Relationship between peroxisomes and endoplasmic reticulum investigated by combined catalase and glucose-6-phosphatase cytochemistry.
The theoretical advantages of electron microscopic cytochemistry were utilized to look for evidence of possible connections between peroxisomes and the endoplasmic reticulum in rat liver. Established cytochemical procedures for catalase (peroxisomes) and glucose-6-phosphatase (endoplasmic reticulum) were carried out, and evidence was sought of diffusion of reaction products between the organelles. No such diffusion was observed: lead phosphate was found in the endoplasmic reticulum and in the nuclear envelope but not in peroxisomes; oxidized diaminobenzidine (DAB) was seen only in peroxisomes. In addition, both types of cytochemistry were carried out on the same tissue. The two kinds of reaction product could be distinguished by virtue of their different electron opacities. No mixing of the two reaction products was observed. These results do not support the hypothesis that peroxisomes and endoplasmic reticulum may be connected; rather, they support the idea that the two organelles exist as separate cellular compartments.
D015100:3,3'-Diaminobenzidine; D000818:Animals; D002374:Catalase / Q000378:metabolism*; D002451:Cell Compartmentation; D004721:Endoplasmic Reticulum / Q000648:ultrastructure*; D005952:Glucose-6-Phosphatase / Q000378:metabolism*; D006651:Histocytochemistry; D008099:Liver / Q000201:enzymology* / Q000648:ultrastructure; D008297:Male; D008830:Microbodies / Q000648:ultrastructure*; D009940:Organoids / Q000648:ultrastructure*; D051381:Rats; D011916:Rats, Inbred F344
D015100:3,3'-Diaminobenzidine; D002374:Catalase; D005952:Glucose-6-Phosphatase