Primate involucrins: antigenic relatedness and detection of multiple forms.
Primate involucrins: antigenic relatedness and detection of multiple forms.
复制标题
灵长类动物外皮蛋白：抗原相关性和多种形式的检测。
DOI：
10.1073/pnas.84.21.7571
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发表时间：
1987
影响因子：
11.1
通讯作者：
Rice,RH
中科院分区：
文献类型：
--
作者：
Parenteau,NL;Eckert,RL;Rice,RH
类人猿（大猩猩、黑猩猩、红毛猩猩、长臂猿）、旧世界猴（恒河猴、食蟹猴）、新世界猴（猫头鹰、cebus）和原猴（狐猴）在培养的角质形成细胞中表达外皮蛋白样蛋白。灵长类动物外皮蛋白可用三氯乙酸沉淀，在 pH 8 下重新溶解，随后在 67% 乙醇中保持水溶性。经过快速部分纯化后，对角质形成细胞提取物进行聚丙烯酰胺凝胶电泳，结果显示在每个测试物种中，有一种（黑猩猩、猩猩、长臂猿）或两种（大猩猩、恒河猴、猫头鹰、宿雾）抗原交叉反应蛋白在人外皮蛋白附近迁移。在进一步研究的物种中（大猩猩、黑猩猩、恒河猴），从培养物中分离出的 Poly(A)+ mRNA 指导多肽进行无细胞翻译，其迁移率与从细胞中提取的迁移率相似。从五只食蟹猴身上获得了三种不同的电泳图谱，表明存在不同的等位基因。通过灵敏的酶联免疫吸附测定进行的定量比较表明，某些灵长类外皮蛋白具有比人类蛋白更高密度的抗原决定簇，而其他外皮蛋白则缺乏某些决定簇。与来自其他物种的蛋白相比，所有这些蛋白均表现出显着的交叉反应性，而狐猴蛋白通过免疫印迹检测的免疫反应性极低，并且通过固相测定无法清楚地检测到。整个灵长类动物中显示的电泳和抗原差异表明该蛋白质经历了相对快速的进化。
Hominoid apes (gorilla, chimpanzee, orangutan, gibbon), Old World monkeys (rhesus, cynomolgus), New World monkeys (owl, cebus), and a prosimian (lemur) express involucrin-like proteins in cultured keratinocytes. Primate involucrins can be precipitated with trichloroacetic acid, resolubilized at pH 8, and subsequently retain aqueous solubility in 67% ethanol. Polyacrylamide gel electrophoresis of keratinocyte extracts after this rapid partial purification has revealed in each species tested one (chimpanzee, orangutan, gibbon) or two (gorilla, rhesus, owl, cebus) antigenically crossreactive proteins that migrate in the vicinity of human involucrin. In the species examined further (gorilla, chimpanzee, rhesus), poly(A)+ mRNA isolated from the cultures directed the cell-free translation of polypeptides with mobilities similar to those extracted from the cells. From five cynomolgus monkeys, three different electrophoretic profiles were obtained, suggesting the existence of different alleles. Quantitative comparisons by a sensitive enzyme-linked immunosorbent assay indicated that certain primate involucrins have a higher density of antigenic determinants than the human protein, whereas others lack some determinant(s). In contrast to those from other species, all of which showed substantial crossreactivity, the lemur protein was minimally immunoreactive by immunoblotting and not clearly detected by solid-phase assay. The electrophoretic and antigenic differences displayed throughout the primate order suggest that this protein has been subject to relatively rapid evolution.