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  • 1
    Electronic Resource
    Electronic Resource
    Detection and identification of Flavobacterium psychrophilum from gill washings and benthic diatoms by PCR-based sequencing analysis (2005)
    Oxford, UK : Blackwell Science Ltd
    Journal of fish diseases 28 (2005), S. 0 
    Details
    ISSN: 1365-2761
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: A nested polymerase chain reaction (PCR) amplification technique was used to detect Flavobacterium psychrophilum from washings of fish gill surfaces and benthic diatoms as environmental samples. Gill washing samples were prepared from kawamutsu, Zacco temminckii (Temminck & Schlegel) and oikawa, Z. platypus (Temminck & Schlegel). Benthic diatom samples were collected from stone surfaces. All samples were collected from rivers in Wakayama Prefecture, Japan from November 2003 to January 2004. Following simple DNA extraction using a chelating resin, nested PCR techniques targeting 16S-rDNA and gyrB regions were performed, and PCR products were cloned and sequenced. With nested PCR amplification for the 16S-rDNA gene, ambiguous PCR products were detected from two of six samples, and by cloning and sequencing analysis were found not to be DNA fragments amplified from F. psychrophilum. Using nested PCR for the gyrB gene, however, five of six samples were clearly positive for F. psychrophilum in agarose gel electrophoresis, and were found to be identical with nucleotide sequences of F. psychrophilumgyrB deposited in DNA databases by sequencing analysis. Results indicate that nested PCR for the gyrB region is a useful technique to detect low levels of F. psychrophilum from environmental samples contaminated with many other organisms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2761.2005.00663.x
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  • 2
    Electronic Resource
    Electronic Resource
    A novel serotype of Flavobacterium psychrophilum detected using antiserum against an isolate from amago, Oncorhynchus masou rhodurus Jordan & Gilbert, in Japan (2003)
    Oxford, UK : Blackwell Science Ltd
    Journal of fish diseases 26 (2003), S. 0 
    Details
    ISSN: 1365-2761
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2761.2003.00502.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Purification and characterization of cathepsin H fromhepatopancreas of carp Cyprinus carpio
    Amsterdam : Elsevier
    Comparative Biochemistry and Physiology -- Part B: Biochemistry and 102 (1992), S. 499-505 
    Details
    ISSN: 0305-0491
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0305-0491(92)90040-X
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  • 4
    Electronic Resource
    Electronic Resource
    Epidermal response of the Japanese eel to environmental stress (1998)
    Springer
    Fish physiology and biochemistry 19 (1998), S. 197-203 
    Details
    ISSN: 1573-5168
    Keywords: epidermal cathepsins ; Japanese eel ; Anguilla japonica ; proteolytic activity ; bacteriolytic activity ; hemolytic activity ; immune response ; primary defence ; thermal adaptation ; bacterial infection
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Nonspecific responses of Japanese eels to environmental stress were monitored by assaying various lytic activities in eel epidermal extract. In fish maintained at 10 and 30 °C for up to 10 days, epidermal proteolytic activities due to serine protease and aminopeptidase and hemolytic activity varied within a 2-fold value range. Other proteolytic activities, due to cathepsins B and L, in the fish at 30 °C increased for up to 8 days and were 3.4 and 2.9-fold over those in fish maintained at 10 °C, respectively. This was accompanied by a 3.0-fold increase in bacteriolytic activity. Other forms of stress were exerted on the fishes by immersing them in a suspension of Flavobacterium columnare or giving them intraperitoneal injections of Edwardsiella tarda over 72 h. Although serine protease and aminopeptidase activities and hemolytic activity in the fishes exposed to F. columnare changed marginally, and were similar to those in the control fish, cathepsins B and L activities in the infected fishes increased more than 1.5-fold over their initial values over a 48 h period, along with a 4.5-fold increase in bacteriolytic activity. No marked change was detected in any of the lytic activities of the fishes exposed to E. tarda. These findings indicate that epidermal cathepsins B and L probably participate in bacteriolysis associated with Japanese eel skin and that their activities are elicited by environmental stimuli and may be an important nonspecific response of eels. Abbreviations: Cbz – carbobenzoxy; MCA – 4-methylcoumaryl-7-amide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007746514851
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  • 5
    Electronic Resource
    Electronic Resource
    Fluorescence localization of epidermal cathepsins L and B in the Japanese eel (1998)
    Springer
    Fish physiology and biochemistry 19 (1998), S. 205-209 
    Details
    ISSN: 1573-5168
    Keywords: direct activity detection ; epidermal cathepsins ; fluorescence microscopy ; histochemical localization ; Japanese eel ; primary defense ; secretory cells ; skin ; Anguilla japonica
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Histochemical localization of proteolytic activities in the dorsal epidermis of Japanese eel was demonstrated by fluorescent microscopy utilizing 4-methoxy-2-naphthylamide (4M$\beta$NA) derivatives as substrates and 5-nitrosalicylaldehyde as a trapping agent. Carbobenzoxy-L-phenylalanyl-L-arginyl-4M$\beta$NA (Cbz-Phe-Arg-4M$\beta$NA) and Cbz-Arg-Arg-4M$\beta$NA were used for direct detection of cathepsins L and B activities, respectively, in fresh frozen sections and unfixed cells of the eel epidermis. The fluorescing areas, where Cbz-Phe-Arg-4M$\beta$NA was hydrolyzed by cathepsin L, were shown in mucus secretory cells and club cells and broadly around skin surface. The fluorescing areas due to Cbz-Arg-Arg-4M$\beta$NA hydrolysis by cathepsin B were localized similarly in these tissues. The fluorescing intensity for both catheptic activities in mucus secretory cells was higher than that in club cells, where small fluorescing granules were distributed. These results indicate that eel cathepsins L and B are stored in epidermal secretory cells at different levels and probably serve as defense factors before or after secretion by these cells. Abbreviations: Cbz – carbobenzoxy; 4M$\beta$NA – 4-methoxy-2-naphthylamide; NSA – 5-nitrosalicylaldehyde.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007779600183
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  • 6
    Electronic Resource
    Electronic Resource
    Lysis of pathogenic bacteria by epidermal cathepsins L and B in the Japanese eel (1999)
    Springer
    Fish physiology and biochemistry 20 (1999), S. 37-41 
    Details
    ISSN: 1573-5168
    Keywords: Anguilla japonica ; bacterial diseases ; bacteriolysis ; epidermal cathepsins ; Japanese eel nonspecific defense ; pathogenic bacteria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cysteine proteases, cathepsins L and B, in Japanese eel epidermis are suspected bacteriolysins against aquatic pathogens. This work examines the lysis of three species of gram-negative pathogenic bacteria by the eel epidermal extract according to the assay method for cysteine proteases. The optimum pH for the lysis of the three species of bacteria were commonly determined to be 5.0, where both of eel epidermal cathepsins L and B caused active proteolysis. Four kinds of specific inhibitors for cysteine proteases strongly inhibited these catheptic proteolyses and bacteriolyses. The activities for the lysis of three types of bacteria were at a similar level, but the effects on the bacterium which infects predominantly eel skin largely varied with individual fish. These results suggest that epidermal cathepsins L and B are responsible for lysis of any pathogenic bacteria in the nonspecific defense of Japanese eel.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007763711158
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  • 7
    Electronic Resource
    Electronic Resource
    Epidermal proteases of the Japanese eel (1997)
    Springer
    Fish physiology and biochemistry 16 (1997), S. 471-478 
    Details
    ISSN: 1573-5168
    Keywords: epidermal proteases ; Japanese eel ; Anguilla japonica ; skin ; mucus ; primary defence ; fluorescent assay ; proteolytic factor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A fluorescent-sensitive assay was used to demonstrate the protease activity in the dorsal skin of Japanese eel (Anguilla japonica). Two distinct extracts were separately prepared from skin mucus and epidermal cell layers, with no mutual contamination. The epidermal extract was sensitive to various substrates, whereas there was no, or only marginal, susceptibility to the same substrates for the mucous extract. Optimum hydrolysis pHs of the epidermal extract was variable and below pH 7.0, and the optimum hydrolysis temperatures were between 40 and 50 °C. In addition, Tos-Phe-Ch2Cl, chymostatin, CdCl2, CuCl2, HgCl2 and ZnCl2 inhibited protease activities to different extents. Several other reagents specifically affected the protease activities, and their induced effects were useful for the identification of epidermal proteases. The findings indicate that a proteolytic factor, exhibiting various enzymological specificities, is retained within epidermal cell layers of Japanese eel. This factor is composed of 4 distinct proteases, such as cathepsins L and B-like proteases, a serine protease and an aminopeptidase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007736804243
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