{"title":"基质金属蛋白酶对冷藏期间鲈鱼 I 型胶原降解和肌肉软化的协同作用","authors":"Ru-Qing Yang, Yu-Lei Chen, Duanquan Lin, Kai-Yuan Cao, Le-Chang Sun, Ling-Jing Zhang, Asami Yoshida, Min-Jie Cao","doi":"10.1021/acs.jafc.4c04461","DOIUrl":null,"url":null,"abstract":"Matrix metalloproteinases (MMPs) play critical roles in the degradation of collagens, while their mechanism remains unclear. In the present study, the involvement of matrix metalloproteinases (MMPs) in collagen degradation of sea bass muscle during cold storage was explored. Immunohistochemical staining results showed significant degradation of type I collagen in the connective tissue of muscle endomysium during cold storage, thus affecting the muscle structural integrity and quality. Western blot analysis revealed an increment in the α1 chain and a decrease in the β and γ chains of type I collagen. Immunofluorescence staining showed that MMP-2, MMP-9, and MMP-13 were distributed in the endomysium surrounding the muscle fibers. Additionally, the catalytic domains of MMP-2, MMP-9, and MMP-13 with biological activities were successfully expressed. The degradation trend of type I collagen by MMPs under 4 °C was similar to that of muscle collagen during cold storage, suggesting that the degradation of type I collagen was attributed to the cooperative action of the MMPs. In conclusion, our study elucidated that the MMPs-engaged degradation of type I collagen is quite possibly the leading cause of sea bass muscle softening during cold storage.","PeriodicalId":41,"journal":{"name":"Journal of Agricultural and Food Chemistry","volume":null,"pages":null},"PeriodicalIF":5.7000,"publicationDate":"2024-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Collaborative Effect of Matrix Metalloproteinases on Type I Collagen Degradation and Muscle Softening in Sea Bass (Lateolabrax japonicus) during Cold Storage\",\"authors\":\"Ru-Qing Yang, Yu-Lei Chen, Duanquan Lin, Kai-Yuan Cao, Le-Chang Sun, Ling-Jing Zhang, Asami Yoshida, Min-Jie Cao\",\"doi\":\"10.1021/acs.jafc.4c04461\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Matrix metalloproteinases (MMPs) play critical roles in the degradation of collagens, while their mechanism remains unclear. In the present study, the involvement of matrix metalloproteinases (MMPs) in collagen degradation of sea bass muscle during cold storage was explored. Immunohistochemical staining results showed significant degradation of type I collagen in the connective tissue of muscle endomysium during cold storage, thus affecting the muscle structural integrity and quality. Western blot analysis revealed an increment in the α1 chain and a decrease in the β and γ chains of type I collagen. Immunofluorescence staining showed that MMP-2, MMP-9, and MMP-13 were distributed in the endomysium surrounding the muscle fibers. Additionally, the catalytic domains of MMP-2, MMP-9, and MMP-13 with biological activities were successfully expressed. The degradation trend of type I collagen by MMPs under 4 °C was similar to that of muscle collagen during cold storage, suggesting that the degradation of type I collagen was attributed to the cooperative action of the MMPs. In conclusion, our study elucidated that the MMPs-engaged degradation of type I collagen is quite possibly the leading cause of sea bass muscle softening during cold storage.\",\"PeriodicalId\":41,\"journal\":{\"name\":\"Journal of Agricultural and Food Chemistry\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":5.7000,\"publicationDate\":\"2024-10-05\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Agricultural and Food Chemistry\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://doi.org/10.1021/acs.jafc.4c04461\",\"RegionNum\":1,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"AGRICULTURE, MULTIDISCIPLINARY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Agricultural and Food Chemistry","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.1021/acs.jafc.4c04461","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"AGRICULTURE, MULTIDISCIPLINARY","Score":null,"Total":0}
引用次数: 0
摘要
基质金属蛋白酶(MMPs)在胶原降解过程中起着关键作用,但其作用机制仍不清楚。本研究探讨了基质金属蛋白酶(MMPs)在海鲈肌肉冷藏期间参与胶原降解的情况。免疫组化染色结果显示,冷藏期间肌肉内膜结缔组织中的 I 型胶原蛋白发生了显著降解,从而影响了肌肉结构的完整性和质量。Western 印迹分析显示 I 型胶原蛋白的 α1 链增加,β 和 γ 链减少。免疫荧光染色显示,MMP-2、MMP-9 和 MMP-13 分布在肌纤维周围的内膜中。此外,具有生物活性的 MMP-2、MMP-9 和 MMP-13 的催化结构域也被成功表达。I 型胶原蛋白在 4 °C 下被 MMPs 降解的趋势与肌肉胶原蛋白在冷藏过程中的降解趋势相似,这表明 I 型胶原蛋白的降解归因于 MMPs 的协同作用。总之,我们的研究阐明了 MMPs 引起的 I 型胶原蛋白降解可能是海鲈肌肉在冷藏期间变软的主要原因。
Collaborative Effect of Matrix Metalloproteinases on Type I Collagen Degradation and Muscle Softening in Sea Bass (Lateolabrax japonicus) during Cold Storage
Matrix metalloproteinases (MMPs) play critical roles in the degradation of collagens, while their mechanism remains unclear. In the present study, the involvement of matrix metalloproteinases (MMPs) in collagen degradation of sea bass muscle during cold storage was explored. Immunohistochemical staining results showed significant degradation of type I collagen in the connective tissue of muscle endomysium during cold storage, thus affecting the muscle structural integrity and quality. Western blot analysis revealed an increment in the α1 chain and a decrease in the β and γ chains of type I collagen. Immunofluorescence staining showed that MMP-2, MMP-9, and MMP-13 were distributed in the endomysium surrounding the muscle fibers. Additionally, the catalytic domains of MMP-2, MMP-9, and MMP-13 with biological activities were successfully expressed. The degradation trend of type I collagen by MMPs under 4 °C was similar to that of muscle collagen during cold storage, suggesting that the degradation of type I collagen was attributed to the cooperative action of the MMPs. In conclusion, our study elucidated that the MMPs-engaged degradation of type I collagen is quite possibly the leading cause of sea bass muscle softening during cold storage.
期刊介绍:
The Journal of Agricultural and Food Chemistry publishes high-quality, cutting edge original research representing complete studies and research advances dealing with the chemistry and biochemistry of agriculture and food. The Journal also encourages papers with chemistry and/or biochemistry as a major component combined with biological/sensory/nutritional/toxicological evaluation related to agriculture and/or food.