Anti-prion activity found in beetle grub hemolymph of Trypoxylus dichotomus septentrionalis
| Autor: | Taichi Hamanaka, Hiroshi Kurahashi, Katsumi Doh-ura, Ayumi Oguma, Keiko Nishizawa, Kenta Teruya, Yuji Sakasegawa |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
Autophagosome
animal structures animal diseases medicine.medical_treatment Biophysics Biochemistry symbols.namesake Aminoguanidine Hemolymph medicine Bovine serum albumin PrPc normal cellular PrP Lipid raft Insect hemolymph chemistry.chemical_classification PrP prion protein Protease biology Molecular mass nervous system diseases Amino acid PrPres protease-resistant abnormal PrP AGE advanced glycation end product Maillard reaction chemistry Prion symbols biology.protein Advanced glycation end product Strain dependency Research Article Maillard reaction product |
| Zdroj: | Biochemistry and Biophysics Reports |
| ISSN: | 2405-5808 |
| DOI: | 10.1016/j.bbrep.2015.07.009 |
| Popis: | No remedies for prion disease have been established, and the conversion of normal to abnormal prion protein, a key event in prion disease, is still unclear. Here we found that substances in beetle grub hemolymph, after they were browned by aging for a month or heating for hours, reduced abnormal prion protein (PrP) levels in RML prion-infected cells. Active anti-prion components in the hemolymph were resistant to protease treatment and had molecular weights larger than 100 kDa. Aminoguanidine treatment of the hemolymph abolished its anti-prion activity, suggesting that Maillard reaction products are enrolled in the activity against the RML prion. However, levels of abnormal PrP in RML prion-infected cells were not decreased by incubation with the Maillard reaction products formed by amino acids or bovine serum albumin. The anti-prion components in the hemolymph modified neither cellular or cell-surface PrP levels nor lipid raft or autophagosome levels. The anti-prion activity was not observed in cells infected with 22 L prion or Fukuoka-1 prion, suggesting the anti-prion action is prion strain-dependent. Although the active components of the hemolymph need to be further evaluated, the present findings imply that certain specific chemical structures in the hemolymph, but not chemical structures common to all Maillard reaction products, are involved in RML prion formation or turnover, without modifying normal PrP expression. The anti-prion components in the hemolymph are a new tool for elucidating strain-dependent prion biology. Highlights • Mechanism of prion formation is still unclear in prion-infected cells. • Browned beetle-grub hemolymph has a prion strain-dependent anti-prion activity. • Anti-prion activity of the hemolymph is abolished by a Maillard reaction inhibitor. • No anti-prion activity is observed in other Maillard reaction products. • Browned hemolymph is a new tool for elucidating strain-dependent prion biology. |
| Databáze: | OpenAIRE |
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