Dalhoff A
Zentralbl Bakteriol Mikrobiol Hyg A Med Mikrobiol Infekt Parasitol. 1983 May;254(3):379-87.
Uptake of nine aminoglycosides was studied in E. coli K12 and mutants being defective in the outer membrane proteins OmpF and OmpC or in ATPase (uncA). OmpF/OmpC as well as uncA mutants did not take up the aminoglycosides; transport in wild type cells was cAMP dependent. The specific binding of phages using the OmpF and OmpC proteins as receptors was strongly reduced by the aminoglycosides or by other polycationic peptides. Thus it may be assumed that the initial step of aminoglycoside transport is their electrostatic binding to the anionic porins, especially to the ompF porin, followed by a facilitated permeation through the outer membrane. As the synthesis of this porin is under cAMP control, aminoglycoside transport is cAMP dependent as well. The fact that the uncA mutant did not take up the aminoglycosides to any appreciable extent indicates that the cytoplasmic membrane is involved in aminoglycoside transport too.
研究了9种氨基糖苷类药物在大肠杆菌K12及其外膜蛋白OmpF和OmpC或ATP酶（uncA）缺陷型突变体中的摄取情况。OmpF/OmpC以及uncA突变体不摄取氨基糖苷类药物；野生型细胞中的转运是cAMP依赖性的。以OmpF和OmpC蛋白作为受体的噬菌体的特异性结合被氨基糖苷类药物或其他聚阳离子肽强烈降低。因此，可以推测氨基糖苷类药物转运的起始步骤是它们与阴离子孔蛋白，特别是与ompF孔蛋白的静电结合，随后通过外膜的易化渗透。由于这种孔蛋白的合成受cAMP控制，氨基糖苷类药物的转运也是cAMP依赖性的。uncA突变体在任何可观程度上都不摄取氨基糖苷类药物这一事实表明，细胞质膜也参与了氨基糖苷类药物的转运。
