Published March 28, 2024
| Version v1
Journal article
In Drosophila Hemolymph, Serine Proteases Are the Major Gelatinases and Caseinases
Contributors
Others:
- Institut Sophia Agrobiotech (ISA) ; Université Nice Sophia Antipolis (1965 - 2019) (UNS)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement (INRAE)-Université Côte d'Azur (UniCA)
- Plateforme Protéomique [Marseille] ; Institut de Microbiologie de la Méditerranée (IMM) ; Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)
- Department of Plant Health and Environment (SPE) INRAE
- ANR-11-LABX-0028,SIGNALIFE,Réseau d'Innovation sur les Voies de Signalisation en Sciences de la Vie(2011)
- ANR-15-IDEX-0001,UCA JEDI,Idex UCA JEDI(2015)
Description
Insect hemolymph transports, exchanges, and eliminates soluble compounds from the hemocoel. These processes play a critical role in many physiological processes, including development and immunity. Since matrix metalloproteases (MMPs) are the major circulating gelatinases in the blood of various species, including mammals, we used gel zymography to analyze gelatinase and caseinase activities in Drosophila larval hemolymph under normal and pathological conditions. Our investigations demonstrate that the major gelatinases and caseinases in Drosophila larval hemolymph are not MMPs but serine proteases (SPs). We identified more than 60 SPs in these proteolytic active bands. While a role in immunity has been suggested for some of these circulating SPs, the physiological functions of most of them remain to be elucidated.
Abstract
International audienceAdditional details
Identifiers
- URL
- https://hal.inrae.fr/hal-04524350
- URN
- urn:oai:HAL:hal-04524350v1
Origin repository
- Origin repository
- UNICA