Body surface metalloprotease activity in Apis mellifera L. workers relative to environmental pollution

• Autorzy: Strachecka A. , Borsuk G. , Paleolog J. , Olszewski K. , Chobotow J. , Skoczylas D.
• Języki publikacji: EN

Abstrakty

EN

Metalloproteases are enzymes containing metallic ions, predominantly zinc ions, in their active sites. They are important for the maintenance of homeostasis and prevention of infections. The study was aimed at analysing the activity of metalloproteases on the cuticle of bees depending on environmental pollution and the development stage of the bees. The experiments were conducted on bees from two apiaries: one located in a polluted environment (close to the trunk road no. 17) and the other situated in a clean area (Nowiny). Eggs, larvae and pupae, as well as one-day-old, two-week-old, three-week-old and four-week-old workers, were collected in spring, summer, autumn and winter. The following methods were employed: protein content testing by the Lowry method (modified by Schacterle-Pollack) and metalloprotease activity testing by the Lee and Lin method (using o-phenantroline). Protein concentration values were found to be higher in the eggs, larvae and pupae than in the workers in both environments. Metalloprotease activity was not observed in the workers from the clean environment, but it was found in those kept in the polluted area. An elevated metalloprotease activity in the latter environment was observed only in summer. Bee workers, which synthesise and secrete metalloproteases onto their body surface, can be regarded as bioindicators of environmental pollution.

• Wydawca: -
• Czasopismo: Medycyna Weterynaryjna
• Rocznik: 2012
• Tom: 68
• Numer: 07
• Opis fizyczny: p.406-410,fig.,ref.

Twórcy

autor

Strachecka A.

• Department of Biological Basis of Animal Production, Faculty of Biology and Animal Breeding, University of Life Sciences in Lublin, Akademicka 13, 20-950 Lublin, Poland

autor

Borsuk G.

autor

Paleolog J.

autor

Olszewski K.

autor

Chobotow J.

autor

Skoczylas D.

Bibliografia

• 1.Atwood J., Steed J.: Encyclopedia of supramolecular chemistry. Teylor and Francis, New York 2004, 1632-1636.
• 2.Bania J., Polanowski A.: Bioinsecticides and insect defense mechanisms. Post. Biochem. 1999, 45, 143-150.
• 3.Billingsley P.: Blood digestion in the mosquito, Anopheles stephensi Liston (Diptera: Culicidae): Partial characterization and post-feeding activity of midgut aminopeptidases. Arch. Insect Biochem. Physiol. 1999, 15, 116-146.
• 4.Cornette R., Farine J., Quennedey B., Riviere S., Brossut R.: Molecular characterization of Lma-p45, a new epiculticular surface protein in the cockroach Leucophaea maderae (Dictyoptera, oxyhaloine). Insect Biochem. Mol. Biol. 2002, 32, 1635-1642.
• 5.Currie C.: A community of ants, fungi and bacteria: a multilateral approach to studying symbiosis. Annu. Rev. Microbiol. 2001, 55, 357-380.
• 6.Currie C., Scott J., Summerbell R., Malloch D.: Fungus-growing ants use antibiotic-producing bacteria to control garden parasites. Nature 1999, 398, 701-704.
• 7.Evans J., Aronstein K., Chen Y., Hetru C., Imler J., Jiang H., Kanost M., Thompson G., Zou Z., Hultmark D.: Immune pathways and defence mechanisms in honey bees Apis mellifera. Insect Mol. Biol. 2006, 15, 645-656.
• 8.Fox J., Serrano S.: Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases. Toxicon 2005, 45, 969-985.
• 9.Gliński Z., Kostro K., Luft-Deptuła D.: Apian diseases. PWRiL, Warszawa 2006, 37-73.
• 10.Gromisz Z.: Apian protection against contamination. PWRiL, Warszawa 1990, 37-55.
• 11.Harrison C., Dowdle E.: Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates. J. Apic. Res. 1980, 23, 61-63.
• 12.Heussen C., Dowdle E.: Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and co-polymerized substrates. Anal. Biochem. 1980, 102, 196-202.
• 13.Hoffel I.: Schwermetallen in Bienen und Bienenprodukten. Apidologie 1985, 16, 6-197.
• 14.Imamura N., Ishikawa T., Takeda K., Fukami H., Konno A., Nishida R.: The relationship between a leaf-rolling moth (Dactylioglypha tonica) and fungi covering the cocoon. Biosci. Biotechnol. Biochem. 2001, 65, 1965-1969.
• 15.Jorma E. Fräki, Väinö K. Hopsu-Havu: Human skin proteases. Arch. Derm. Forsch. 1972, 243, 153-163.
• 16.Laemmli U.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
• 17.Lee T., Lin Y.: Trypsin inhibitor and trypsin-like protease activity in air- or submergence-grown rice (Oryza sativa L.) coleoptiles. Plant Sci. 1995, 106, 43-54.
• 18.North M.: Comparative biochemistry of the proteinases of eukaryotic microorganisms. Microbiol. Rev. 1982, 46, 308-340.
• 19.Pavlukova E., Belozersky M., Dunaevsky Y.: Extracellular proteolityc enzymes of filamentous fungi. Biochemistry (Moscow) 1998, 63, 1059-1089.
• 20.Pliszczyński M., Chełmiński M., Bizoń K.: Hemocytic immune parameters of the wintering workers of the honey bee Apis mellifera L. (Apidae). Ann. Univ. Mariae Curie-Skłodowska 2006, 20, 157-172.
• 21.Pliszczyński M., Luft-Deptuła D., Bizoń K.: Monitoring the resistance of wintering honeybee workers, Apis mellifera L. (Apidae) based on the protective activity test. Ann. Univ. Mariae Curie-Skłodowska 2006, 21, 173-178.
• 22.Ray J., Stetler-Stevenson W.: The role of matrix metalloproteases and their inhibitors in tumour invasion, metastasis and angiogenesis. Eur. Respir. J. 1994, 7, 2062-2072.
• 23.Rohlfs M.: Clash of kingdoms or why Drosophila larvae positively respond to fungal competitors. Front. Zool. 2005, 2, 1-7.
• 24.Roman A.: Bees and bee products as environmental pollution bioindicators in areas influenced by copper (LGOM) and cement and lime (Opole) industries. Zesz. Nauk. AR, Wroc³aw 1997, 323, 175-195.
• 25.SAS Institute (2002-2003) SAS/STAT User's Guide release 9.13, Cary, NC, Statistical Analysis System Institute, license 86636.
• 26.Schacterle G., Pollack R.: Simplified method for quantitative assay of small amounts of protein in biological material. Anal. Biochem. 1973, 51, 654-655.
• 27.Walter R., Clèlia F.: Insect digestive enzymes: properties, compartmentalization and function. Comp. Biochem. Physiol. 1994, 109B, 1-62.
• 28.Wawrzycka-Kaflik A., Pełka M., Broniarczyk-Dyła G.: Metalloproteinases of the extracellular matrix and their tissue inhibitors - biochemical profile and clinical importance. Dermatologia Estetyczna 2007, 51, 10-16.
• 29.Zeeuwen P.: Epidermal differentiation: The role of proteases and their inhibitors. Eurpean J of Cell Biol. 2004, 83, 761-773.
• 30.Zhang N., Suh S., Blackwell M.: Microorganisms in the gut of beetles: evidence from molecular cloning. J. Invertebrate Pathol. 2003, 84, 226-233.
• 31.Żółtowska K., Frączek R., Lipiński Z.: Hydrolases of developing worker brood and newly emerged worker of Apis mellifera ceranica. J. Apic. Sci. 2011, 55, 27-35.

Uwagi

Rekord w opracowaniu