Lapolla A, Fedele D, Reitano R, Bonfante L, Pastori G, Seraglia R, Tubaro M, Traldi P
Cattedra di Malattie del Metabolismo, Universitá di Padova, Italy.
Ann N Y Acad Sci. 2005 Jun;1043:267-75. doi: 10.1196/annals.1333.032.
Advanced glycation end products/peptides (AGE/peptides) originate by in vivo enzymatic digestion of nonenzymatically glycated proteins, which are produced by reaction of glucose with primary amino groups present in the protein chain following the Maillard pattern. AGE/peptides are highly reactive species and can interact with tissue and circulating proteins, leading to tissue modification and impaired protein functionality. Serum levels of AGE/peptides are reported to be particularly high in diabetes (in terms of higher production) or in end-stage renal disease (in terms of accumulation). For these reasons, their structural identification is of high interest, giving information on their relationship with the pathological state and allowing the design of possible therapeutic interventions. We report here some preliminary results obtained by liquid chromatography/electrospray ionization/mass spectrometry (LC/ESI/MS) and matrix-assisted laser desorption ionization MS (MALDI-MS) investigations carried out on the low-molecular-weight serum peptide fraction from 10 healthy subjects, 10 patients with poorly controlled diabetes, and 10 patients with end-stage nephropathy.
晚期糖基化终末产物/肽（AGE/肽）源自体内对非酶糖基化蛋白质的酶促消化，这些非酶糖基化蛋白质是葡萄糖按照美拉德反应模式与蛋白质链中存在的伯氨基反应产生的。AGE/肽是高反应性物质，可与组织蛋白和循环蛋白相互作用，导致组织改变和蛋白质功能受损。据报道，糖尿病患者（从产生量较高的角度来看）或终末期肾病患者（从积累的角度来看）的血清AGE/肽水平特别高。基于这些原因，对其进行结构鉴定具有很高的价值，这有助于了解它们与病理状态的关系，并为可能的治疗干预措施提供设计依据。我们在此报告通过液相色谱/电喷雾电离/质谱（LC/ESI/MS）和基质辅助激光解吸电离质谱（MALDI-MS）对10名健康受试者、10名糖尿病控制不佳患者和10名终末期肾病患者的低分子量血清肽组分进行研究获得的一些初步结果。
