{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T23:19:16Z","timestamp":1790637556626,"version":"4.1.0"},"reference-count":68,"publisher":"MDPI AG","issue":"12","license":[{"start":{"date-parts":[[2022,12,12]],"date-time":"2022-12-12T00:00:00Z","timestamp":1670803200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["CIMB"],"abstract":"<jats:p>The prokineticin family comprises a group of secreted peptides that can be classified as chemokines based on their structural features and chemotactic and immunomodulatory functions. Prokineticins (PKs) bind with high affinity to two G protein-coupled receptors (GPCRs). Prokineticin receptor 1 (PKR1) and prokineticin receptor 2 (PKR2) are involved in a variety of physiological functions such as angiogenesis and neurogenesis, hematopoiesis, the control of hypothalamic hormone secretion, the regulation of circadian rhythm and the modulation of complex behaviors such as feeding and drinking. Dysregulation of the system leads to an inflammatory process that is the substrate for many pathological conditions such as cancer, pain, neuroinflammation and neurodegenerative diseases such as Alzheimer\u2019s and Parkinson\u2019s disease. The use of PKR\u2019s antagonists reduces PK2\/PKRs upregulation triggered by various inflammatory processes, suggesting that a pharmacological blockade of PKRs may be a successful strategy to treat inflammatory\/neuroinflammatory diseases, at least in rodents. Under certain circumstances, the PK system exhibits protective\/neuroprotective effects, so PKR agonists have also been developed to modulate the prokineticin system.<\/jats:p>","DOI":"10.3390\/cimb44120431","type":"journal-article","created":{"date-parts":[[2022,12,13]],"date-time":"2022-12-13T04:00:11Z","timestamp":1670904011000},"page":"6323-6332","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":17,"title":["Non-Peptide Agonists and Antagonists of the Prokineticin Receptors"],"prefix":"10.3390","volume":"44","author":[{"given":"Roberta","family":"Lattanzi","sequence":"first","affiliation":[{"name":"Department of Physiology and Pharmacology \u201cVittorio Erspamer\u201d, Sapienza University of Rome, Piazzale Aldo Moro 5, I-00185 Rome, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rossella","family":"Miele","sequence":"additional","affiliation":[{"name":"Department of Biochemical Sciences \u201cA. Rossi Fanelli\u201d, CNR-Institute of Molecular Biology and Pathology, Sapienza University of Rome, Piazzale Aldo Moro 5, I-00185 Rome, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,12,12]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/S0014-2999(99)00229-0","article-title":"Bv8, a small protein from frog skin and its homologue from snake venom induce hyperalgesia in rats","volume":"374","author":"Mollay","year":"1999","journal-title":"Eur. J. 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