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ProteomicsCell surface processing of CD109 by meprin β leads to the release of soluble fragments and reduced expression on extracellular vesicles
Cluster of differentiation 109 (CD109) is a glycosylphosphatidylinositol (GPI) anchored protein expressed on primitive hematopoietic stem cells, activated platelets, CD4+ and CD8+ T-cells and keratinocytes. In recent years CD109 was also associated with different tumor entities and identified as a p...
ORGANISM(S): Mus musculus (Mouse) Homo sapiens (Human) 
2021-01-28 | PXD023727 | Pride
Cd109  macroglobulin  meprin β  exosomes  extracellular vesicles  tem  tep1r 
ProteomicsProteolytic processing of CD99
The adhesion molecule CD99 is essential for transendothelial migration (TEM) of leukocytes. Here we demonstrate by biochemical and cellular assays that CD99 undergoes ectodomain shedding by the metalloprotease meprin ? and subsequent intramembrane proteolysis by ?-secretase. The cleavage site in CD9...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080746 | MassIVE
UnknownThe metalloproteases meprin α and meprin β: unique enzymes in inflammation, neurodegeneration, cancer and fibrosis.
Not available
S-EPMC3573791 | biostudies-literature
ProteomicsTargeted approach to determine the impact of cancer-associated protease variants
Several mechanisms of cancer progression, from tumour onset to metastasis, critically involve proteolytic activity. Studying the role of proteases in cancer, it is important to consider single nucleotide variants (SNVs) affecting the active site of proteases, that might impact cleavage specificity, ...
ORGANISM(S): Homo sapiens (Human) 
2025-05-06 | PXD048501 | Pride
Snvs Meprin β Proteases Cancer Migration Spheroids Cancer-associated variants Cleavage specificity N-terminomics Organotypic brain slices 
UnknownOrigin and Diversification of Meprin Proteases.
Not available
S-EPMC4545420 | biostudies-literature
UnknownMetalloproteases meprin α and meprin β are C- and N-procollagen proteinases important for collagen assembly and tensile strength.
Not available
S-EPMC3761563 | biostudies-literature
UnknownCharacterization of the Cancer-Associated Meprin Βeta Variants G45R and G89R.
Not available
S-EPMC8526939 | biostudies-literature
UnknownDiscovery and Optimization of Selective Inhibitors of Meprin α (Part II).
Not available
S-EPMC7997411 | biostudies-literature
ProteomicsProteolytic processing of galectin-3 is crucial for host microbiome homeostasis
To identify relevant substrates for meprin α/β heterodimers, we applied mass spectrometry-based N-terminomics of mouse colon tissue as well as of human Caco-2 cells and identified galectin-3 as a novel intestinal substrate. The proteolytic processing of galectin-3 by meprin α/β heterodimers plays a ...
ORGANISM(S): Mus musculus (Mouse) 
2023-05-10 | PXD037000 | Pride
Lc-ms Meprin N-terminomics 
UnknownMeprin β Modulates Brevican Proteolysis Impairing Neural Plasticity and Memory Formation.
Not available
S-EPMC12093287 | biostudies-literature
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