{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T20:12:04Z","timestamp":1790021524973,"version":"4.0.1"},"reference-count":43,"publisher":"MDPI AG","issue":"5","license":[{"start":{"date-parts":[[2022,4,29]],"date-time":"2022-04-29T00:00:00Z","timestamp":1651190400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"NICHD","award":["#R01HD088549"],"award-info":[{"award-number":["#R01HD088549"]}]},{"name":"Indian Council of Agricultural Research","award":["#R01HD088549"],"award-info":[{"award-number":["#R01HD088549"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Genes"],"abstract":"<jats:p>Although metabolic acidosis is associated with numerous pathophysiological conditions and its vasorelaxation effects have been well described in different animal and culture models, the molecular mechanisms of acidosis-induced vasorelaxation are not fully understood. Mesenteric artery models have been used extensively to examine the vascular response to various pathophysiological conditions. Our previous studies and several other reports have suggested the vascular responses of goat mesenteric arteries and human arteries to various stimuli, including acidic stress, are highly similar. In this study, to further identify the signaling molecules responsible for altered vasoreactivity in response to acidic pH, we examined the proteomic profile of acid stress-induced vasorelaxation using a goat mesenteric artery model. The vascular proteomes under acidic pH were compared using 2D-GE with 7 cm IPG strips and mini gels, LC-MS\/MS, and MALDI TOF MS. The unique proteins identified by mass spectroscopy were actin, transgelin, WD repeat-containing protein 1, desmin, tropomyosin, ATP synthase \u03b2, Hsp27, aldehyde dehydrogenase, pyruvate kinase, and vitamin K epoxide reductase complex subunit 1-like protein. Out of five protein spots identified as actin, three were upregulated &gt; 2-fold. ATP synthase \u03b2 was also upregulated (2.14-fold) under acid stress. Other actin-associated proteins upregulated were transgelin, desmin, and WD repeat-containing protein 1. Isometric contraction studies revealed that both receptor-mediated (histamine) and non-receptor-mediated (KCl) vasocontraction were attenuated, whereas acetylcholine-induced vasorelaxation was augmented under acidosis. Overall, the altered vasoreactivity under acidosis observed in the functional studies could possibly be attributed to the increase in expression of actin and ATP synthase \u03b2.<\/jats:p>","DOI":"10.3390\/genes13050801","type":"journal-article","created":{"date-parts":[[2022,4,29]],"date-time":"2022-04-29T16:49:57Z","timestamp":1651250997000},"page":"801","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Proteomic Profiling and Pathway Analysis of Acid Stress-Induced Vasorelaxation of Mesenteric Arteries In Vitro"],"prefix":"10.3390","volume":"13","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0894-4770","authenticated-orcid":false,"given":"Ipsita","family":"Mohanty","sequence":"first","affiliation":[{"name":"ICAR-Central Inland Fisheries Research Institute, Biochemistry Laboratory, Proteomics Unit, Barrackpore, Kolkata 700120, India"},{"name":"Department of Pharmacology and Toxicology, College of Veterinary Sciences and Animal Husbandry, Orissa University of Agriculture and Technology, Bhubaneswar 751003, India"},{"name":"Departments of Pediatrics, Children\u2019s Hospital of Philadelphia Research Institute, The Raymond and Ruth Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sudeshna","family":"Banerjee","sequence":"additional","affiliation":[{"name":"ICAR-Central Inland Fisheries Research Institute, Biochemistry Laboratory, Proteomics Unit, Barrackpore, Kolkata 700120, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arabinda","family":"Mahanty","sequence":"additional","affiliation":[{"name":"ICAR-Central Inland Fisheries Research Institute, Biochemistry Laboratory, Proteomics Unit, Barrackpore, Kolkata 700120, India"},{"name":"ICAR-National Rice Research Institute, Cuttack 753006, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1378-3775","authenticated-orcid":false,"given":"Sasmita","family":"Mohanty","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, Faculty of Science & Technology, Rama Devi Women\u2019s University, Bhubaneswar 751022, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nihar Ranjan","family":"Nayak","sequence":"additional","affiliation":[{"name":"Department of Obstetrics and Gynecology, UMKC School of Medicine, Kansas City, MO 64108, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6421-4006","authenticated-orcid":false,"given":"Subas Chandra","family":"Parija","sequence":"additional","affiliation":[{"name":"Department of Pharmacology and Toxicology, College of Veterinary Sciences and Animal Husbandry, Orissa University of Agriculture and Technology, Bhubaneswar 751003, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9749-9466","authenticated-orcid":false,"given":"Bimal Prasanna","family":"Mohanty","sequence":"additional","affiliation":[{"name":"ICAR-Central Inland Fisheries Research Institute, Biochemistry Laboratory, Proteomics Unit, Barrackpore, Kolkata 700120, India"},{"name":"Indian Council of Agricultural Research (ICAR), ICAR-Fisheries Science Division, Room No. 308, Krishi Anusandhan Bhawan II, New Delhi 110012, India"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,4,29]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"F628","DOI":"10.1152\/ajprenal.00210.2013","article-title":"Proteomic profiling and pathway analysis of the response of rat renal proximal convoluted tubules to metabolic acidosis","volume":"305","author":"Schauer","year":"2013","journal-title":"Am. 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