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• W2022398116 endingPage "13811" @default.
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• W2022398116 abstract "Cysteine cathepsins are primarily lysosomal proteases involved in general protein turnover, but they also have specific proteolytic functions in antigen presentation and bone remodeling. Cathepsins are most stable at acidic pH, although growing evidence indicates that they have physiologically relevant activity also at neutral pH. Post-translational proteolytic processing of mature chemokines is a key, yet underappreciated, level of chemokine regulation. Although the role of selected serine proteases and matrix metalloproteases in chemokine processing has long been known, little has been reported about the role of cysteine cathepsins. Here we evaluated cleavage of CXC ELR (CXCL1, -2, -3, -5, and -8) and non-ELR (CXCL9–12) chemokines by cysteine cathepsins B, K, L, and S at neutral pH by high resolution Tris-Tricine SDS-PAGE and matrix-assisted laser desorption ionization time-of-flight mass spectrometry. Whereas cathepsin B cleaved chemokines especially in the C-terminal region, cathepsins K, L, and S cleaved chemokines at the N terminus with glycosaminoglycans modulating cathepsin processing of chemokines. The functional consequences of the cleavages were determined by Ca2+ mobilization and chemotaxis assays. We show that cysteine cathepsins inactivate and in some cases degrade non-ELR CXC chemokines CXCL9–12. In contrast, cathepsins specifically process ELR CXC chemokines CXCL1, -2, -3, -5, and -8 N-terminally to the ELR motif, thereby generating agonist forms. This study suggests that cysteine cathepsins regulate chemokine activity and thereby leukocyte recruitment during protective or pathological inflammation.Background: Chemokine function is regulated by proteolytic processing.Results: Cysteine cathepsins activate signaling by ELR CXC chemokines and terminate signaling by non-ELR chemokines.Conclusion: Cysteine cathepsins process CXC chemokines and promote inflammation by recruitment of CXCR2-expressing cells.Significance: This is the first comprehensive study on the processing of CXC chemokines by cysteine cathepsins. Cysteine cathepsins are primarily lysosomal proteases involved in general protein turnover, but they also have specific proteolytic functions in antigen presentation and bone remodeling. Cathepsins are most stable at acidic pH, although growing evidence indicates that they have physiologically relevant activity also at neutral pH. Post-translational proteolytic processing of mature chemokines is a key, yet underappreciated, level of chemokine regulation. Although the role of selected serine proteases and matrix metalloproteases in chemokine processing has long been known, little has been reported about the role of cysteine cathepsins. Here we evaluated cleavage of CXC ELR (CXCL1, -2, -3, -5, and -8) and non-ELR (CXCL9–12) chemokines by cysteine cathepsins B, K, L, and S at neutral pH by high resolution Tris-Tricine SDS-PAGE and matrix-assisted laser desorption ionization time-of-flight mass spectrometry. Whereas cathepsin B cleaved chemokines especially in the C-terminal region, cathepsins K, L, and S cleaved chemokines at the N terminus with glycosaminoglycans modulating cathepsin processing of chemokines. The functional consequences of the cleavages were determined by Ca2+ mobilization and chemotaxis assays. We show that cysteine cathepsins inactivate and in some cases degrade non-ELR CXC chemokines CXCL9–12. In contrast, cathepsins specifically process ELR CXC chemokines CXCL1, -2, -3, -5, and -8 N-terminally to the ELR motif, thereby generating agonist forms. This study suggests that cysteine cathepsins regulate chemokine activity and thereby leukocyte recruitment during protective or pathological inflammation. Background: Chemokine function is regulated by proteolytic processing. Results: Cysteine cathepsins activate signaling by ELR CXC chemokines and terminate signaling by non-ELR chemokines. Conclusion: Cysteine cathepsins process CXC chemokines and promote inflammation by recruitment of CXCR2-expressing cells. Significance: This is the first comprehensive study on the processing of CXC chemokines by cysteine cathepsins." @default.
• W2022398116 created "2016-06-24" @default.
• W2022398116 creator A5019184331 @default.
• W2022398116 creator A5053252393 @default.
• W2022398116 creator A5056440307 @default.
• W2022398116 creator A5066775150 @default.
• W2022398116 date "2015-05-01" @default.
• W2022398116 modified "2023-10-14" @default.
• W2022398116 title "Cysteine Cathepsins Activate ELR Chemokines and Inactivate Non-ELR Chemokines" @default.
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• W2022398116 doi "https://doi.org/10.1074/jbc.m115.638395" @default.
• W2022398116 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4447957" @default.
• W2022398116 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25833952" @default.
• W2022398116 hasPublicationYear "2015" @default.
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• W2022398116 hasAuthorship W2022398116A5056440307 @default.
• W2022398116 hasAuthorship W2022398116A5066775150 @default.

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