Lehto V P, Kantola I, Tervo T, Laitinen L A
Undersea Biomed Res. 1981 Jun;8(2):101-11.
The ultrastructure of the blood-bubble interface has been studied in rats decompressed experimentally. Subsequent to staining with ruthenium red there was detected by electron microscopy a continuous envelope like layer about 20 nm thick at the bubble-facing surface of the interface. The envelope like structure was visualized also by concanavalin A-ferritin, a glycosyl- and mannosyl residue-recognizing lectin coupled with an electron-dense probe, but the structure was not at all seen by the use of the conventional stains used in electron microscopy, uranyl acetate and lead citrate. No electron-dense layer was discernible on the application of only osmium tetroxide without further staining. The results indicate that material stainable by ruthenium red, and binding concanavalin A (probably a glycoprotein), is concentrated at the blood-bubble interface upon decompression. It is suggested that it plays a role in stabilization of the bubble and in the hematological alterations that are frequently observable in decompression sickness.
已对实验性减压大鼠的血泡界面超微结构进行了研究。用钌红染色后,通过电子显微镜在界面面向气泡的表面检测到一层约20纳米厚的连续包膜样层。伴刀豆球蛋白A-铁蛋白(一种与电子致密探针偶联的识别糖基和甘露糖基残基的凝集素)也显示出包膜样结构,但使用电子显微镜常规染色剂醋酸铀和柠檬酸铅则完全看不到该结构。仅使用四氧化锇而不进行进一步染色时,未观察到电子致密层。结果表明,可被钌红染色且结合伴刀豆球蛋白A(可能是一种糖蛋白)的物质在减压时集中于血泡界面。有人认为,它在气泡的稳定以及减压病中常见的血液学改变中起作用。