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MetabolomicsLysosomal Acidity and Cathepsin L Activate Eosinophils via ARG1-Mediated Arginine Metabolism in Allergic Airway Inflammation

Eosinophils are the predominant immune cells implicated in the pathogenesis of asthma, highlighting the need for strategies to mitigate their effects. While previous studies have indicated a potential relationship between lysosomes and eosinophils, the precise role of lysosomes in eosinophil acti...

2025-09-15 | MTBLS13001 | MetaboLights
ProteomicsMSP-MS of Cathepsin L and Cathepsin V pH 5.5
MSP-MS of Cathepsin L and Cathepsin V pH 5.5 at 37C
ORGANISM(S): Synthetic Construct (ncbitaxon:32630) 
MSV000088091 | MassIVE
TranscriptomicsAdenosine-to-inosine RNA editing controls cathepsin S expression in atherosclerosis by enabling HuR-mediated post-transcriptional regulation
Adenosine-to-inosine (A-to-I) RNA editing, which is catalyzed by a family of adenosine deaminase acting on RNA (ADAR) enzymes, is important in the epitranscriptomic regulation of RNA metabolism. However, the role of A-to-I RNA editing in vascular disease is unknown. Here we show that cathepsin S mRN...
ORGANISM(S): Homo sapiens 
2016-09-05 | E-GEOD-60217 | biostudies-arrayexpress
ProteomicsCathepsin B and Cathepsin Z tumor secretome of murine breast cancers
MS-based proteomics study of the cancer secretome and tumor interstitial fluid of tumor cell/macrophage co-cultures and breast tumors in cells and mice lacking both cathepsin B and cathepsin Z
ORGANISM(S): Mus musculus (Mouse) 
2021-09-08 | PXD015209 | Pride
Tumor interstitial fluid Ccm Mouse Secretome 
ProteomicsQuantitative proteomics reveals the crucial roles of Cathepsin D in bacterial infections
Bacterial resistance has become more and more widespread which seriously threatens human life and health. Therefore, using the natural immune system of host to kill bacteria is particularly fascinating. Here, using mass spectrometry analyses, we depicted the dynamic expression landscape of mitochond...
ORGANISM(S): Mus Musculus 
2020-05-13 | PXD016938 |
TranscriptomicsHuman cystatin D (CST5) locates in the nucleus at sites of active transcription and regulates gene expression
Cystatin D (CST5) is an inhibitor of several proteases of the cathepsin family that inhibits cell proliferation, migration and invasion of colon carcinoma cells. Some of these effects are unrelated to its antiprotease activity. Here, we use genome-wide expression microarrays to show that cystatin D ...
ORGANISM(S): Homo sapiens 
2015-11-04 | E-GEOD-45904 | biostudies-arrayexpress
ProteomicsQuantitative analysis to the subcellular proteome in response to cathepsin D knockdown in HeLa cells
Cathepsin D is reportedly to be closely associated with tumor development, migration and invasion, but its pathological mechanism is not fully elucidated. We aimed to evaluate phenotypic changes and molecular events in response to cathepsin D knockdown. Lowering endogenous cathepsin D abundance (CR)...
ORGANISM(S): Homo sapiens (Human) 
2015-12-17 | PXD002844 | Pride
Cytosol Lysosome Silac Nucleus Subcellular fractionation 
ProteomicsImpact of cathepsin A on the murine cardiac proteome
Cathepsin A (CTSA) is a lysosomal carboxypeptidase present at the cell surface and secreted outside the cell. Additionally, CTSA binds to β-galactosidase and neuraminidase 1 to protect them from degradation. CTSA has gained attention as a drug target for the treatment of cardiac hypertrophy and hear...
ORGANISM(S): Mus musculus (Mouse) 
2016-07-25 | PXD003860 | Pride
Transgenic mouse Cathepsin a Lc-ms/ms 
ProteomicsProteomic analysis of mouse liver with conditional knock-out of Cathepsin D in macrophages
The cell-specific role of lysosomal protease cathepsin D (CtsD) in liver fibrosis is not completely clear. This study reports that while CtsD is highly expressed in liver macrophages of cirrhotic patients, CtsD deletion in macrophages resulted in enhanced liver fibrosis. For this scope, a macrophage...
ORGANISM(S): Mus musculus (Mouse) 
2024-07-25 | PXD032827 | Pride
Label-free proteomics Liver fibrosis Cathepsin d S-trap 
ProteomicsA 9-kDa matricellular SPARC fragment released by cathepsin D exhibits pro-tumor activity in cancer
The remodeling of the extracellular matrix (ECM) by proteases releases fragments that promote tumor progression and metastasis. The protease cathepsin D (cath-D), a marker of poor prognosis in triple-negative breast cancer (TNBC), is aberrantly secreted in the ECM. Using degradomics, we discovered t...
ORGANISM(S): Homo sapiens (Human) 
2021-09-09 | PXD022826 | Pride
Ecm Tnbc Protease Proteolysis Matricellular protein Tumor microenvironment 
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