Detailed Information on Publication Record
2024
APOLIPOPHORINS IN HONEY BEE BIOLOGY
MARCINIAK, Jacek, Jana HURYCHOVÁ, Sara ŠREIBR, Pavel HYRŠL, James B. BURRITT et. al.Basic information
Original name
APOLIPOPHORINS IN HONEY BEE BIOLOGY
Name in Czech
APOLIPOPHORINS IN HONEY BEE BIOLOGY
Authors
MARCINIAK, Jacek (203 Czech Republic, guarantor, belonging to the institution), Jana HURYCHOVÁ (203 Czech Republic, belonging to the institution), Sara ŠREIBR (276 Germany, belonging to the institution), Pavel HYRŠL (203 Czech Republic, belonging to the institution), James B. BURRITT and Pavel DOBEŠ (203 Czech Republic, belonging to the institution)
Edition
BeeConnected 2024, 2024
Other information
Language
English
Type of outcome
Prezentace na konferencích
Field of Study
10616 Entomology
Country of publisher
Czech Republic
Confidentiality degree
není předmětem státního či obchodního tajemství
Organization unit
Faculty of Science
ISBN
978-80-8077-819-4
Keywords (in Czech)
Apis mellifera; včela medonosná; apolipoforiny; metabolismus tuků
Keywords in English
Apis mellifera; honey bee; apolipophorins; lipid metabolism
Tags
International impact
Změněno: 9/4/2024 13:50, Mgr. Jacek Marciniak
V originále
Apolipophorins are a group of insect proteins belonging to the large lipid transfer protein (LLTP) superfamily. They participate in the transport of lipids, carbohydrates, and other hydrophobic compounds through the formation of lipophorin particles. Lipophorins are assembled in the fat body and after their release to the hemolymph operate as reusable lipid shuttles between the fat body and target tissues such as flight muscles or epidermis1. Three distinct apolipophorins are predicted in honey bees, apoLp-I-III. In our research, we focus on the apoLp-I and its precursor the apoLp-II/I. The role of this protein in honey bee biology has so far not been investigated thoroughly, except for its function in lipid transport. However, we believe that it is worth investigating also in other contexts such as immune response or physiological adaptation to seasons. This is based on the fact, that the apoLp-I shares multiple functional domains with another member of the LLTP superfamily, the vitellogenin, which is supposed to have a plethora of biological functions such as protection from oxidative stress2, regulation of social behavior3, and transfer of immune elicitors4, to name a few. We expect that the apoLp-I may share some of these properties and our preliminary results support this expectation. As an example, we have observed seasonal variation in the apoLp-I level, which has a similar expression pattern when compared to vitellogenin. We aim to further investigate this protein utilizing our in-house monoclonal antibodies, mass spectrometry-based techniques, and RNAi-based functional assays.
In Czech
Apolipophorins are a group of insect proteins belonging to the large lipid transfer protein (LLTP) superfamily. They participate in the transport of lipids, carbohydrates, and other hydrophobic compounds through the formation of lipophorin particles. Lipophorins are assembled in the fat body and after their release to the hemolymph operate as reusable lipid shuttles between the fat body and target tissues such as flight muscles or epidermis1. Three distinct apolipophorins are predicted in honey bees, apoLp-I-III. In our research, we focus on the apoLp-I and its precursor the apoLp-II/I. The role of this protein in honey bee biology has so far not been investigated thoroughly, except for its function in lipid transport. However, we believe that it is worth investigating also in other contexts such as immune response or physiological adaptation to seasons. This is based on the fact, that the apoLp-I shares multiple functional domains with another member of the LLTP superfamily, the vitellogenin, which is supposed to have a plethora of biological functions such as protection from oxidative stress2, regulation of social behavior3, and transfer of immune elicitors4, to name a few. We expect that the apoLp-I may share some of these properties and our preliminary results support this expectation. As an example, we have observed seasonal variation in the apoLp-I level, which has a similar expression pattern when compared to vitellogenin. We aim to further investigate this protein utilizing our in-house monoclonal antibodies, mass spectrometry-based techniques, and RNAi-based functional assays.
Links
| QK21010088, research and development project |
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