Serial section analysis of mouse hepatic peroxisomes

Publisher Website
Google Scholar
Abstract
The ultrastructure and organization of mouse hepatic peroxisomes were investigated using serial thin sections and the alkaline diaminobenzidine technique for visualization of the peroxidatic activity of catalase. Mouse periportal hepatocytes exhibit three classes of peroxisomes which display morphological and cytochemical heterogeneity: 1) large, circular to ovoid organelles containing a crystalline nucleoid, 2) small, circular to elongate, anucleoid particles, and 3) tail-like extensions which are devoid of both catalase activity (only traces of reaction deposits) and a crystaline core. Serial section analysis reveals that these profiles correspond to three diverse interconnecting peroxisomal segments which constitute a highly complex organelle. In particular, the large nucleoid-containing peroxisomal segment exhibits an intimate relationship to the endoplasmic reticulum. However, direct membrane continuities between the two compartments are never observed. With respect to the complex structure of the organelle the following conclusions can be drawn concerning biochemical studies on liver peroxisomes: 1) During homogenization and subcellular fractionation procedures, fragmentation of peroxisomes into particles of different size classes should be expected. 2) These peroxisomal fragments are inhomogeneous with respect to their matrix contents and possess at least one rupture site on their membrane surface. 3) Soluble matrix and, to a lesser degree, membrane components of peroxisomes contribute to the soluble fraction. 4) Crude microsomal fractions are regularly contaminated by peroxisomal membrane fragments.