{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Gatti JL"],"funding":["Department of Plant Health and Environment (SPE) from INRAE and the French Government (National Research Agency, ANR)","Agence Nationale de la Recherche"],"pagination":["234"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11050137"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(4)"],"pubmed_abstract":["After separation on gel zymography, <i>Drosophila melanogaster</i> hemolymph displays gelatinase and caseinase bands of varying sizes, ranging from over 140 to 25 kDa. Qualitative and quantitative variations in these bands were observed during larval development and between different <i>D. melanogaster</i> strains and Drosophila species. The activities of these Drosophila hemolymph gelatinase and caseinase were strongly inhibited by serine protease inhibitors, but not by EDTA. Mass spectrometry identified over 60 serine proteases (SPs) in gel bands corresponding to the major <i>D. melanogaster</i> gelatinases and caseinases, but no matrix metalloproteinases (MMPs) were found. The most abundant proteases were tequila and members of the Jonah and trypsin families. However, the gelatinase ban"],"journal":["Insects"],"pubmed_title":["In Drosophila Hemolymph, Serine Proteases Are the Major Gelatinases and Caseinases."],"pmcid":["PMC11050137"],"funding_grant_id":["ANR-15-IDEX-01","LABEX SIGNALIFE ANR-11-LABX-0028-01","IDEX UCAJedi ANR-15-IDEX-01","ANR-11-LABX-0028-01"],"pubmed_authors":["Belghazi M","Gatti JL","Poirie M","Arthaud L","Lemauf S"],"additional_accession":[]},"is_claimable":false,"name":"In Drosophila Hemolymph, Serine Proteases Are the Major Gelatinases and Caseinases.","description":"After separation on gel zymography, <i>Drosophila melanogaster</i> hemolymph displays gelatinase and caseinase bands of varying sizes, ranging from over 140 to 25 kDa. Qualitative and quantitative variations in these bands were observed during larval development and between different <i>D. melanogaster</i> strains and Drosophila species. The activities of these Drosophila hemolymph gelatinase and caseinase were strongly inhibited by serine protease inhibitors, but not by EDTA. Mass spectrometry identified over 60 serine proteases (SPs) in gel bands corresponding to the major <i>D. melanogaster</i> gelatinases and caseinases, but no matrix metalloproteinases (MMPs) were found. The most abundant proteases were tequila and members of the Jonah and trypsin families. However, the gelatinase ban","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Mar","modification":"2026-04-13T03:24:43.569Z","creation":"2026-04-13T03:12:45.67Z"},"accession":"S-EPMC11050137","cross_references":{"pubmed":["38667364"],"doi":["10.3390/insects15040234"]}}