Elastin-binding protein ; Lectins ; Galactose ; Monocytes ; Immunocytochemistry ; Rat (Wistar)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary 67 kDa elastin-binding protein (RL-67EBP) has been isolated from neonatal rat lungs by the use of an elastin-coupled affinity column, followed by elution with either lactose or synthetic elastin hexapeptide (VGVAPG), and immunohistochemistry has been used on perinatal rat lungs to determine the tissue localization of this protein. No immunoreactive structures occur in fetal lungs, or in the lungs of day-1 and-4 neonates. On day-7 after birth, immunoreactive cells appear in the subepithelial connective tissue of the intrapulmonary airways, from day-10 on, these cells become evenly distributed in the alveolar parenchyma. Occasionally, some cells occur in the alveolar air space, being free from the surface of the alveolar septum. Unpermeabilized cells obtained by bronchoalveolar lavage, show cell surface immunoreactivity, indicating that RL-67EBP is expressed on the surface membrane of the cells. From these findings, it is suggested that the immunoreactive cells are blood-borne monocytes, and that RL-67EBP may function as an elastin peptide receptor by which monocytes mobilize through interstitial connective tissue during their migration from blood to alveolar air space, where they eventually differentiate into alveolar macrophages.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00318796
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  • 7
    Electronic Resource
    Electronic Resource
    Genetic and physical characterization of putP, the proline carrier gene of Escherichia coli K12 (1986)
    Springer
    Molecular genetics and genomics 202 (1986), S. 35-41 
    Details
    ISSN: 1617-4623
    Keywords: Proline carrier gene ; putP ; Escherichia coli ; putC ; proT
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Two new mutants of E. coli K12, strains PT9 and PT32 were isolated, that were defective in proline transport. They had no high affinity proline transport activity, but their cytoplasmic membranes retained proline binding activity with altered sensitivity to inhibition by p-chloromercuribenzoate(pCMB). The lesion was mapped at the putP gene, which is located at min 23 on the revised E. coli genetic map (Bachmann 1983) as a composite gene in the proline utilization gene cluster, putP, putC, and putA, arranged in this order. The putC gene was shown to regulate the synthesis of proline dehydrogenase (putA gene product). Hybrid plasmids carrying the put region (Motojima et al. 1979; Wood et al. 1979) were used to construct the physical map of the put region. The possible location of the putP gene in the DNA segment was determined by subcloning the putP gene, genetic complementation, and recombination analyses using several proline transport mutants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00330513
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  • 8
    Electronic Resource
    Electronic Resource
    Nucleotide sequence of putP, the proline carrier gene of Escherichia coli K12 (1987)
    Springer
    Molecular genetics and genomics 208 (1987), S. 70-75 
    Details
    ISSN: 1617-4623
    Keywords: Proline carrier gene ; putP ; Escherichia coli ; DNA sequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The nucleotide sequence of the putP gene coding for the proline carrier in Escherichia coli has been determined and the amino acid sequence of the proline carrier deduced from it. The proline carrier is predicted to consist of 502 amino acids, resulting in a molecular weight of 54,343. The predicted protein is very hydrophobic (70% nonpolar amino acids), and its hydropathy profile suggests that it is composed of 12 hydrophobic segments with a mean length of 24.4 residues/segment. If these segments are assumed to be α-helical, the mean length of each domain corresponds to the thickness of the hydrophobic core of the membrane. Potential promoter, catabolite gene activator protein (CAP) binding sites and several palindromic sequence, which might be regulatory regions by the putA gene product, were also found in the 5′ flanking region of the postulated putP gene. A typical p-independent transcription termination signal was found after the terminator codon of the putP gene.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00330424
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  • 9
    Electronic Resource
    Electronic Resource
    Nucleotide sequence of putC, the regulatory region for the put regulon of Escherichia coli K12 (1987)
    Springer
    Molecular genetics and genomics 210 (1987), S. 364-368 
    Details
    ISSN: 1617-4623
    Keywords: Promoter region of the putA gene ; putC ; Nucleotide sequence ; Escherichia coli ; nitrogen control
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The nucleotide sequence of the putC region, from which divergent transcription of the putP and putA genes starts, was determined. The promoter region for the putA gene was restricted to the location between the HindIII site and the NcoI site or at the NcoI site by using putA-lacZ fusion plasmids and the transcriptional start for the putA gene was identified in the region between the HindIII site and the NcoI site by S1 mapping. This region also contains a potential CAP binding site, a ribosome binding site, and a sequence that is highly homologous to argTr. five potential promoters (putPp1-putPp5) for the putP gene, which were separate from the promoter region for the putA gene, were indicated by S1 mapping analysis of the putP gene transcripts. We concluded that the putC region is 419 bp long and contains two independent sets of promoters, regulating the expression of putP and putA genes in opposite directions. In addition, this region was found to contain an open reading frame (orf) capable of encoding a polypeptide of 111 amino acids in overlapping fashion. But studies using an orf-lacZ fusion gene showed that this open reading frame was not expressed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00325707
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  • 10
    Electronic Resource
    Electronic Resource
    Nucleotide sequence of the cybB gene encoding cytochrome b 561 in Escherichia coli K12 (1988)
    Springer
    Molecular genetics and genomics 212 (1988), S. 1-5 
    Details
    ISSN: 1617-4623
    Keywords: Cytochrome b 561 ; Diheme b-type cytochrome ; cybB gene ; Escherichia coli ; DNA sequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The complete nucleotide sequence of the Escherichia coli cybB gene for diheme cytochrome b 561 and its flanking region was determined. The cybB gene comprises 525 nucleotides and encodes a 175 amino acid polypeptide with a molecular weight of 20160. From its deduced amino acid sequence, cytochrome b 561 is predicted to be very hydrophobic (polarity 33.7%) and to have three membrane spanning regions. Histidines, canonical ligand residues for protohemes, are localized in these regions, and the heme pockets are thought to be in the cytoplasmic membrane. No significant homology of the primary structure of cytochrome b 561 with those of other bacterial b-type cytochromes was observed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00322437
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