Das B K, Sun T X, Akhtar N J, Chylack L T, Liang J J
Center for Ophthalmic Research, Brigham and Women's Hospital, Boston, Massachusetts 02115, USA.
Invest Ophthalmol Vis Sci. 1998 Oct;39(11):2058-66.
To establish whether advanced glycation is the major mechanism for yellowing of lens proteins.
Synchronous fluorescence (SF) and immunochemical assays were used to study glycation in vitro and in vivo. In the in vitro study, advanced glycation end products (AGEs) were prepared and used as antigens to induce antibodies to AGEs. The in vitro AGEs and classified nuclear cataracts were analyzed by SF and immunochemical assays.
In vitro AGEs generated from various glycating agents and carrier proteins displayed strong SF above 350 nm; the spectra were well resolved with major bands at 380 nm and 420 nm. Samples from human lenses manifested a band at 395 nm in addition to the two bands shown by in vitro AGEs. SF intensity is greater for the water-insoluble (WI) than water-soluble (WS) fraction, but both increased with increasing nuclear color. The immunoreactivity data also showed that the WI fraction contained more AGEs than the WS fraction and that the amount of AGEs increased with increasing nuclear color.
Fluorescence and immunoassays indicated that pigmented AGEs contributed to yellowing of the crystalline lens nucleus.
确定晚期糖基化是否为晶状体蛋白变黄的主要机制。
采用同步荧光（SF）和免疫化学分析方法研究体内外的糖基化情况。在体外研究中，制备晚期糖基化终产物（AGEs）并用作抗原以诱导抗AGEs抗体。通过SF和免疫化学分析对体外AGEs和分类的核性白内障进行分析。
由各种糖基化剂和载体蛋白生成的体外AGEs在350nm以上显示出强烈的SF；光谱分辨率良好，主要谱带位于380nm和420nm处。人晶状体样本除了体外AGEs显示的两条谱带外，在395nm处还表现出一条谱带。水不溶性（WI）部分的SF强度高于水溶性（WS）部分，但两者均随核颜色加深而增加。免疫反应性数据还表明，WI部分比WS部分含有更多的AGEs，且AGEs的量随核颜色加深而增加。
荧光和免疫分析表明，色素性AGEs导致晶状体核变黄。
