scholarly journals Cytochemical demonstration of extraperoxisomal catalase. I. Sheep liver.

1976 ◽  
Vol 24 (6) ◽  
pp. 713-724 ◽  
Author(s):  
F Roels
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Golgi Apparatus ◽  
Rough Endoplasmic Reticulum ◽  
Catalase Activity ◽  
Nonparenchymal Cells ◽  
Sheep Liver ◽  
Heat Stable ◽  
Cytochemical Demonstration ◽  
Electron Microscopes

In sheep hepatocytes catalase activity was demonstrated both within peroxisomes and within the cytosol. In the cytosol the catalase reaction product is contiguous to the plasma membrane and surrounds the nuclei, rough endoplasmic reticulum, cisternae, mitochondria and Golgi apparatus. This is the first cytochemical demonstration of guine extraperoxisomal catalase. No catalase reaction product was seen in the cytosol of nonparenchymal cells. To demonstrate catalase, both glutaraldehyde and formaldehyde fixation were used, followed by a diaminobenzidine technique modified from Novikoff and Goldfischer. Control reactions were performed to distinguish catalase reaction product from adsorption of oxidized diaminobenzidine and from precipitate due to oxidase-, peroxidase- or heat-stable peroxidatic activities. The results were evaluated in the light and electron microscopes.

Development of the lateral palatal brush in larvae of Aedes aegypti (L.) (Diptera: Culicidae)

1990 ◽  
Vol 68 (7) ◽  
pp. 1454-1467 ◽  
Author(s):  
K. M. Fry ◽  
S. B. McIver
Keyword(s):  
Electron Microscopy ◽  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Golgi Apparatus ◽  
Aedes Aegypti ◽  
Rough Endoplasmic Reticulum ◽  
Light And Electron Microscopy ◽  
Fourth Instar ◽  
Muscle Fibres ◽  
Final Length

Light and electron microscopy were used to observe development of the lateral palatal brush in Aedes aegypti (L.) larvae. Development was sampled at 4-h intervals from second- to third-instar ecdyses. Immediately after second-instar ecdysis, the epidermis apolyses from newly deposited cuticle in the lateral palatal pennicular area to form an extensive extracellular cavity into which the fourth-instar lateral palatal brush filaments grow as cytoplasmic extensions. On reaching their final length, the filaments deposit cuticulin, inner epicuticle, and procuticle sequentially on their outer surfaces. The lateral palatal crossbars, on which the lateral palatal brush filaments insert, form after filament development is complete. At the beginning of development, the organelles involved in plasma membrane and cuticle production are located at the base and middle of the cells. As the filament rudiments grow, most rough endoplasmic reticulum, mitochondria, and Golgi apparatus move to the apex of the epidermal cells and into the filament rudiments. After formation of the lateral palatal brush filaments and lateral palatal crossbars, extensive organelle breakdown occurs. Lateral palatal brush formation is unusual in that no digestion and resorption of old endocuticle occurs prior to deposition of new cuticle. No mucopolysaccharide secretion by the lateral palatal brush epidermis was observed, nor were muscle fibres observed to attach to the lateral palatal crossbars, as has been suggested by other workers.

scholarly journals Effect of microtubule assembly status on the intracellular processing and surface expression of an integral protein of the plasma membrane.

1984 ◽  
Vol 99 (3) ◽  
pp. 1101-1109 ◽  
Author(s):  
A A Rogalski ◽  
J E Bergmann ◽  
S J Singer
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Golgi Apparatus ◽  
G Protein ◽  
Rough Endoplasmic Reticulum ◽  
Intracellular Transport ◽  
Temperature Shift ◽  
Surface Expression ◽  
Microtubule Assembly ◽  
In Cells

We studied the effects of changes in microtubule assembly status upon the intracellular transport of an integral membrane protein from the rough endoplasmic reticulum to the plasma membrane. The protein was the G glycoprotein of vesicular stomatitis virus in cells infected with the Orsay-45 temperature-sensitive mutant of the virus; the synchronous intracellular transport of the G protein could be initiated by a temperature shift-down protocol. The intracellular and surface-expressed G protein were separately detected and localized in the same cells at different times after the temperature shift, by double-immunofluorescence microscopic measurements, and the extent of sialylation of the G protein at different times was quantitated by immunoprecipitation and SDS PAGE of [35S]methionine-labeled cell extracts. Neither complete disassembly of the cytoplasmic microtubules by nocodazole treatment, nor the radical reorganization of microtubules upon taxol treatment, led to any perceptible changes in the rate or extent of G protein sialylation, nor to any marked changes in the rate or extent of surface appearance of the G protein. However, whereas in control cells the surface expression of G was polarized, at membrane regions in juxtaposition to the perinuclear compact Golgi apparatus, in cells with disassembled microtubules the surface expression of the G protein was uniform, corresponding to the intracellular dispersal of the elements of the Golgi apparatus. The mechanisms of transfer of integral proteins from the rough endoplasmic reticulum to the Golgi apparatus, and from the Golgi apparatus to the plasma membrane, are discussed in the light of these observations, and compared with earlier studies of the intracellular transport of secretory proteins.

scholarly journals The rough endoplasmic reticulum and the Golgi apparatus visualized using specific antibodies in normal and tumoral prolactin cells in culture.

1983 ◽  
Vol 96 (5) ◽  
pp. 1197-1207 ◽  
Author(s):  
C Tougard ◽  
D Louvard ◽  
R Picart ◽  
A Tixier-Vidal
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Golgi Apparatus ◽  
Rough Endoplasmic Reticulum ◽  
Primary Cultures ◽  
Gh3 Cells ◽  
Membrane Flow ◽  
Golgi Membranes ◽  
Membrane Components ◽  
Golgi Zone

Antibodies directed against membrane components of dog pancreas rough endoplasmic reticulum (A-RER) and rat liver Golgi apparatus (A-Golgi) (Louvard, D., H. Reggio, and G. Warren, 1982, J. Cell Biol. 92:92-107) have been applied to cultured rat prolactin (PRL) cells, either normal cells in primary cultures, or clonal GH3 cells. In normal PRL cells, the A-RER stained the membranes of the perinuclear cisternae as well as those of many parallel RER cisternae. The A-Golgi stained part of the Golgi membranes. In the stacks it stained the medial saccules and, with a decreasing intensity, the saccules of the trans side, as well as, in some cells, a linear cisterna in the center of the Golgi zone. It also stained the membrane of many small vesicles as well as that of lysosomelike structures in all cells. In contrast, it never stained the secretory granule membrane, except at the level of very few segregating granules on the trans face of the Golgi zone. In GH3 cells the A-RER stained the membrane of the perinuclear cisternae, as well as that of short discontinuous flat cisternae. The A-Golgi stained the same components of the Golgi zone as in normal PRL cells. In some cells of both types the A-Golgi also stained discontinuous patches on the plasma membrane and small vesicles fusing with the plasma membrane. Immunostaining of Golgi membranes revealed modifications of membrane flow in relation to either acute stimulation of PRL release by thyroliberin or inhibition of basal secretion by monensin.

scholarly journals Subcellular localization of the enzyme that forms mannosyl retinyl phosphate from guanosine diphosphate [14C]mannose and retinyl phosphate

1979 ◽  
Vol 180 (3) ◽  
pp. 449-453 ◽  
Author(s):  
M J Smith ◽  
J B Schreiber ◽  
G Wolf
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Golgi Apparatus ◽  
Subcellular Localization ◽  
Rat Liver ◽  
Rough Endoplasmic Reticulum ◽  
Subcellular Distribution ◽  
Smooth Endoplasmic Reticulum ◽  
Marker Enzymes ◽  
Guanosine Diphosphate

The subcellular distribution of the enzyme catalysing the conversion of retinyl phosphate and GDP-[14C]mannose into [14C]mannosyl retinyl phosphate was determined by using subcellular fractions of rat liver. Purity of fractions, as determined by marker enzymes, was 80% or better. The amount of mannosyl retinyl phosphate formed (pmol/min per mg of protein) for each fraction was: rough endoplasmic reticulum 0.48 +/- 0.09 (mean +/- S.D.); smooth membranes (consisting of 60% smooth endoplasmic reticulum and 40% Golgi apparatus), 0.18 +/- 0.03; Golgi apparatus, 0.13 +/- 0.03; and plasma membrane 0.02.

scholarly journals Immunocytochemical localization of Mullerian inhibiting substance in the rough endoplasmic reticulum and Golgi apparatus in Sertoli cells of the neonatal calf testis using a monoclonal antibody.

1984 ◽  
Vol 32 (6) ◽  
pp. 649-654 ◽  
Author(s):  
M Hayashi ◽  
H Shima ◽  
K Hayashi ◽  
R L Trelstad ◽  
P K Donahoe
Keyword(s):  
Monoclonal Antibody ◽  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Rough Endoplasmic Reticulum ◽  
Sertoli Cells ◽  
Neonatal Calf ◽  
Müllerian Inhibiting Substance ◽  
Pap Method ◽  
Unlabeled Antibody ◽  
Mullerian Inhibiting Substance

Mullerian Inhibiting Substance (MIS) has been localized in the Sertoli cells of the neonatal calf testis using preembedding immunoperoxidase techniques and a monoclonal antibody which almost completely blocks the biological activity of MIS. Both the peroxidase-labeled antibody method using a peroxidase-conjugated F(ab')2 fragment of IgG as a second antibody and the unlabeled antibody peroxidase-antiperoxidase (PAP) method using Fab fragments of the PAP complex were employed. With both methods, MIS was demonstrated within the cisternae of the rough endoplasmic reticulum (RER) and the Golgi apparatus. In the Golgi, MIS was concentrated in the transmost cisternae especially at their peripheral expansions. This study indicates that MIS is synthesized in the RER and transported to the Golgi apparatus, presumably for glycosidation, before secretion from Golgi derived vacuoles.

scholarly journals The pattern of appearance of enzymic activity during the development of the Golgi apparatus in amoebae

1978 ◽  
Vol 34 (1) ◽  
pp. 53-63
Author(s):  
C.J. Flickinger
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Rough Endoplasmic Reticulum ◽  
Enzymic Activity ◽  
Nuclear Transplantation ◽  
Similar Distribution ◽  
Cytochemical Staining ◽  
Light Reaction ◽  
Golgi Bodies ◽  
Golgi Membranes

The appearance of enzymic activity during the development of the Golgi apparatus was studied by cytochemical staining of renucleated amoebae. In cells enucleated for 4 days, there was a great decline in size and number of Golgi bodies, or dictyosomes. Subsequent renucleation by nuclear transplantation resulted in a regeneration of Golgi bodies. Samples of amoebae were fixed and incubated for cytochemical staining at intervals of 1, 6, or 24 h after renucleation. Enzymes selected for study were guanosine diphosphatase (GDPase), esterase, and thiamine pyrophosphatase (TPPase). All three were found in the Golgi apparatus of normal amoebae but they differed in their overall intracellular distribution. GDPase was normally present at the convex pole of the Golgi apparatus, in rough endoplasmic reticulum, and in the nuclear envelope. In amoebae renucleated for 1 h, light reaction product for GDPase was present throughout the small stacks of cisternae that represented the forming Golgi apparatus. By 6 h following the operation GDPase reaction product was concentrated at the convex pole of the Golgi apparatus. Esterase, which was distributed throughout the stacks of normal Golgi cisternae, displayed a similar distribution in the forming Golgi bodies as soon as they were visible. TPPase was normally present in the Golgi apparatus but was not found in the endoplasmic reticulum. In contrast to the other enzymes, TPPase reaction product was absent from the forming Golgi apparatus 1 and 6 h after renucleation, and did not appear in the Golgi apparatus until 24 h after operation. Thus, enzymes held in common between the rough endoplasmic reticulum and the Golgi apparatus were present in the forming Golgi apparatus as soon as it was detectable, but an enzyme cytochemically localized to the Golgi apparatus only appeared later in development of the organelle. It is suggested that Golgi membranes might be derived from the endoplasmic reticulum and thus immediately contain endoplasmic reticulum enzymes, while Golgi-specific enzymes are added later in development.

scholarly journals THE ELABORATION OF PROTEIN AND CARBOHYDRATE BY RAT PARATHYROID CELLS AS REVEALED BY ELECTRON MICROSCOPE RADIOAUTOGRAPHY

1971 ◽  
Vol 51 (3) ◽  
pp. 596-610 ◽  
Author(s):  
K. Nakagami ◽  
H. Warshawsky ◽  
C. P. Leblond
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Intravenous Injection ◽  
Rough Endoplasmic Reticulum ◽  
Secretory Granules ◽  
Glycoprotein Precursor ◽  
Secretion Granules ◽  
And Migration ◽  
The One ◽  
Membrane Cell

The parathyroid glands of young rats were radioautographed after a single injection of the protein precursor tyrosine-3H in the hope of identifying the sites of synthesis and migration of newly formed protein in the gland cells. The same procedure was used after injection of the glycoprotein precursor galactose-3H. As early as 2 min after intravenous injection of tyrosine-3H, the label was mainly found in the rough endoplasmic reticulum suggesting that cisternal ribosomes are sites of protein synthesis. By 5 and 10 min, much of the label had migrated from the rough endoplasmic reticulum into the Golgi apparatus. By 20 and 30 min, some label had migrated from there into secretory granules. By 45 min and 1 hr, the label content of the cell had decreased, indicating release of labeled material outside the cell. At 2 min after intravenous injection of galactose-3H, the label was mainly present in the Golgi apparatus, where presumably galactose is taken up into glycoprotein. By 10 min, some label appeared in secretion granules and by 30 min release of the material to the outside of the cell was under way. In conclusion, it is likely that the tyrosine-labeled protein material consists mainly of the parathyroid hormone. The galactose-labeled carbohydrate material would be either associated with the hormone in the cell or be part of a distinct glycoprotein which may be the one present on the outer surface of the plasma membrane (cell coat).

Sign in / Sign up

Export Citation Format

Share Document