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  • 1
    Electronic Resource
    Electronic Resource
    Haemoglobin receptor protein is intragenically encoded by the cysteine proteinase-encoding genes and the haemagglutinin-encoding gene of Porphyromonas gingivalis (1998)
    Oxford BSL : Blackwell Publishing Ltd
    Molecular microbiology 27 (1998), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The obligately anaerobic bacterium Porphyromonas gingivalis produces characteristic black-pigmented colonies on blood agar. It is thought that the black pigmentation is caused by haem accumulation and is related to virulence of the microorganism. P. gingivalis cells expressed a prominent 19 kDa protein when grown on blood agar plates. Analysis of its N-terminal amino acid sequence indicated that the 19 kDa protein was encoded by an internal region (HGP15 domain) of an arginine-specific cysteine proteinase (Arg-gingipain, RGP)-encoding gene (rgp1) and was also present in genes for lysine-specific cysteine proteinases (prtP and kgp) and a haemagglutinin (hagA) of P. gingivalis. The HGP15 domain protein was purified from an HGP15-overproducing Escherichia coli and was found to have the ability to bind to haemoglobin in a pH-dependent manner. The anti-HGP15 antiserum reacted with the 19 kDa haemoglobin-binding protein in the envelope of P. gingivalis. P. gingivalis wild-type strain showed pH-dependent haemoglobin adsorption, whereas its non-pigmented mutants that produced no HGP15-related proteins showed deficiency in haemoglobin adsorption. These results strongly indicate a close relationship among HGP15 production, haemoglobin adsorption and haem accumulation of P. gingivalis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1998.00656.x
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  • 2
    Electronic Resource
    Electronic Resource
    Increased Expression of Cathepsins E and D in Neurons of the Aged Rat Brain and Their Colocalization with Lipofuscin and Carboxy-Terminal Fragments of Alzheimer Amyloid Precursor Protein (1997)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 68 (1997), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Age-related changes in the expression and localization of two distinct intracellular aspartic proteinases, cathepsin E (CE) and cathepsin D (CD), were investigated in the rat cerebral cortex and the brainstem by immunocytochemical and quantitative methods using discriminative antibodies specific for each enzyme. Non-lysosomal CE was barely detectable in these two brain tissues in the embryonic stages, whereas relatively high expression of lysosomal CD was observed in embryonic tissues. After birth, CE was increasingly expressed in these tissues with aging to attain maximal levels at 30 months of age. Western blot analyses revealed that CE existed predominantly as the mature enzyme at 2 and 17 months of age, whereas it was present as not only the mature enzyme but also the proenzyme at 30 months of age. On the other hand, CD was mainly present in the mature form throughout development, although its level in these tissues was also significantly increased with aging. The CE-positive cortical and brainstem neurons of the aged rat corresponded well with cells emitting autofluorescence for lipopigments. By the double-staining technique, most of the CE-positive cortical and brainstem neurons of the aged rat were also positive for antibody to the carboxyl-terminal fragments of amyloid precursor protein (APP634–695), intracellular accumulation of which is thought to be associated with age-related changes in the endosome/lysosome system. It is important that electron microscopy revealed that CE in brainstem neurons of the aged rat colocalized with CD in the lipofuscin-containing lysosomes. These results indicate that aging results in the increased expression and lysosomal localization of CE in cortical and brainstem neurons and changes in the endosomal/lysosomal proteolytic system, which may be related to lipofuscinogenesis and altered intracellular APP metabolism.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1997.68020739.x
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  • 3
    Electronic Resource
    Electronic Resource
    Excitotoxin-Induced Neuronal Death Is Associated with Response of a Unique Intracellular Aspartic Proteinase, Cathepsin E (1998)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 71 (1998), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Excitotoxicity produced by excessive stimulation of glutamate receptors is known to lead to neuronal lesion and death. Here, we demonstrate that quantitative and qualitative changes in cathepsin E (CE) gene products are associated with execution of the excitotoxic neuronal death. Intracerebroventricular injection of kainate (KA) resulted in marked elevation of both mRNA and protein levels of CE in the rat hippocampal CA3 region, where the enzyme was mainly found in vulnerable neurons and activated microglia. Northern blot analysis showed that the size of the transcript for CE was identical with that normally expressed in rat spleen. Immunoblot analysis, however, revealed the predominant occurrence of the highly modified CE species, besides the mature CE. This polypeptide was distinct from the mature CE in molecular masses (106 vs. 82 kDa) and pl (6.4–7.3 vs. 5.0–5.5) and showed resistance to conversion into the enzymatically active form by acid treatment. Consistent with these in vivo results, administration of glutamate to primary cultured rat hippocampal neurons resulted in a marked expression of this novel CE species. These data indicate that excessive stimulation of glutamate receptors causes induction of the CE gene response followed by persistent expression of CE in the novel form, besides its mature form, predominantly in the hippocampal neurons.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1998.71062574.x
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  • 4
    Electronic Resource
    Electronic Resource
    Identification of Cellular Compartments Involved in Processing of Cathepsin E in Primary Cultures of Rat Microglia (1998)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 70 (1998), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Cathepsin E is a major nonlysosomal, intracellular aspartic proteinase that localizes in various cellular compartments such as the plasma membrane, endosome-like organelles, and the endoplasmic reticulum (ER). To learn the segregation mechanisms of cathepsin E into its appropriate cellular destinations, the present studies were initiated to define the biosynthesis, processing, and intracellular localization as well as the site of proteolytic maturation of the enzyme in primary cultures of rat brain microglia. Immunohistochemical and immunoblot analyses revealed that cathepsin E was the most abundant in microglia among various brain cell types, where the enzyme existed predominantly as the mature enzyme. Immunoelectron microscopy studies showed the presence of the enzyme predominantly in the endosome-like vacuoles and partly in the vesicles located in the trans-Golgi area and the lumen of ER. In the primary cultured microglial cells labeled with [35S]methionine, 〉95% of labeled cathepsin E were represented by a 46-kDa polypeptide (reduced form) after a 30-min pulse. Most of it was proteolytically processed via a 44-kDa intermediate to a 42-kDa mature form within 4 h of chase. This processing was completely inhibited by bafilomycin A1, a specific inhibitor of vacuolar-type H+-ATPase. Brefeldin A, a blocker for the traffic of secretory proteins from the ER to the Golgi complex, also inhibited the processing of procathepsin E and enhanced its degradation. Procathepsin E, after pulse-labeling, showed complete susceptibility to endoglycosidase H, whereas the mature enzyme almost acquired resistance to endoglycosidases H as well as F. The present studies provide the first evidence that cathepsin E in microglia is first synthesized as the inactive precursor bearing high-mannose oligosaccharides and processed to the active mature enzyme with complex-type oligosaccharides via the intermediate form and that the final proteolytic maturation step occurs in endosome-like acidic compartments.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1998.70052045.x
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  • 5
    Electronic Resource
    Electronic Resource
    Helical Structure Formation Between Complementary Oligonucleotides. Minimum Chain Length Required for the Template-Directed Synthesis of Oligonucleotides (1997)
    Springer
    Origins of life and evolution of the biospheres 27 (1997), S. 525-533 
    Details
    ISSN: 1573-0875
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Geosciences
    Notes: Abstract Helix formation between various combinations of 3‘–5’ linked oligoribouridylates and oligoriboadenylates from dimer to dodecamer has been studied to gain information on the chain-length requirement for the template-directed condensation of oligoribonucleotides. We have measured the helix formation under high oligoribonucleotide concentration in the presence of magnesium ion at 0–50°C by UV or CD, as many model processes of oligoribonucleotides replication have been carried out under such conditions. Adenylic acid, (pA), diadenylic acid, (pA)2, or triadenylic acid, (pA)3, forms a helix with poly(U) or oligo(U) with a chain length of more than eight. On the other hand, neither uridylic acid, (pU), nor diuridylic acid, (pU)2, can form a helix with oligo(A) or poly(A). Triuridylic acid, (pU)3, or the longer oligo(U) forms a helix with oligo(A) with a chain length of over six. The results suggest that a trimer is the minimum unit as an incorporating nucleotide for conducting any set of nonenzymatic template-directed synthesis, A→U and U→A, as the nonenzymatic template-directed condensation of oligoribonucleotides correlates well with the results of helix formation of complementary oligoribonucleotides. We have further found the partial helix formation between 2‘–5’ linked decauridylate, (pU)10, and pA or 2‘–5’ linked (pA)2 at 0 °C, which indicates the possibility of the template activity of long 2‘–5’ linked oligonucleotides for the nonenzymatic oligonucleotide synthesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006566212455
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  • 6
    Electronic Resource
    Electronic Resource
    Ascending myelinated axons of primary sensory neurons of the sciatic nerve in the posterior column of the rat spinal cord (1996)
    Springer
    Acta neuropathologica 92 (1996), S. 27-34 
    Details
    ISSN: 1432-0533
    Keywords: Key words Myelinated axon ; Primary sensory neuron ; Posterior column ; Morphometry ; Doxorubicin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The present study was undertaken to obtain morphologic data about the posterior column of the spinal cord to characterize ascending myelinated axons of primary sensory neurons of the sciatic nerve. By applying doxorubicin to the right sciatic nerve in eight male Wistar rats, selective degeneration of centrally directed axons of these neurons in the posterior column was produced. Epon-embedded transverse sections of the posterior column at spinal cord segments C1, C3, C8, T6, L3 and L5 showed a circumscribed area (R) that contained a cluster of degenerated myelinated fibers. To characterize area R, its size and distances between various defined points on transverse sections of the posterior column were measured and compared at several spinal segments. The location of area R was illustrated in representative rats. The posterior intermediate septum corresponded to the lateral border of area R at C8 and T6. To characterize the putatively degenerating and degenerated myelinated fibers, area L in the left posterior column, corresponding to area R, was defined, and subsequently the number and size distribution of normal-appearing myelinated fibers in areas R and L were evaluated at C3, T6 and L3 in four rats. After comparative evaluation of these data, it was concluded that large myelinated fibers degenerated preferentially in area R. The number of putatively degenerating and degenerated myelinated fibers in area R at segments C3 and T6 was estimated to be 38.6% and 50.1%, respectively, of that at segment L3.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004010050485
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  • 7
    Electronic Resource
    Electronic Resource
    Specific immunocytochemical localization of cathepsin E at the ruffled border membrane of active osteoclasts (1995)
    Springer
    Cell & tissue research 281 (1995), S. 85-91 
    Details
    ISSN: 1432-0878
    Keywords: Cathepsin E ; Aspartic proteinase ; Osteoclasts ; Immunocytochemistry ; Rat (WKA)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The immunocytochemical localization of cathepsin E, a non-lysosomal aspartic proteinase, was investigated in rat osteoclasts using the monospecific antibody to this protein. At the light-microscopic level, the preferential immunoreactivity for cathepsin E was found at high levels in active osteoclasts in the physiological bone modeling process. Neighboring osteoblastic cells were devoid of its immunoreactivity. At the electron-microscopic level, cathepsin E was exclusively confined to the apical plasma membrane at the ruffled border of active osteoclasts and the eroded bone surface. Cathepsin E was also concentrated in some endocytotic vacuoles of various sizes in the vicinity of the ruffled border membrane, some of which appeared to be secondary lysosomes containing the phagocytosed materials. These results strongly suggest that this enzyme is involved both in the extracellular degradation of the bone organic matrix and in the intracellular breakdown of the ingested substances in osteoclasts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00307961
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  • 8
    Electronic Resource
    Electronic Resource
    Specific immunocytochemical localization of cathepsin E at the ruffled border membrane of active osteoclasts (1995)
    Springer
    Cell & tissue research 281 (1995), S. 85-91 
    Details
    ISSN: 1432-0878
    Keywords: Key words: Cathepsin E ; Aspartic proteinase ; Osteoclasts ; Immunocytochemistry ; Rat (WKA)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. The immunocytochemical localization of cathepsin E, a non-lysosomal aspartic proteinase, was investigated in rat osteoclasts using the monospecific antibody to this protein. At the light-microscopic level, the preferential immunoreactivity for cathepsin E was found at high levels in active osteoclasts in the physiological bone modeling process. Neighboring osteoblastic cells were devoid of its immunoreactivity. At the electron-microscopic level, cathepsin E was exclusively confined to the apical plasma membrane at the ruffled border of active osteoclasts and the eroded bone surface. Cathepsin E was also concentrated in some endocytotic vacuoles of various sizes in the vicinity of the ruffled border membrane, some of which appeared to be secondary lysosomes containing the phagocytosed materials. These results strongly suggest that this enzyme is involved both in the extracellular degradation of the bone organic matrix and in the intracellular breakdown of the ingested substances in osteoclasts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00307961
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  • 9
    Electronic Resource
    Electronic Resource
    Angiogenic growth factor release system for in vivo tissue engineering: a trial of bone marrow transplantation into ischemic myocardium (1999)
    Springer
    Journal of artificial organs 2 (1999), S. 85-91 
    Details
    ISSN: 1619-0904
    Keywords: In vivo tissue engineering ; Bone marrow transplantation ; bFGF ; Release system of angiogenic growth factors ; Revascularization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine , Technology
    Notes: Abstract For successful in vivo tissue engineering, a growth factor release system will be useful. We adopted autologous bone marrow transplantation as an angiogenic growth factor release system. Bone marrow transplanted into a synthetic vascular prosthesis produced continuous synthesis of angiogenic growth factors, resulting in rapid neointima formation on the prosthesis after implantation. We expected a similar angiogenic phenomenon to occur if bone marrow was transplanted into ischemic myocardium. Bone marrow was transplanted into ischemic myocardium created in dogs. Marrow cells continued synthesis of angiogenic growth factors, which were effective in protecting the capillary network from ischemia, but not myocytes. Autologous bone marrow was injected intramuscularly into ischemic myocardium created in the left ventricular wall of dogs. Control operations were performed without bone marrow. On days 3 and 7, marrow cells survived, and their adjacent cells and the surrounding extracellular matrix were immunohistochemically bFGF reactive. At 3 weeks, no marrow cells were identified. Myocytes disappeared, but the capillary blood vessel networks remained. With some exceptions, these capillaries did not contain blood cell components. In the controls, scar tissue with a very small number of capillaries was formed. In conclusion, marrow cells survived for a short period of time after transplantation, and continued synthesis of angiogenic growth factors, which were effective in protecting endothelial cells from ischemia, but not myocytes. Therefore, the results also suggest that there are limitations in the treatment of ischemic myocardium using angiogenic growth factors alone.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01235530
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