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  • 11
    Electronic Resource
    Electronic Resource
    Granulocyte medullasin levels in gingival crevicular fluid from chronic adult periodontitis patients and experimental gingivitis subjects (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 25 (1990), S. 0 
    Details
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The concentration of medullasin, an elastase-like serine proteinase, in gingival crevicular fluid (GCF) from chronic adult periodontitis patients and experimental gingivitis subjects was determined by the highly sensitive immunoassay method. In periodontitis patients, the medullasin content increased with increase of the GCF volume and then attained a maximum value at a relatively mildly inflamed stage. The value was maintained through more serious stages of disease activity. However, the medullasin content was independent of the probing depth. The medullasin content of the patients was markedly decreased after periodontal treatment, indicating that the enzyme participates in the development of the chronic periodontitis. Large amounts of medullasin were also detected in GCF from experimental gingivitis subjects, although it was not detected by the activity measurements. There was a rapid increase in the medullasin content during the 4-day period after abstention from oral hygiene measures, which corresponded to those of severely inflamed periodontitis patients. The peak value decreased up to the 7th-d followed by a gradual increase during the 21-d experimental period. The increased medullasin level rapidly decreased following resumption of oral hygiene measures. The results suggest that medullasin plays important roles both in the defence mechanism against the gingival inflammation and in the development of the acute inflammation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0765.1990.tb00927.x
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  • 12
    Electronic Resource
    Electronic Resource
    Cathepsins B, H and L activities in gingival crevicular fluid from chronic adult periodontitis patients and experimental gingivitis subjects (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 25 (1990), S. 0 
    Details
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: To clarify roles of lysosomal cysteine proteinases cathepsins B, H and L in pathological destructive process of periodontal tissues, levels of their enzymatic activities were determined in gingival crevicular fluid (GCF) from chronic adult periodontitis patients and from experimental gingivitis subjects. In periodontitis patients, higher levels of cathepsins B, H and L activities were found at sites with more serious signs of the disease activity. The total activity of each enzyme (per unit time) was positively correlated with the GCF volume. However, it had little or no correlation with the probing depth (PD). In contrast, the specific activity of each enzyme in GCF (activity units per mg protein), which reflects the selectivity of enzyme exudation, was negatively correlated with the GCF volume. These results suggest that the cysteine proteinases are selectively released into gingival crevices at a relatively mild stage of periodontitis. In experimental gingivitis subjects, no significant activity of each enzyme was detected in GCF, even when the quantity of GCF was comparable to that from periodontitis patients. These data suggest that no significant amounts of these enzymes are released at experimental gingivitis sites or that a homeostatic mechanism, including regulation by protease inhibitors, may control activities of these enzymes in GCF with acute inflammation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0765.1990.tb00894.x
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  • 13
    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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  • 14
    Electronic Resource
    Electronic Resource
    Endogenous formation of 1-methyl-1,2,3,4-tetrahydro-β-carboline-3-carboxylic acid in man as the possible causative substance of eosinophilia-myalgia syndrome associated with ingestion ofl-tryptophan (1991)
    Springer
    Archives of toxicology 65 (1991), S. 505-509 
    Details
    ISSN: 1432-0738
    Keywords: Tetrahydro-β-carboline ; Human urine ; Tryptophan pathway ; Ethanol ; Eosinopilia-myalgia syndrome
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract 1-Methyl-1,2,3,4-tetrahydro-β-carboline-3-carboxylic acid (MTCA) is now thought to be a possible causative substance of eosinophilia-myalgia syndrome associated with ingestion ofl-tryptophan. In the present study a factor affecting endogenous formation of MTCA in 32 healthy men is studied. Urinary excretions of MTCA and 1,2,3,4-tetrahydro-β-carboline-3-carboxylic acid (TCCA) were measured by high-performance liquid chromatography (HPLC) with fluorometric detection after administration of a high or low protein diet as well as peroral tryptophan (0.5 g) or ethanol (0.4 g/kg). Blood ethanol and acetaldehyde levels were determined by gas chromatography after ethanol consumption. Both, the high protein diet and tryptophan resulted in a significant rise of urinary TCCA. In contrast, ethanol intake caused increased excretion of MTCA, though a relationship between blood acetaldehyde level and urinary excretion of MTCA was not shown. We showed for the first time that an elevation of urinary excretion of MTCA following ethanol consumption in man without ingestion ofl-tryptophan tablets implicated eosinophilia-myalgia syndrome.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01977365
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  • 15
    Electronic Resource
    Electronic Resource
    Comparative study on accumulation and elimination of hexachlorobiphenyls and decachlorobiphenyl in mice (1980)
    Springer
    Bulletin of environmental contamination and toxicology 25 (1980), S. 181-187 
    Details
    ISSN: 1432-0800
    Source: Springer Online Journal Archives 1860-2000
    Topics: Energy, Environment Protection, Nuclear Power Engineering , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01985508
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  • 16
    Electronic Resource
    Electronic Resource
    Detection of 4-hydroxy-BHT residues in laboratory animals as an indicator of exposure to butylated hydroxytoluene (BHT) (1984)
    Springer
    Bulletin of environmental contamination and toxicology 33 (1984), S. 533-537 
    Details
    ISSN: 1432-0800
    Source: Springer Online Journal Archives 1860-2000
    Topics: Energy, Environment Protection, Nuclear Power Engineering , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01625580
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  • 17
    Electronic Resource
    Electronic Resource
    Using the scoparone O-demethylase assay for categorizing types of hepatic microsomal monooxygenase inducers (1989)
    Springer
    Bulletin of environmental contamination and toxicology 42 (1989), S. 489-494 
    Details
    ISSN: 1432-0800
    Source: Springer Online Journal Archives 1860-2000
    Topics: Energy, Environment Protection, Nuclear Power Engineering , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01700226
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  • 18
    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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  • 19
    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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  • 20
    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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