scholarly journals Dietary fish oils inhibit early events in the assembly of very low density lipoproteins and target apoB for degradation within the rough endoplasmic reticulum of hamster hepatocytes

1999 ◽  
Vol 40 (3) ◽  
pp. 504-514 ◽  
Author(s):  
John S. Kendrick ◽  
Joan A. Higgins
2016 ◽  
Vol 213 (3) ◽  
pp. 297-299 ◽  
Author(s):  
Suzanne R. Pfeffer

An unsolved mystery in cell biology is how unusually large secretory cargoes are exported from the endoplasmic reticulum. In this issue, Santos et al. (2016. J. Cell Biol. http://dx.doi.org/10.1083/jcb.201603072) report the function of a Mia2/cTAGE5 transcript fusion, named TALI, in the endoplasmic reticulum export of chylomicrons and very low-density lipoproteins, but not collagen XII.


1998 ◽  
Vol 336 (2) ◽  
pp. 311-316 ◽  
Author(s):  
Sandrine WOUTERS ◽  
Michèle LERUTH ◽  
Etienne DECROLY ◽  
Michel VANDENBRANDEN ◽  
John W. M. CREEMERS ◽  
...  

The intracellular compartmentalization in rat liver of the membrane-associated convertases furin and proprotein convertase 7 (PC7)/lymphoma PC (LPC) was investigated by analytical subcellular fractionation. In control animals, both enzymes were found to localize in fractions depleted of endoplasmic reticulum, cis-Golgi and lysosomal markers, but to co-distribute with the Golgi marker galactosyltransferase and the trans-Golgi network (TGN) marker TGN38. After overloading Golgi-derived vesicles with very-low-density lipoproteins (VLDL) by feeding rats with ethanol, the distribution of PC7/LPC was shifted markedly towards lower densities, in contrast with those of furin and the TGN marker. This provides support for the TGN localization of endogenously expressed furin and indicates that, at steady state, a considerable proportion of PC7/LPC may be associated with vesicles derived from the TGN.


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