Studies on Rat Liver Catalase V. Incorporation of 14C-Leucine into Catalase by Isolated Rat Liver Ribosomes*

Kashiwagi, Kiyoko; Tobe, Takashi; Higashi, Tokuhiko

doi:10.1093/oxfordjournals.jbchem.a129696

Cited by 20 publications

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“…It appears more likely, however, that such content proteins represent products of the ER which are first discharged into the cisternae but are retained intracellularly by subsequent diversion into other membrane-bound compartments . In this respect it is interesting to note that an ER origin has been suggested for lysosomal (de Duve and Wattiaux, 1966 ;Goldstone and Koenig, 1972) and peroxisomal proteins, and evidence has been presented to suggest that recently synthesized catalase is contained in rough microsomes (Higashi and Peters, 1963 a,b;Kashiwagi et al ., 1971 ; but see and Lazarow and de Duve, 1973) . In the gel system used by us, catalase has the same mobility as band no .…”

Section: Discussionmentioning

confidence: 99%

“…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) . It has also been shown that at least some membrane proteins of the ER are synthesized on membrane-bound ribosomes (Omura, 1973), and it is possible that these proteins are first discharged into the cisternal cavity before being incorporated into the membranes .…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Discussionmentioning

confidence: 99%

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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“…Or it could be made by both free and bound ribosomes, as proposed by Higashi and co-workers (13,19) . Or it could be synthesized in, or rapidly transferred to, a fragile cytoplasmic particle, which is largely destroyed by homogenization .…”

Section: Mode Of Transfer Of Catalase To Peroxisomesmentioning

confidence: 92%

The Synthesis and Turnover of Rat Liver Peroxisomes

Lazarow

Duve

1973

The Journal of Cell Biology

195

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The subcellular distribution of the biosynthetic intermediates of catalase was studied in the livers of rats receiving a mixture of [3H]leucine and [14C]δ-aminolevulinic acid by intraportal injection. Postnuclear supernates were fractionated by a one-step gradient centrifugation technique that separates the main subcellular organelles, partly on the basis of size, and partly on the basis of density. Labeled catalase and its biosynthetic intermediates were separated from the gradient fractions by immunoprecipitation, and the distributions of radioactivity were compared with those of marker enzymes. The results show that catalase protein is synthesized outside the peroxisomes, but rapidly appears in these particles, mostly still in the form of the first hemeless biosynthetic intermediate. Addition of heme and completion of the catalase molecule take place within the peroxisomes. During the first 15 min after [3H]leucine administration, more than half of the newly formed first intermediate was recovered in the supernatant fraction, where it was found to exist as an aposubunit of about 60,000 molecular weight.

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“…Besides NADPH-cytochrome c reductase, two other proteins, catalase (Higashi et al, 1972;Kashiwagi et al, 1971) and globin (Woodward et al, 1973), are similarly synthesized by free and membranebound ribosomes, although in the reticulocyte the latter are not attached to an endoplasmic reticulum but to the cell membrane. Therefore only the relative proportions in the cell of both kinds of ribosomes would determine their contribution to the formation of those proteins in vivo.…”

mentioning

confidence: 99%

Role of membrane-bound and free polyribosomes in the synthesis of cytochrome c in rat liver

González‐Cadavid

Córdova

1974

Biochemical Journal

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The functional distinction of membrane-bound and free polyribosomes for the synthesis of exportable and non-exportable proteins respectively is not so strict as was initially thought, and it was therefore decided to investigate their relative contribution to the elaboration of an internal protein integrated into a cell structure. Cytochrome c was chosen as an example of a soluble mitochondrial protein, and the incorporation of [(14)C]leucine and delta-amino[(14)C]laevulinate into the molecule was studied by using different ribosomal preparations from regenerating rat liver. A new procedure was devised for the purification of cytochrome c, based on ion-exchange chromatography combined with sodium dodecyl sulphate-polyacrylamide-gel electrophoresis. In spite of cytochrome c being a non-exportable protein, the membrane-bound polyribosomes were at least as active as the free ribosomes in the synthesis in vitro of the apoprotein and the haem moiety. The detergent-treated ribosomes could also effect the synthesis of cytochrome c, although at a lower rate. Since in liver more than two-thirds of the ribosomes are bound to the endoplasmic-reticulum membranes, it is considered that in vivo they are responsible for the synthesis of most of the cytochrome c content of the cell. This suggests that in secretory tissues the endoplasmic reticulum plays a predominant role in mitochondrial biogenesis, although free ribosomes may participate in the partial turnover of some parts of the organelle. The hypothesis on the functional specialization of the different kinds of ribosomes was therefore modified to account for their parallel intervention in the synthesis of proteins associated with membranous structures.

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Studies on Rat Liver Catalase V. Incorporation of 14C-Leucine into Catalase by Isolated Rat Liver Ribosomes*

Cited by 20 publications

References 0 publications

Selective Release of Content From Microsomal Vesicles Without Membrane Disassembly

Selective Release of Content From Microsomal Vesicles Without Membrane Disassembly

The Synthesis and Turnover of Rat Liver Peroxisomes

Role of membrane-bound and free polyribosomes in the synthesis of cytochrome c in rat liver

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