{"title":"晚期糖基化终产物改变了腹膜内胶原的结构完整性,增加了通透性并改变了其生物相容性。","authors":"Makoto Fukuda, Yusuke Chiwata, Takayuki Narita, Maki Yoshihara, Hiroyuki Morimoto, Ayako Takamori, Shota Shibuki, Rinko Hinami, Ayano Ishibashi, Akinori Nagashima, Motoaki Miyazono, Shigehisa Aoki","doi":"10.1007/s13577-025-01229-4","DOIUrl":null,"url":null,"abstract":"<p><p>In patients undergoing long-term peritoneal dialysis, the peritoneal accumulation of advanced glycation end-products (AGEs) due to the Maillard reaction has long been acknowledged as problematic, although the underlying mechanisms remain insufficiently understood. Recognizing collagen as both a principal substrate for AGEs deposition and a vital cellular scaffold, we developed an innovative procedure that induces the Maillard reaction in collagen at near-physiological temperatures, enabling systematic evaluations of its structural and functional modifications. Our findings reveal that Maillard reaction-treated collagen exhibits markedly increased permeability to small- and medium-sized molecules. Furthermore, this denatured collagen diminishes the proliferative capacity of adherent mesothelial cells, implicating glycation-induced alterations in collagen in the progressive deterioration of peritoneal membrane function during extended dialysis. By illuminating previously uncharacterized morphological and functional shifts in collagen triggered by the Maillard reaction, our model provides critical insights that will enhance the safety of peritoneal dialysis and inform the development of novel therapeutic strategies.</p>","PeriodicalId":49194,"journal":{"name":"Human Cell","volume":"38 4","pages":"99"},"PeriodicalIF":3.4000,"publicationDate":"2025-05-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Advanced glycation end products alter the structural integrity, increase the permeability and transform the biocompatibility of collagen within the peritoneal membrane.\",\"authors\":\"Makoto Fukuda, Yusuke Chiwata, Takayuki Narita, Maki Yoshihara, Hiroyuki Morimoto, Ayako Takamori, Shota Shibuki, Rinko Hinami, Ayano Ishibashi, Akinori Nagashima, Motoaki Miyazono, Shigehisa Aoki\",\"doi\":\"10.1007/s13577-025-01229-4\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>In patients undergoing long-term peritoneal dialysis, the peritoneal accumulation of advanced glycation end-products (AGEs) due to the Maillard reaction has long been acknowledged as problematic, although the underlying mechanisms remain insufficiently understood. Recognizing collagen as both a principal substrate for AGEs deposition and a vital cellular scaffold, we developed an innovative procedure that induces the Maillard reaction in collagen at near-physiological temperatures, enabling systematic evaluations of its structural and functional modifications. Our findings reveal that Maillard reaction-treated collagen exhibits markedly increased permeability to small- and medium-sized molecules. Furthermore, this denatured collagen diminishes the proliferative capacity of adherent mesothelial cells, implicating glycation-induced alterations in collagen in the progressive deterioration of peritoneal membrane function during extended dialysis. By illuminating previously uncharacterized morphological and functional shifts in collagen triggered by the Maillard reaction, our model provides critical insights that will enhance the safety of peritoneal dialysis and inform the development of novel therapeutic strategies.</p>\",\"PeriodicalId\":49194,\"journal\":{\"name\":\"Human Cell\",\"volume\":\"38 4\",\"pages\":\"99\"},\"PeriodicalIF\":3.4000,\"publicationDate\":\"2025-05-12\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Human Cell\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1007/s13577-025-01229-4\",\"RegionNum\":3,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"CELL BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Human Cell","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1007/s13577-025-01229-4","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"CELL BIOLOGY","Score":null,"Total":0}
Advanced glycation end products alter the structural integrity, increase the permeability and transform the biocompatibility of collagen within the peritoneal membrane.
In patients undergoing long-term peritoneal dialysis, the peritoneal accumulation of advanced glycation end-products (AGEs) due to the Maillard reaction has long been acknowledged as problematic, although the underlying mechanisms remain insufficiently understood. Recognizing collagen as both a principal substrate for AGEs deposition and a vital cellular scaffold, we developed an innovative procedure that induces the Maillard reaction in collagen at near-physiological temperatures, enabling systematic evaluations of its structural and functional modifications. Our findings reveal that Maillard reaction-treated collagen exhibits markedly increased permeability to small- and medium-sized molecules. Furthermore, this denatured collagen diminishes the proliferative capacity of adherent mesothelial cells, implicating glycation-induced alterations in collagen in the progressive deterioration of peritoneal membrane function during extended dialysis. By illuminating previously uncharacterized morphological and functional shifts in collagen triggered by the Maillard reaction, our model provides critical insights that will enhance the safety of peritoneal dialysis and inform the development of novel therapeutic strategies.
期刊介绍:
Human Cell is the official English-language journal of the Japan Human Cell Society. The journal serves as a forum for international research on all aspects of the human cell, encompassing not only cell biology but also pathology, cytology, and oncology, including clinical oncology. Embryonic stem cells derived from animals, regenerative medicine using animal cells, and experimental animal models with implications for human diseases are covered as well.
Submissions in any of the following categories will be considered: Research Articles, Cell Lines, Rapid Communications, Reviews, and Letters to the Editor. A brief clinical case report focusing on cellular responses to pathological insults in human studies may also be submitted as a Letter to the Editor in a concise and short format.
Not only basic scientists but also gynecologists, oncologists, and other clinical scientists are welcome to submit work expressing new ideas or research using human cells.