In vivo effect of colchicine on hepatic protein synthesis and on the conversion of proalbumin to serum albumin

Redman, CM; Banerjee, Dev; Manning, Curt; Huang, C. W.; Green, K

doi:10.1083/jcb.77.2.400

Cited by 76 publications

(13 citation statements)

References 31 publications

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“…Upon reestablishing secretory flow from the ER to the Golgi in this manner, transport from dispersed Golgi sites to the cell surface, as shown by occurs efficiently, but is no longer directed to specific regions of the cell surface. This interpretation offers a reasonable explanation to the conflicting data regarding the role of microtubules in secretion, where some studies have shown no effect of microtubule disruption Van De Moortele et al, 1993), while others have found significant effects (Redman et al, 1978;Boyd et al, 1982;Breitfield et al, 1990;Gilbert et al, 1991;Rennison et al, 1992). It also supports studies of Saraste and Svensson (1991) that suggested that ER-to-Golgi transport intermediates use microtubules to translocate into the Golgi region.…”

Section: Golgi Fragmentationmentioning

confidence: 90%

Golgi dispersal during microtubule disruption: regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites.

Cole

Sciaky

Marotta

et al. 1996

MBoC

476

468

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Microtubule disruption has dramatic effects on the normal centrosomal localization of the Golgi complex, with Golgi elements remaining as competent functional units but undergoing a reversible "fragmentation" and dispersal throughout the cytoplasm. In this study we have analyzed this process using digital fluorescence image processing microscopy combined with biochemical and ultrastructural approaches. After microtubule depolymerization, Golgi membrane components were found to redistribute to a distinct number of peripheral sites that were not randomly distributed, but corresponded to sites of protein exit from the ER. Whereas Golgi enzymes redistributed gradually over several hours to these peripheral sites, ERGIC-53 (a protein which constitutively cycles between the ER and Golgi) redistributed rapidly (within 15 minutes) to these sites after first moving through the ER. Prior to this redistribution, Golgi enzyme processing of proteins exported from the ER was inhibited and only returned to normal levels after Golgi enzymes redistributed to peripheral ER exit sites where Golgi stacks were regenerated. Experiments examining the effects of microtubule disruption on the membrane pathways connecting the ER and Golgi suggested their potential role in the dispersal process. Whereas clustering of peripheral pre-Golgi elements into the centrosomal region failed to occur after microtubule disruption, Golgi-to-ER membrane recycling was only slightly inhibited. Moreover, conditions that impeded Golgi-to-ER recycling completely blocked Golgi fragmentation. Based on these findings we propose that a slow but constitutive flux of Golgi resident proteins through the same ER/Golgi cycling pathways as ERGIC-53 underlies Golgi Dispersal upon microtubule depolymerization. Both ERGIC-53 and Golgi proteins would accumulate at peripheral ER exit sites due to failure of membranes at these sites to cluster into the centrosomal region. Regeneration of Golgi stacks at these peripheral sites would re-establish secretory flow from the ER into the Golgi complex and result in Golgi dispersal.

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Section: Golgi Fragmentationmentioning

confidence: 90%

Golgi dispersal during microtubule disruption: regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites.

Cole

Sciaky

Marotta

et al. 1996

MBoC

476

468

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“…As noted in Table VI the radiolabeled material from subcellular fractions of colchicine-treated rats was comparable in integrity to that from subcellular fractions of control rats. In previous studies it was shown that colchicine administration (0.5-25 pmol/100 g body wt) caused an inhibition of hepatic protein synthesis (40) . Since cycloheximide treatment of rats resulted in a rapid decrease in hepatic lactogen receptors levels (18), we considered whether the inhibition of 125 1-oPRL uptake into GI and Gi fractions reflected a depletion of lactogen receptor in these fractions secondary to an inhibition of protein synthesis.…”

Section: Discussionmentioning

confidence: 99%

“…Colchicine has been shown to inhibit the secretory process in liver (2,10,(39)(40)(41) and other tissues (15,20,21,30,31,47) . It has been shown to have a disorganizing effect on Golgi structure in certain tissues (44) and to inhibit endocytosis in chondrocytes (33), fibroblasts (45), and macrophages (44).…”

mentioning

confidence: 99%

Effect of colchicine on the uptake of prolactin and insulin into Golgi fractions of rat liver.

Posner¹,

Verma²,

Patel³

et al. 1982

The Journal of Cell Biology

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In previous studies we have shown that 125I-labeled prolactin is taken up by a receptor-dependent process and concentrated in an intact form in Golgi elements from female rat liver (J. Biol. Chem., 1979, 254:209-214). In this study we have examined the effect of colchicine on this uptake process into Golgi elements. Colchicine [25 mumol (10 mg)/100 gm body wt] was injected intraperitoneally in adult female rats, and hepatic Golgi fractions were prepared at 1, 2, and 3 h postinjection. The enzyme recoveries and morphological appearance of fractions from colchicine-treated and control (alcohol alone) animals were similar. At times greater than 1 h after colchicine there was a marked (greater than 60%) inhibition of uptake of 125I-ovine prolactin (125I-oPRL) into Golgi light and intermediate fractions but no inhibition of uptake into Golgi heavy and plasmalemma elements. At times from 2 to 45 min postinjection, 125I-oPRL was extracted from Golgi elements and found to be largely intact as judged by rebinding to receptors. The inhibitory effect of colchicine was seen at doses ranging from 0.25 mumol to 25 mumol/100 g body wt. Vincristine also inhibited 125I-oPRL uptake into the Golgi light and intermediate fractions but lumicolchicine had no inhibitory effect. There was a smaller effect of colchicine both at early (1 h) and later (3 h) times on the extent and pattern of 125I-insulin uptake. Colchicine treatment did not produce a significant change in lactogen receptor levels in the Golgi fractions. These results demonstrate that colchicine treatment inhibited the transfer of prolactin into Golgi vesicular elements. The much smaller effect on insulin uptake suggests that there may be differences in the manner in which the two hormones are handled in the course of internalization.

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“…There was no difference in the appearance of the RER in colchicine-treated rats and the RER of rats given cycloheximide; in both cases bound ribosomes were positive for antigens of albumin and the lumen of the RER was negative. After colchicine injection, excessive albumin has been demonstrated in the Golgi region and in an increased number of Golgiderived secretion vesicles (Redman et al, 1978); both of these effects were seen here.…”

Section: Discussionmentioning

confidence: 69%

Ultrastructural immunocytochemistry of nascent albumin topology: Proposed cytosolic folding and membrane transit of the protein

LeBouton

Masse

1981

Anat. Rec.

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The relationship of nascent albumin and hepatocyte organelles was studied with the immunoperoxidase reaction in rats given various drugs to alter cellular albumin content. colchicine was used to increase intracellular albumin. Cycloheximide inhibited synthesis but allowed nascent albumin to remain with its ribosome of origin. Puromycin also inhibited synthesis but released albumin from its ribosome. There was no difference in the appearance of attached ribosomes in hepatocytes from saline-injected rats and those given colchicine or cycloheximide. In these cases, membranes of the endoplasmic reticulum were consistently decorated with ribosomes positive for the presence of albumin antigenicity on their cytosolic surface. The cisternal and cytosolic compartments were negative. The situation after puromycin was different. Here the membranes appeared to be denuded of ribosomes and reaction product, indicative of albumin, was present only on the lumenal surface. To determine whether puromycin had caused the release of ribosomes, sections from puromycin-treated cells were stained nonspecifically with uranyl acetate. This showed that the normal amount of ribosomes was still bound but that they could not be seen when a probe specific only for albumin was used. It appears that nascent albumin can associate with its ribosome within the cytosol. Also, apparently after albumin passes through the membrane of the rough endoplasmic reticulum, it remains attached to its lumenal surface. A model incorporating cytosolic folding of albumin followed by its entropic membrane transit is presented.

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In vivo effect of colchicine on hepatic protein synthesis and on the conversion of proalbumin to serum albumin

Cited by 76 publications

References 31 publications

Golgi dispersal during microtubule disruption: regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites.

Golgi dispersal during microtubule disruption: regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites.

Effect of colchicine on the uptake of prolactin and insulin into Golgi fractions of rat liver.

Ultrastructural immunocytochemistry of nascent albumin topology: Proposed cytosolic folding and membrane transit of the protein

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