Passage of serum-destined proteins through the Golgi apparatus of rat liver. An examination of heavy and light Golgi fractions.

Bergeron, John J.M.; Borts, D; Cruz, Jonathan C.

doi:10.1083/jcb.76.1.87

Cited by 66 publications

(23 citation statements)

References 25 publications

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“…A large body of indirect evidence [considered elsewhere (6)] supports this view by implying that the terminal glycosyltransferases that act in the late compartment are concentrated in the trans-most cisterna or two of the stack. The compartment boundary would then divide the Golgi stack into two distinct portions, explaining the cis-trans asymmetry so evident in earlier morphological and histochemical studies (1)(2)(3)(4)(5)(6)(7)(8)(9)(10). It is entirely possible, however, that there are additional Golgi-associated compartments.…”

Section: Resultsmentioning

confidence: 94%

“…It is likely that these compartments consist of cisternae on the cis and trans sides of the Golgi stack. The stack of cisternae composing the Golgi apparatus is markedly asymmetric (1-7), its cis [or entry (8,9)] and trans [or exit (9, 10)] faces differing in morphological and histochemical properties. This cis-trans polarity could signify a fundamental division of the stack into functionally distinct compartments between which proteins can be transported vectorially.…”

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confidence: 99%

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Early and late functions associated with the Golgi apparatus reside in distinct compartments.

Dunphy¹,

Fries²,

Urbani³

et al. 1981

Proc. Natl. Acad. Sci. U.S.A.

198

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Enzymes that catalyze the two successive stages of Golgi-associated processing of asparagine-linked oligosaccharides distributed differently when membranes from Chinese hamster ovary cells were centrifuged in a sucrose density gradient. A mannosidase that removes only outer, a-1,2-linked mannose residues from the precursor oligosaccharides of the vesicular stomatitis viral G protein (to yield a "trimmed" oligosaccharide core) was separated from enzymes (galactosyl-and sialyltransferases) that act in the later, terminal stage ofglycosylation. Freshly acylated G protein with newly trimmed oligosaccharides banded in the distribution of early-acting membranes, defined by the mannosidase, whereas G protein pulse-labeled with [3H]galactose distributed in the profile of the late-acting membranes. G protein present in the early-acting membranes in crude fractions could be terminally glycosylated by incubation with exogenous Golgi membranes in vitro; G protein lost its ability to be processed in vitro as it appeared to enter the late-acting membranes in vivo. These experiments reveal the existence of two distinct compartments through which intracellularly transported proteins such as G pass in sequence as Golgi-associated processes are carried out. It is likely that these compartments consist of cisternae on the cis and trans sides of the Golgi stack. The stack of cisternae composing the Golgi apparatus is markedly asymmetric (1-7), its cis [or entry (8, 9)] and trans [or exit (9, 10)] faces differing in morphological and histochemical properties. This cis-trans polarity could signify a fundamental division of the stack into functionally distinct compartments between which proteins can be transported vectorially. Alternatively, this overall asymmetry could reflect a continuous gradient ofcomposition, the result ofa sorting process operating within a stack composed of multiple copies of the same kind of compartment.We recently reported (11) a dramatic change in the behavior in a cell-free assay system (12, 13) of a plasma membrane-type glycoprotein [the G protein encoded by vesicular stomatitis virus (VSV)] that occurred as a result of passage through the Golgi. Specifically, the assay distinguished two intracellular pools through which G protein passed in rapid succession: an earlier "transferable" pool that can be donated by membranes from infected cells to exogenous Golgi for oligosaccharide processing in vitro and a later "nontransferable" pool that cannot. The transferable pool appeared to reside in Golgi membranes (11). If the other pool also resided in Golgi membranes, but in a different region, then the change in properties of G protein (transferable-versus nontransferable) in going from one region ofthe Golgi to the other would signify a compartment boundary in between.Asparagine-linked oligosaccharides (such as those ofthe VSV G protein) are processed in two major stages (14-16). First, the precursor oligosaccharide is "trimmed" by the removal of four a-1,2-linked mannose units. Later, terminal glycosyl...

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Section: Resultsmentioning

confidence: 94%

mentioning

confidence: 99%

Early and late functions associated with the Golgi apparatus reside in distinct compartments.

Dunphy¹,

Fries²,

Urbani³

et al. 1981

Proc. Natl. Acad. Sci. U.S.A.

198

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“…Specific glycosyltransferases and associated glycosidases have been assigned to distinct Golgi subcompart ments as defined by subcellular fractionation [6,7], in situ lectin binding [8,9], sugar uptake as assessed by radioautography [10] as well as in situ immunocytochemistry of galactosyltransferases [11], These studies as well as observations on the transport of secretory [12] and membrane proteins [13,14] imply distinct domains in the Golgi apparatus containing the corresponding gly cosyltransferases.…”

Section: Discussionmentioning

confidence: 99%

Seminal Plasma Levels of Fucosyltransferase, Galactosyltransferase and Sialyltransferase in Normospermic and Oligospermic Men

Ronquist¹

1987

Urol Int

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The activities of fucosyltransferase, galactosyltransferase, and sialyltransferase were estimated in ultra-centrifuged seminal plasma samples from normospermic and oligospermic men. There was no significant difference with regard to these activities between the two groups. Hence, fucosyltransferase activity was high in both normospermic (mean value: 190.2 nmol/l) and oligospermic men (mean value: 157.2 nmol/l) and exceeded that of blood plasma (mean value: 7.6 nmol/l) by 20–25 times. On the contrary, the activity ratio between seminal plasma and blood plasma of galactosyltransferase and sialyltransferase was low and fairly close to 1. A significant correlation was noted between seminal plasma galactosyltransferase activity and semen volume only in normospermic men. Significant inverse correlations in oligospermic men were observed between seminal plasma sialyltransferase activity and sperm concentration (and total sperm count) as well as between galactosyltransferase and fucosyltransferase activities.

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“…The secretion of plasma proteins via the Golgi apparatus of rat liver has been described (3,14,32,39) . 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) .…”

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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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Passage of serum-destined proteins through the Golgi apparatus of rat liver. An examination of heavy and light Golgi fractions.

Cited by 66 publications

References 25 publications

Early and late functions associated with the Golgi apparatus reside in distinct compartments.

Early and late functions associated with the Golgi apparatus reside in distinct compartments.

Seminal Plasma Levels of Fucosyltransferase, Galactosyltransferase and Sialyltransferase in Normospermic and Oligospermic Men

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

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