{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,17]],"date-time":"2026-10-17T11:39:25Z","timestamp":1792237165390,"version":"4.4.0"},"reference-count":27,"publisher":"MDPI AG","issue":"2","license":[{"start":{"date-parts":[[2012,2,15]],"date-time":"2012-02-15T00:00:00Z","timestamp":1329264000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/3.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Marine Drugs"],"abstract":"<jats:p>Antihypertensive effect of long-term oral administration of jellyfish (Rhopilema esculentum) collagen peptides (JCP) on renovascular hypertension rats (RVHs) was evaluated. The systolic blood pressure and diastolic blood pressure of the RVHs were significantly reduced with administration of JCP (p &lt; 0.05), compared with model control group. However, the arterial blood pressure of normal rats showed no significant changes during long-term oral treatment with high dose JCP (p &gt; 0.05). Furthermore, effect of JCP on angiotensin II (Ang II) concentration of plasma had no significance (p &gt; 0.05), but JCP significantly inhibited the Ang II concentration in RVHs\u2019 kidney (p &lt; 0.05). The kidney should be the target site of JCP.<\/jats:p>","DOI":"10.3390\/md10020417","type":"journal-article","created":{"date-parts":[[2012,2,15]],"date-time":"2012-02-15T12:03:12Z","timestamp":1329307392000},"page":"417-426","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":74,"title":["Antihypertensive Effect of Long-Term Oral Administration of Jellyfish (Rhopilema esculentum) Collagen Peptides on Renovascular Hypertension"],"prefix":"10.3390","volume":"10","author":[{"given":"Yongliang","family":"Zhuang","sequence":"first","affiliation":[{"name":"Research Center of Food Engineering, College of Chemistry and Engineering, Kunming University of Science and Technology, Kunming, Yunnan 650600, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Liping","family":"Sun","sequence":"additional","affiliation":[{"name":"Research Center of Food Engineering, College of Chemistry and Engineering, Kunming University of Science and Technology, Kunming, Yunnan 650600, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9409-468X","authenticated-orcid":false,"given":"Yufeng","family":"Zhang","sequence":"additional","affiliation":[{"name":"Research Center of Food Engineering, College of Chemistry and Engineering, Kunming University of Science and Technology, Kunming, Yunnan 650600, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gaoxiang","family":"Liu","sequence":"additional","affiliation":[{"name":"Research Center of Food Engineering, College of Chemistry and Engineering, Kunming University of Science and Technology, Kunming, Yunnan 650600, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2012,2,15]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Zhuang, Y., Sun, L., and Li, B. (2010). Production of the angiotensin-I-converting enzyme (ACE)-inhibitory peptide from hydrolysates of jellyfish (Rhopilema esculentum) collagen. Food Bioprocess Technol.","DOI":"10.1007\/s11947-010-0439-9"},{"key":"ref_2","first-page":"980","article-title":"The emerging role of dairy protein and bioactive peptides in nutrition and health","volume":"134","author":"Richard","year":"2004","journal-title":"J. Nutr."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"968","DOI":"10.1016\/j.foodchem.2011.03.127","article-title":"Antihypertensive effect of corn peptides, produced by a continuous production in enzymatic membrance reactor, in spontaneously hypertensive rats","volume":"128","author":"Huang","year":"2011","journal-title":"Food Chem."},{"key":"ref_4","first-page":"225","article-title":"Screening of biofunctional peptides from cod processing wastes","volume":"43","author":"Kim","year":"2000","journal-title":"J. Korean Soc. Agric. Chem. Biotechnol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"1028","DOI":"10.1016\/j.peptides.2009.03.002","article-title":"A novel ACE inhibitory peptide isolated from Acaudina molpadioidea hydrolysate","volume":"30","author":"Zhao","year":"2009","journal-title":"Peptides"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"2042","DOI":"10.1111\/j.1365-2621.2009.02028.x","article-title":"Angiotensin converting enzyme inhibitory activity of Acetes chinensis peptic hydrolysate and its antihypertensive effect in spontaneously hypertensive rats","volume":"44","author":"Zhang","year":"2009","journal-title":"Int. J. Food Sci. Technol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1111\/j.1365-2621.2005.01080.x","article-title":"Inhibition properties of dipeptides from salmon muscle hydrolysate on angiotensin I-converting enzyme","volume":"41","author":"Ono","year":"2006","journal-title":"Int. J. Food Sci. Technol."},{"key":"ref_8","doi-asserted-by":"crossref","unstructured":"Lin, L., Shun, L., and Li, B.F. (2011). Angiotensin-I-converting enzyme (ACE)-inhibitory and antihypertensive properties of squid skin gelatin hydrolysates. Food Chem.","DOI":"10.1016\/j.foodchem.2011.08.064"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1021\/jf051263l","article-title":"Structural requirements of angiotensin I converting enzyme inhibitory peptides: Quantitative structure-activity relationship study of di- and tripeptides","volume":"54","author":"Wu","year":"2006","journal-title":"J. Agric. Food Chem."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1021\/jf1037823","article-title":"Angiotensin I-converting enzyme inhibitory activity of gelatin hydrolysates and identification of bioactive peptides","volume":"59","author":"Herregods","year":"2011","journal-title":"J. Agric. Food Chem."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1016\/j.foodchem.2009.04.086","article-title":"A novel angiotensin I converting enzyme inhibitory peptide from tuna frame protein hydrolysate and its antihypertensive effect in spontaneously hypertensive rats","volume":"118","author":"Lee","year":"2010","journal-title":"Food Chem."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"117","DOI":"10.3945\/jn.109.116228","article-title":"Current in vitro testing of bioactive peptides is not valuable","volume":"140","author":"Foltz","year":"2010","journal-title":"J. Nutr."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1316","DOI":"10.3168\/jds.S0022-0302(96)76487-1","article-title":"Identification of an antihypertensive peptide from casein hydrolysate produced by a proteinase from Lactobacillus helveticus CP790","volume":"79","author":"Maeno","year":"1996","journal-title":"J. Dairy Sci."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1146\/annurev.bi.51.070182.001435","article-title":"Enzymes of the rennin angiotensin system and their inhibitors","volume":"51","author":"Ondetti","year":"1982","journal-title":"Ann. Rev. Biochem."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"1411","DOI":"10.1161\/01.CIR.97.14.1411","article-title":"Angiotensin-converting enzyme inhibitors","volume":"97","author":"Brown","year":"1998","journal-title":"Circulation"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"564","DOI":"10.1111\/j.1365-2621.2000.tb16049.x","article-title":"Classification and antihypertensive activity of angiotensin I-converting enzyme inhibitory peptides derived from food proteins","volume":"65","author":"Fujita","year":"2000","journal-title":"J. Food Sci."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"5207","DOI":"10.1021\/jf050337q","article-title":"ACE inhibitory activity in enzymatic hydrolysates of insect protein","volume":"53","author":"Vercruysse","year":"2005","journal-title":"J. Agric Food. Chem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1016\/j.peptides.2009.05.029","article-title":"Ala-Val-Phe and Val-Phe: ACE inhibitory peptides derived from insect protein with antihypertensive activity in spontaneously hypertensive rats","volume":"31","author":"Vercruysse","year":"2010","journal-title":"Peptides"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1161\/01.RES.85.7.643","article-title":"The cardiac rennin-angiotensin system conceptual, or a regulator of cardiac function?","volume":"85","author":"Dostal","year":"1999","journal-title":"Circ. Res."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/S0165-022X(02)00006-4","article-title":"Optimisation and validation of an angiotensin-converting enzyme inhibition assay for the screening of bioactive peptides","volume":"51","author":"Vermeirssen","year":"2002","journal-title":"J. Biochem. Biophys. Meth."},{"key":"ref_21","first-page":"1062","article-title":"The antihypertensive effect of peptides: A novel alternative to drugs?","volume":"20","author":"Fang","year":"2008","journal-title":"Peptides"},{"key":"ref_22","first-page":"3063","article-title":"Antihypertensive peptides are present in aorta after oral administration of sour milk containing these peptides to spontaneously hypertensive rats","volume":"126","author":"Masuda","year":"1996","journal-title":"Nutrition"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"2196","DOI":"10.1016\/j.peptides.2008.08.011","article-title":"Pharmacokinetics of proline-rich tripeptides in the pig","volume":"29","author":"Kies","year":"2008","journal-title":"Peptides"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1097\/00005344-198501000-00007","article-title":"Persistent tissue converting enzyme inhibition following chronic treatment with Hoe498 and MK421 in spontaneously hypertensive rats","volume":"7","author":"Unger","year":"1985","journal-title":"J. Cardiovasc. Pharmacol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/j.foodchem.2008.05.041","article-title":"ACE-inhibitory and antihypertensive properties of a bovine casein hydrolysate","volume":"112","author":"Miguel","year":"2009","journal-title":"Food Chem."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1002\/psc.568","article-title":"Tissue distribution of antihypertensive dipeptide, Val-Tyr, after its single oral administration to spontaneously hypertensive rats","volume":"10","author":"Matsui","year":"2004","journal-title":"J. Peptide Sci."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/j.jss.2005.02.031","article-title":"Angiotensin converting enzyme-independent angitotensin II production by chymase is up-regulated in the ischemic kidney in renovascular hypertension","volume":"127","author":"Sadjadi","year":"2005","journal-title":"J. Surg. Res."}],"container-title":["Marine Drugs"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1660-3397\/10\/2\/417\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T21:48:54Z","timestamp":1760219334000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1660-3397\/10\/2\/417"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2012,2,15]]},"references-count":27,"journal-issue":{"issue":"2","published-online":{"date-parts":[[2012,2]]}},"alternative-id":["md10020417"],"URL":"https:\/\/doi.org\/10.3390\/md10020417","relation":{},"ISSN":["1660-3397"],"issn-type":[{"value":"1660-3397","type":"electronic"}],"subject":[],"published":{"date-parts":[[2012,2,15]]}}}