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2008 | 64 | 10 |

Tytuł artykułu

Aktywnosc inhibitorow proteaz na powierzchni ciala pszczoly miodnej

Warianty tytułu

EN
Activity of protease inhibitors on the body surface of the honeybee

Języki publikacji

PL

Abstrakty

EN
The proteolytic system of insects, both its protease activities, and protease inhibitors activities, in the hemolymph and digestive tract are poorly described. The authors present protease inhibitors activities in connection with the level of antifungal activities as a part of the honeybee body surface proteolytic system. The object of the study was to compare this in castes (the queen, workers and drones), in developmental stages (eggs, larvae, pupae and imagoes) and in seasons (spring, summer and autumn). The following methods were used: protease inhibitors activity testing by the Lee and Lin method and antifungal activity testing in the presence of marker fungi on the SABG substratum. The highest protease inhibitors activities were present on the workers and the lowest ones on the queen, according to exposure to pathogens. The highest protease inhibitors activities were present during the autumn and spring. The highest protease inhibitors activities were observed in the spring in the worker larvae (16.697 U/mg) and in the mature workers (17.605 U/mg). Surface protease inhibitors activity was not observed in the drone eggs and larvae for neutral pH and in the queen larvae and pupae for neutral and alkaline pH in the summer. The larvae and pupae were found to have higher acidic protease inhibitors activity than the imagoes. The obtained results of antifungal activity presented better enthomopathogen protection in the workers and queens than in the drones. The authors have provided data connecting body surface inhibitors with antifungal cuticle protection. Our data present an initial pattern of the honeybee body surface proteolysis, and will pave the way for future biochemical studies of immunity in this insect.

Wydawca

-

Rocznik

Tom

64

Numer

10

Opis fizyczny

s.1256-1259,tab.,bibliogr.

Twórcy

autor
  • Uniwersytet Przyrodniczy w Lublinie, ul.Akademicka 13, 20-950 Lublin

Bibliografia

  • 1.Bania J., Polanowski A.: Bioinsektycydy a mechanizmy obronne owadów. Postępy Biochemii 1999, 45, 143-149.
  • 2.Bode W., Fernandez-Catalan C., Nagase H., Maskos K.: Endoproteinase protein inhibitor interaction. AMPIS 1999, 107, 3-10.
  • 3.Bode W., Huber R.: Natural protein proteinase inhibitors and their interaction with proteinases. Eur. J. Biochem. 1992, 204, 433-451.
  • 4.Gawlik K., Poręba W., Rutowicz J.: Cystatyny, tyropiny i inhibitory homologiczne do propeptydów proteaz cysteinowych. Postępy Biochemii 2005, 51 (3), 317-327.
  • 5.Harborne J. B.: Ekologia biochemiczna. PWN, Warszawa 1997.
  • 6.Kanost M. R.: Serine proteinase inhibitors in arthropod immunity. Develop. Comp. Immunol. 1999, 23, 291-301.
  • 7.Lee Tse-Min, Lin Yaw-Huei: Trypsin inhibitor and trypsin-like protease activity in air or submergence grown rice (Oryza sativa L.) coleoptiles. Plant Sci. 1995, 106, 43-54.
  • 8.Locht A. Van de, Lamba D., Bauer M., Huber R., Friedrich T., Kroger B., Hoffken W., Bode W.: Two heads are better than one: crystal structure of insect derived double domain Kazal inhibitor rhodniin in complex with trombin. Eur. Mol. Biol. Organ. J. 1995, 14, 5149-5157.
  • 9.Malone L. A., Todd J. H., Burgess E., Christeller J. T.: Development of hypopharyngeal glands in adult honey bees fed with a Bt toxin, a biotin- -binding protein and a protease inhibitor. Apidologie 2004, 35, 655-664.
  • 10.Nirmala X., Kodrik D., Žurovec M., Sal F.: Insect silk contains both a Kunitz-type and a unique Kazal-type proteinase inhibitor. Eur. J. Biochem. 2001, 268, 2064-2073.
  • 11.Page K., Hughes V. S., Odoms K. K., Dunsmore K. E., Hershenson M. B.: German Cockroach Proteases Regulate Interleukin 8 Expression via Nuclear Factor for Interleukin 6 in Human Bronchial Epithelial Cells. Am. J. Respir. Cell Mol. Biol. 2005, 32, 229-231.
  • 12.Paleolog J.: Podział pracy w roju pszczelim jako szczytowe osiągnięcie ewolucji. Referat na BiNoZ (Katedra Biologicznych Podstaw Produkcji Zwierzęcej AR w Lublinie), UMCS 2006. 13.Prabucki J.: Pszczelnictwo. Wyd. Promocyjne Albatros, Szczecin 1998.
  • 14.Tabor A.: Badanie aktywności proteolitycznej obojętnej i zasadowej oraz odpowiadającej jej aktywnoœci inhibitorowej powierzchni ciała pszczoły miodnej Apis mellifera. Praca mgr, Zakład Biochemii UMCS, Lublin 2006.
  • 15.Wünschmann S., Gustchina A., Chapman M. D., Pomés A.: Cockroach alergen Bla g2: An unusual aspartic proteinases. J. Allergy Clin. Immunol. 2005, 116, 140-145.
  • 16.Yamamoto Y., Watabe S., Kageyama T., Takahashi S. Y.: A novel inhibitor protein for Bombox cysteine proteinase is homologus to propeptide region sof cysteine proteinases. Fed. Eur. Bioch. Soc. J. 1999, 448, 257-260

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-article-76ba2816-aa16-46b0-9f26-30e1240dacd9
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