Whitnall M H, Lee Y C, Driscoll W J, Strott C A
Section on Adrenal Cell Biology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892.
J Histochem Cytochem. 1990 Nov;38(11):1607-14. doi: 10.1177/38.11.2170503.
Two proteins were isolated and purified from guinea pig adrenal cortex: a 34 KD protein that specifically binds pregnenolone (product of the rate-limiting step in steroidogenesis), and a novel co-purifying 32 KD protein that has not been characterized. Specific antisera were generated and used for immunocytochemical analysis. The 34 KD and 32 KD proteins were specific for the adrenal cortex and were absent from other tissues, including the testis. The 34 KD pregnenolone binding protein (PBP) was localized to zona fasciculata and zona reticularis cells and absent from zona glomerulosa cells. Thus, the PBP was absolutely correlated with ACTH-regulated steroidogenic cells, whereas steroidogenic cells regulated by other peptide hormones did not contain the PBP. This finding suggests a functional relationship between the PBP and ACTH. A second interesting finding was that a novel 32 KD co-purifying protein localized to the zona reticularis and was absent from the zona glomerulosa and the zona fasciculata. The 32 KD protein can therefore serve as an excellent marker for the reticularis cell of the adrenal cortex.
一种34 KD的蛋白质，它能特异性结合孕烯醇酮（类固醇生成限速步骤的产物），以及一种尚未被鉴定的新的共纯化32 KD蛋白质。制备了特异性抗血清并用于免疫细胞化学分析。34 KD和32 KD蛋白质对肾上腺皮质具有特异性，在包括睾丸在内的其他组织中不存在。34 KD的孕烯醇酮结合蛋白（PBP）定位于束状带和网状带细胞，而球状带细胞中不存在。因此，PBP与促肾上腺皮质激素（ACTH）调节的类固醇生成细胞绝对相关，而由其他肽类激素调节的类固醇生成细胞不含有PBP。这一发现表明PBP与ACTH之间存在功能关系。另一个有趣的发现是，一种新的32 KD共纯化蛋白质定位于网状带，而球状带和束状带中不存在。因此，32 KD蛋白质可作为肾上腺皮质网状带细胞的优良标志物。
