Studies on the synthesis of serum albumin by the isolated microsome fraction from rat liver

Campbell, P. N.; Greengard, Olga; Kernot, Barbara A.

doi:10.1042/bj0740107

Cited by 142 publications

(71 citation statements)

References 21 publications

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“…A quantitative determination of the amounts of radioactive albumin found in the microsomal membranes and cisternae after 20 and 60 min of intravenous injection of leucine-14C showed that 98 .6%/0 of the albumin was in the cisternal fraction (Table VII) . There is much information from other laboratories which also shows that albumin is in the microsomal cisternae and is not attached to the membranes (33,34) .…”

Section: Discussionmentioning

confidence: 99%

The Secretory Pathways of Rat Serum Glycoproteins and Albumin

Redman

Cherian

1972

The Journal of Cell Biology

147

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These studies compare the secretory pathways of newly formed rat serum glycoproteins and albumin by studying their submicrosomal localization at early times after the beginning of their synthesis and also by determining the submicrosomal site of incorporation of N-acetylglucosamine, mannose, galactose, and leucine into protein . N-acetylglucosamine, mannose, and galactose were only incorporated in vitro into proteins from membraneattached polysomes and not into proteins from free polysomes . Mannose incorporation occurred in the rough endoplasmic reticulum, was stimulated by puromycin but not by cycloheximide, and 90% of the mannose-labeled protein was bound to the membranes .Galactose incorporation, by contrast, occurred in the smooth microsome fraction and 89% of the radioactive protein was in the cisternae . Albumin was mostly recovered (98%0 ) in the cisternae, with negligible amounts in the membranes . To determine whether the radioactive sugars were being incorporated into serum proteins or into membrane protein, the solubilized in vivo-labeled proteins were treated with specific antisera to rat serum proteins or to albumin. Immunoelectrophoresis of the "C-labeled leucine membrane and cisternal proteins showed that the membranes contained radioactive serum glycoprotein but no albumin, while the cisternal fraction contained all of the radioactive albumin and some glycoproteins . The results indicate that newly formed serum glycoproteins remain attached to the membranes of the rough endoplasmic reticulum after they are released from the membrane-attached polysomes, while albumin passes directly into the cisternae .

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Section: Discussionmentioning

confidence: 99%

The Secretory Pathways of Rat Serum Glycoproteins and Albumin

Redman

Cherian

1972

The Journal of Cell Biology

147

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“…An unsettled question is whether the particle must remain on its membrane for complete synthesis of exportable protein to occur. Although amino acid incorporation and protein production occur in bacterial ribosomes unassociated with a cisternal membrane, similar experiments with free mammalian ribosomes from liver have shown that amino acid is incorporated, but some investigators claim that little protein is released (36).…”

Section: The Lack Of Impairment Of Amino Acid Uptake By Livers Of Trementioning

confidence: 99%

“…Histological and Histochemical Studies.--Animals were sacrificed by a sharp blow to the head at time intervals of ~, ~, 1, 2, 3, 4,6,8,12,24,36,48, and 72 hours following treatment. Complete autopsies were performed, and sections of various organs were taken for microscopical examination.…”

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confidence: 99%

An Intracellular Defect in Protein Synthesis Induced by Carbon Tetrachloride

Smuckler

Iseri

Benditt

1962

The Journal of Experimental Medicine

240

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Carbon tetrachloride when administered to animals in sufficient quantities causes liver cell injury. Earlier metabolic studies emphasized the effect of this poison on the tricarboxylic acid cycle and fatty acid oxidation. In both chemical and anatomical investigations, attention has been directed largely to the mitochondrion as the affected organelle: Christie and Judah (1) reported changes in the stability of several enzymes of the tricarboxylic acid cycle when examined 12 to 16 hours after the administration of the carbon tetrachloride. We were unable to find evidence of mitochondrial changes histochemically at earlier periods, 3 to 6 hours following carbon tetrachloride administration, when morphological evidence of cell injury is already apparent. Examination of the liver by electron microscopy at these early times following carbon tetrachloride administration also failed to reveal alterations in the mitochondria, but discernible changes were apparent in the endoplasmic reticulum. Similar changes in the endoplasmic reticulum had already been described by Oberling and Rouiller (2) and by Bassi (3) but no association of these with metabolic alterations was made.Since the rough endoplasmic reticulum is believed currently to participate in protein synthesis, the alterations produced by carbon tetrachloride suggested that there might be a defect in this process (4). The following report presents evidence that an early, and perhaps fundamental, manifestation of carbon tetrachloride is the altered relationship of the ribonucleoprotein (RNP) particles to the membranes of the rough endoplasmic reticulum and associated with this an impairment of protein synthesis within the liver cells.

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“…In liver cells, secretory proteins destined for the bloodstream are thought to be manufactured in membrane-bound polysomes and to be directly discharged into the ER cisternae (Palade and Siekevitz, 1956 ;Campbell et al ., 1960 ;Peters, 1962 a,b ; Redman and Sabatini, 1966 ;Redman, 1969 ;Ganoza and Williams, 1969), where they may be modified by enzymes bound to the limiting membranes (Molnar et al ., 1965 ;DeLorenzo et al ., 1966 ;Wagner and Cynkin, 1971 ;Redman and Cherian, 1972), before being transferred to the Golgi apparatus (Glaumann, 1970 ;Glaumann and Ericsson, 1970;Schachter et al ., 1970 ;Peters et al ., 1972) . The intracisternal route provided by the ER may also be utilized by proteins retained intracellularly which are diverted from the secretory pathway into other membrane-bound compartments, such as lysosomes (de Duve and Wattiaux, 1966 ;Goldstone and Koenig, 1972), or peroxisomes (Higashi and Peters, 1963 a,b ; Kashiwagi et al ., 1971 ; but see Lazarow andde Duve, 1973) .…”

Section: Introductionmentioning

confidence: 99%

Selective Release of Content From Microsomal Vesicles Without Membrane Disassembly

Kreibich

Sabatini

1974

The Journal of Cell Biology

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Rough and smooth microsomes were shown to have similar sets of polypeptide chains except for the proteins of ribosomes bound to the rough endoplasmic reticulum (ER) . More than 50 species of polypeptides were detected by acrylamide gel electrophoresis, ranging in molecular weight from 10,000 to approximately 200,000 daltons . The content of rough and smooth microsomes was separated from the membrane vesicles using sublytic concentrations of detergents and differential centrifugation . A specific subset of proteins which consisted of approximately 25 polypeptides was characteristic of the microsomal content . Some of these proteins showed high rates of in vivo incorporation of radioactive leucine or glucosamine, but several others incorporated only low levels of radioactivity within short labeling intervals and appeared to be long-term residents of the lumen of the ER . Seven polypeptides in the content subfractions, including serum albumin, contained almost 50% of the leucine radioactivity incorporated during 5 min and crossreacted with antiserum against rat serum . Almost all microsomal glycoproteins were at least partly released with the microsomal content .Smooth microsomes contained higher levels of albumin than rough microsomes, but after short times of labeling with [ 3 H]leucine the specific activity of albumin in the latter was higher, supporting the notion that newly synthesized serum proteins are transferred from rough to smooth portions of the ER . On the other hand, after labeling for 30 min with [ 3 H]glucosamine, smooth microsomes contained higher levels of radioactivity than rough microsomes . This would be expected if glycosidation of newly synthesized polypeptides proceeds during their transit through ER cisternae .The labeling pattern of membrane proteins in microsomes obtained from animals which received three daily injections of [ 3 H]leucine, the last administered 1 day before sacrifice, followed the intensity of bands stained with Coomassie blue,

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Studies on the synthesis of serum albumin by the isolated microsome fraction from rat liver

Cited by 142 publications

References 21 publications

The Secretory Pathways of Rat Serum Glycoproteins and Albumin

The Secretory Pathways of Rat Serum Glycoproteins and Albumin

An Intracellular Defect in Protein Synthesis Induced by Carbon Tetrachloride

Selective Release of Content From Microsomal Vesicles Without Membrane Disassembly

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