Fine structural localization of thiamine pyrophosphatase and acid phosphatase activities in the mouse pancreatic acinar cell.
The fine structural localization of thiamine pyrophosphatase (TPPase) and acid phosphatase (AcPase) was examined in pancreatic acinar cells of fasting and fed mice. The results were not affected by these conditions. TPPase activity was positive in two and sometimes three cisternae of the inner Golgi lamellae as well as in the condensing vacuoles of the trans area, but negative in the rigid lamellae and small vesicles of the trans area. AcPase activity was demonstrated in two and sometimes three cisternae of inner Golgi lamellae, condensing vacuoles, rigid lamellae, lysosomes and smooth or coated vesicles in the trans area. The inner Golgi lamellae and the condensing vacuoles were positive for both enzyme activities. From these facts, the lysosome is considered to be formed not only in the GERL system but also through the rough endoplasmic reticulum-Golgi apparatus route. It is reasonable to consider that Novikoff's GERL is not independent from the Golgi apparatus but represents a part of this organelle.
D000135:Acid Phosphatase / Q000032:analysis*; D000818:Animals; D005215:Fasting; D006056:Golgi Apparatus / Q000201:enzymology / Q000648:ultrastructure; D006651:Histocytochemistry; D008297:Male; D051379:Mice; D010179:Pancreas / Q000166:cytology / Q000201:enzymology* / Q000648:ultrastructure; D011755:Pyrophosphatases / Q000032:analysis*; D013834:Thiamine Pyrophosphatase / Q000032:analysis*
D000135:Acid Phosphatase; D011755:Pyrophosphatases; D013834:Thiamine Pyrophosphatase