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MSP-MS of Cathepsin L and Cathepsin V pH 5.5

ABSTRACT: MSP-MS of Cathepsin L and Cathepsin V pH 5.5 at 37C

INSTRUMENT(S): Q Exactive

ORGANISM(S): Synthetic Construct (ncbitaxon:32630)

SUBMITTER: Vivian Hook Anthony ODonoghue

PROVIDER: MSV000088091 | MassIVE |

SECONDARY ACCESSION(S): PXD028454

REPOSITORIES: MassIVE

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Publications

Distinct Dibasic Cleavage Specificities of Neuropeptide-Producing Cathepsin L and Cathepsin V Cysteine Proteases Compared to PC1/3 and PC2 Serine Proteases.

Yoon Michael C MC Ames Janneca J Mosier Charles C Jiang Zhenze Z Podvin Sonia S O'Donoghue Anthony J AJ Hook Vivian V

ACS chemical neuroscience 20220105 2

Neuropeptides, functioning as peptide neurotransmitters and hormones, are generated from proneuropeptide precursors by proteolytic processing at dibasic residue sites (i.e., KR, RK, KK, RR). The cysteine proteases cathepsin L and cathepsin V, combined with the serine proteases proprotein convertases 1 and 2 (PC1/3 and PC2), participate in proneuropeptide processing to generate active neuropeptides. To compare the dibasic cleavage properties of these proteases, this study conducted global, unbias ...[more]

PMID: 34986304

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