动物造模 z-bio 2023-04-26 611

　　Objective To investigate the expression and distribution of regulatory molecules of cellular protein degradation pathway in mouse nervous system.

　　Methods The eye, brain, spinal cord, sciatic nerve and muscle tissues of 6-week-old wild-type C57BL/6J mice were used as materials, and Western blotting was used to detect the distribution and expression differences of protein degradation pathway-related proteins in different tissues, anatomical sites and subcellular structures. .

　　Results The protein degradation pathway-related protein cathepsin D (Cathepsin D), lysosomal-associated membrane protein 2 (LAMP2), autophagy microtubule-associated protein light chain 3A/B (microtubule-associated protein 1A/B) lB-light chain 3, LC3A/B), autophagy-related protein 3 (Atg3), Ras-related GTP-binding protein 7 (Ras-related GTP-binding protein 7, Rab7), calpain (Calpain) The large and small subunits and the calpastatin protein (Calpastatin) are distributed in the mouse eye, brain, spring pulp and muscle, but the expression levels are different. Compared with mouse spinal cord, the content of Calpastatin in sciatic nerve was not significantly different (P>0.05), but the content of ubiquitin, Cathepsin D, LAMP2, LC3A/B, Atg3, Rab7, Calpainl large subunit was significantly decreased (P<0.05). The content of Calpain small subunit was significantly increased (P<0.05).

　　Conclusion Under physiological conditions, the ubiquitin-proteasome system and autophagy system are widespread in cells, and in neurons, they mainly occur in the soma; while the content of the spliced Calpain small subunit in the Calpain system is relatively high in axonal bundles. higher, suggesting that the Calpain degradation pathway may play a major function in neuronal axons.