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Peptides were eluted from the beads and analyzed by nanoLC-nanoESI-TIMS-MS/MS using a Bruker timsTOF Pro."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Raw DDA-PASEF data were processed by Peaks Online 11 (Bioinformatics Solutions) using a Uniprot bovine proteome database filtered for proteins with a signal peptide."],"omics_type":["Proteomics"],"labhead":["Jonathan V. Sweedler"],"instrument_platform":[""],"submission_type":["COMPLETE"],"labhead_affiliation":["Department of Chemistry University of Illinois 71 RAL, Box 63-5 600 South Mathews Avenue Urbana, IL 61801, USA"],"species":["Bos Taurus (bovine)"],"submitter_mail":["romanova@illinois.edu"],"publication":["42089390 Berger JM, Denison JD, De Alwis AC, Sumner HP, McCarty GS, Romanova EV, Sweedler JV, Sombers LA. Profiling Endogenous Opioid Peptide Release from Adrenal Chromaffin Cells. ACS Chem Neurosci. 2026 17(10):1989-2003 10.1021/acschemneuro.6c00180"],"submitter_affiliation":["University of Illinois"],"submitter_country":["United States"],"doi":["10.6019/PXD067807"],"pubmed_abstract":["Despite longstanding recognition that the adrenal medulla is a major source of both catecholamines and opioid peptides, direct measurements of opioid peptide release kinetics─and characterization of the full complexity of the peptidergic forms released─remain under studied. Here, this gap is addressed by introducing a workflow that integrates real-time electrochemical detection of catecholamine (CA) and enkephalin (ENK) release kinetics with tandem mass spectrometry to profile opioid peptide signaling from adrenal chromaffin cells. Fast-scan cyclic voltammetry was used to quantitatively monitor the exocytotic release of ENK peptides and CA from large dense-core vesicles in single chromaffin cells. Interestingly, ENK release events were evident on two separate time scales. The first phase of release was consistent with the codetected CA signal, suggesting release from the same population of vesicles. A slower signal was also present, suggestive of a strong association with the dense-core matrix and hindered mass transport. Liquid chromatography was coupled with mass spectrometry (LC-MS) to profile the activity-dependent opioid peptide release from these cells. The MS data show that proenkephalin-derived peptides dominate the adrenal peptidome, and that extended variants of M-ENK that contain the YGGFM motif plus additional amino acids, including YGGFM-RF, YGGFM-RGL, peptide E, BAM-18 and BAM-22, are actively released in response to both chemical and electrical stimulation. Overall, the results of this study inform on the temporal complexity and chemical diversity of peptide participants in opioid signaling while highlighting a versatile and powerful workflow for further exploration of these molecules in physiological systems."],"pubmed_title":["Profiling Endogenous Opioid Peptide Release from Adrenal Chromaffin Cells."],"pubmed_authors":["Berger Jenna M JM, Denison J Dylan JD, De Alwis A Chathuri AC, Sumner Hannah P HP, McCarty Gregory S GS, Romanova Elena V EV, Sweedler Jonathan V JV, Sombers Leslie A LA"],"additional_accession":[]},"is_claimable":false,"name":"Profiling Neuropeptides in Adrenomedullary Chromaffin Cells: Insights into Regulated Release via Electrical and Chemical Stimulation","description":"Despite longstanding recognition that the adrenal medulla is a major source of catecholamines and opioid peptides, the dynamic co-release of these signaling molecules—and the full complexity of their molecular forms—remains poorly understood. This study addresses this gap by integrating real-time electrochemical detection with tandem mass spectrometry to map and quantify the neurochemical complexity of opioid peptide signaling from adrenal chromaffin cells. Using FSCV, we provide evidence for stimulus-evoked co-release of met-enkephalin and catecholamines from single chromaffin cells (and adrenal slices?). With MS, we show that proenkephalin-derived peptides dominate the adrenal peptidome and that extended enkephalin peptides—such as BAM-18 and BAM-22—are not only present in cell content but are actively 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