scholarly journals Nonuniform distribution of sodium in the rat hepatocyte.

1976 ◽  
Vol 67 (4) ◽  
pp. 469-474 ◽  
Author(s):  
G Hooper ◽  
D A Dick
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Complex ◽  
Rat Hepatocytes ◽  
Nonuniform Distribution ◽  
Flame Photometry ◽  
Ground Substance ◽  
Rat Hepatocyte ◽  
Correlation Parameters ◽  
Cytoplasmic Ground Substance

The volume of the nucleus, endoplasmic reticulum (including Golgi complex), mitochondria, and cytoplasmic ground substance was measured in rat hepatocytes by stereological methods. The Na content was also measured by flame photometry. Variations in Na content correlated significantly with variations in volume of nucleus and endoplasmic reticulum. From the correlation parameters, Na concentrations were estimated as follows: nucleus, 108 mM; endoplasmic reticulum (ER) (including Golgie complex) 27 mM; cytoplasm (including and remaining organelles) 16 mM.

Organisation in the Structure of the Cytoplasmic Ground Substance

1978 ◽  
Vol 36 (3) ◽  
pp. 627-639
Author(s):  
K.R. Porter
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Complex ◽  
Random Distribution ◽  
Ground Substance ◽  
The Matrix ◽  
Cell Processes ◽  
Cytoplasmic Ground Substance

Most types of cells are known from their structure and overall form to possess a characteristic organization. In some instances this is evident in the non-random disposition of organelles and such system subunits as cisternae of the endoplasmic reticulum or the Golgi complex. In others it appears in the distribution and orientation of cytoplasmic fibrils. And in yet others the organization finds expression in the non-random distribution and orientation of microtubules, especially as found in highly anisometric cells and cell processes. The impression is unavoidable that in none of these cases is the organization achieved without the involvement of the cytoplasmic ground substance (CGS) or matrix. This impression is based on the fact that a matrix is present and that in all instances these formed structures, whether membranelimited or filamentous, are suspended in it. In some well-known instances, as in arrays of microtubules which make up axonemes and axostyles, the matrix resolves itself into bridges (and spokes) between the microtubules, bridges which are in some cases very regularly disposed and uniform in size (Mcintosh, 1973; Bloodgood and Miller, 1974; Warner and Satir, 1974).

scholarly journals The effects of low temperatures on intracellular transport of newly synthesized albumin and haptoglobin in rat hepatocytes

1986 ◽  
Vol 237 (1) ◽  
pp. 33-39 ◽  
Author(s):  
E Fries ◽  
I Lindström
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Complex ◽  
Low Temperatures ◽  
Intracellular Transport ◽  
Rat Hepatocytes ◽  
Subcellular Fractionation ◽  
Isolated Rat Hepatocytes ◽  
Different Temperatures ◽  
Lag Period ◽  
Time Courses

Isolated rat hepatocytes were pulse-labelled with [35S]methionine at 37 degrees C and subsequently incubated (chased) for different periods of time at different temperatures (37-16 degrees C). The time courses for the secretion of [35S]methionine-labelled albumin and haptoglobin were determined by quantitative immunoprecipitation of the detergent-solubilized cells and of the chase media. Both proteins appeared in the chase medium only after a lag period, the length of which increased markedly with decreasing chase temperature: from about 10 and 20 min at 37 degrees C to about 60 and 120 min at 20 degrees C for albumin and haptoglobin respectively. The rates at which the proteins were externalized after the lag period were also strongly affected by temperature, the half-time for secretion being 20 min at 37 degrees C and 200 min at 20 degrees C for albumin; at 16 degrees C no secretion could be detected after incubation for 270 min. Analysis by subcellular fractionation showed that part of the lag occurred in the endoplasmic reticulum and that the rate of transfer to the Golgi complex was very temperature-dependent. The maximum amount of the two pulse-labelled proteins in Golgi fractions prepared from cells after different times of chase decreased with decreasing incubation temperatures, indicating that the transport from the Golgi complex to the cell surface was less affected by low temperatures than was the transport from the endoplasmic reticulum to the Golgi complex.

scholarly journals OBSERVATIONS ON A SUBMICROSCOPIC BASOPHILIC COMPONENT OF CYTOPLASM

1953 ◽  
Vol 97 (5) ◽  
pp. 727-750 ◽  
Author(s):  
Keith R. Porter
Keyword(s):  
Endoplasmic Reticulum ◽  
Dark Field ◽  
Ground Substance ◽  
Adjacent Cell ◽  
Submicroscopic Structure ◽  
Dark Field Microscopy ◽  
Reticular System ◽  
Living Unit ◽  
Cytoplasmic Ground Substance

The cytoplasmic ground substance of animal tissue cells grown in vitro has been found by electron microscopy to contain, as a part of its submicroscopic structure, a complex reticulum of strands, to be referred to as the endoplasmic reticulum. It has been found in all types of cells extensively studied. The components of this reticular system vary considerably in size and form, apparently in some relation to physiological changes in the cell. Thus in one cell of a culture colony it may be finely divided into strands or canaliculi, 50 to 100 mµ in diameter, whereas in an adjacent cell of the same type the components of the reticulum may be relatively coarse, 600 mµ in diameter, and vesiculated. The membrane, which can be shown to limit the system and separate it from the rest of the ground substance, is similar in thickness to the plasma membrane surrounding the cell. Photomicrographs of living cells taken by phase contrast and dark field microscopy define a structure of similar form and indicate that the reticulum of the electron microscope image has its equivalent in the living unit. Where its component units are sufficiently large, a structure of identical form can be resolved by light microscopy in cells stained with hematoxylin or with toluidine blue. This indicated that the endoplasmic reticulum is to be identified with the basophilic or chromophilic component (the ergastoplasm) of the cytoplasm and that such properties of this component as have been determined by cytochemical methods, such as a high RNA content, may be assigned to this "submicroscopic" system.

The fine structure of RNA-storing archaeocytes from gemmules of fresh-water sponges

1965 ◽  
Vol s3-106 (73) ◽  
pp. 99-114
Author(s):  
AUGUST RUTHMANN
Keyword(s):  
Endoplasmic Reticulum ◽  
Fine Structure ◽  
Fresh Water ◽  
Structural Integrity ◽  
Structural Aspect ◽  
Ground Substance ◽  
Annulate Lamellae ◽  
Golgi Bodies ◽  
High Concentrations ◽  
Cytoplasmic Ground Substance

Gemmules of fresh-water sponges contain about 500 binucleated cells (‘archaeocytes’) which are loaded with reserve substances including ribonucleoprotein, acidophilic proteins, lipids, and polysaccharides. These substances are utilized during the early phase of histogenesis after germination of the gemmules. Apart from the presence of reserve bodies, the basic fine structure of metabolically inactive archaeocytes within the closed system of a gemmule is not fundamentally different from actively metabolizing cells of rapidly growing tissues. In particular, ribosomes, endoplasmic reticulum, mitochondria, Golgi bodies, and RNA-containing nucleoli are present during inactivity as well as after germination and resumption of growth and synthesis. Changes in cellular fine structure after germination include an increased density of the cytoplasmic ground substance, the appearance of small vesicles in the vicinity of the Golgi bodies and of annulate lamellae and a large, cylindrical centriole near the nuclear envelope. Two general conclusions are drawn from these results. Neither the ultra-structural aspect of a cell nor the presence of high concentrations of RNA in cytoplasm and nucleolus is a valid indication of cellular activity or inactivity. The persistence of Golgi bodies and endoplasmic reticulum through long periods of inactivity shows that their structural integrity is not dependent upon continuous energy input, although these intracellular membrane systems are undoubtedly dynamic structures in metabolically active cells.

Morphological and biochemical analyses of changes in rat hepatocytes related to wine and ethanol consumption

1984 ◽  
Vol 42 ◽  
pp. 232-233
Author(s):  
S.M. Geyer ◽  
C.L. Mendenhall ◽  
J.T. Hung ◽  
E.L. Cardell ◽  
R.L. Drake ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Endoplasmic Reticulum ◽  
Enzyme Activity ◽  
Malic Enzyme ◽  
Smooth Endoplasmic Reticulum ◽  
Rat Hepatocytes ◽  
Mature Male ◽  
Treatment Groups ◽  
Malic Enzyme Activity ◽  
Biochemical Analyses

Thirty-three mature male Holtzman rats were randomly placed in 3 treatment groups: Controls (C); Ethanolics (E); and Wine drinkers (W). The animals were fed synthetic diets (Lieber type) with ethanol or wine substituted isocalorically for carbohydrates in the diet of E and W groups, respectively. W received a volume of wine which provided the same gram quantity of alcohol consumed by E. The animals were sacrificed by decapitation after 6 weeks and the livers processed for quantitative triglycerides (T3), proteins, malic enzyme activity (MEA), light microscopy (LM) and electron microscopy (EM). Morphometric analysis of randomly selected LM and EM micrographs was performed to determine organellar changes in centrilobular (CV) and periportal (PV) regions of the liver. This analysis (Table 1) showed that hepatocytes from E were larger than those in C and W groups. Smooth endoplasmic reticulum decreased in E and increased in W compared to C values.

scholarly journals Effects of taurolithocholate, a Ca2+-mobilizing agent, on cell Ca2+ in rat hepatocytes, human platelets and neuroblastoma NG108-15 cell line

1991 ◽  
Vol 273 (1) ◽  
pp. 153-160 ◽  
Author(s):  
J F Coquil ◽  
B Berthon ◽  
N Chomiki ◽  
L Combettes ◽  
P Jourdon ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Bile Acid ◽  
Cell Line ◽  
Rat Liver ◽  
Neuronal Cell ◽  
Rat Hepatocytes ◽  
Cell Types ◽  
Liver Cells ◽  
Human Platelets ◽  
Rat Liver Cells

The monohydroxy bile acid taurolithocholate permeabilizes the endoplasmic reticulum to Ca2+ in rat liver cells. To assess whether this action on the endoplasmic reticulum was restricted to this tissue, the effects of bile acid were investigated in two cell types quite unrelated to rat hepatocyte, namely human platelets and neuronal NG108-15 cell line. The results showed that taurolithocholate (3-100 microM) had no effect on free cytosolic [Ca2+] in human platelets and NG108-15 cells. whereas it increased it from 180 to 520 nM in rat hepatocytes. In contrast, in cells permeabilized by saponin, taurolithocholate initiated a profound release of the stored Ca2+ from the internal Ca2+ pools in the three cell types. The bile acid released 90% of the Ca2+ pools, with rate constants of about 5 min-1 and half-maximal effects at 15-30 microM. The results also showed that, in contrast with liver cells, which displayed an influx of [14C]taurolithocholate of 2 nmol/min per mg, human platelets and the neuronal cell line appeared to be resistant to [14C]taurolithocholate uptake. The influx measured in these latter cells was about 100-fold lower than in rat liver cells. Taken together, these data suggest that human platelets and NG108-15 cells do not possess the transport system for concentrating monohydroxy bile acids into cells. However, they show that human platelets and neuronal NG108-15 possess, in common with liver cells, the intracellular system responsible for taurolithocholate-mediated Ca2+ release from internal stores.

A characterization of heam uptake and intracellular distribution by isolated hepatocytes

1985 ◽  
Vol 5 (7) ◽  
pp. 609-614 ◽  
Author(s):  
A. Lodola
Keyword(s):  
Endoplasmic Reticulum ◽  
Specific Binding ◽  
Isolated Hepatocytes ◽  
Intracellular Distribution ◽  
Distribution Data ◽  
Temperature Dependent ◽  
Rat Hepatocyte ◽  
Isolated Rat ◽  
Endoplasmic Reticulum Fraction

The uptake and intracellular distribution of haem by isolated rat hepatocyte suspensions was studied. An increase in cell haem content occurred after a challenge with 5, 10 or 20 μM haem, supplied as methaemalbumin. The rate of haem uptake was temperature dependent; no non-specific binding occurred. Intracellular haem distribution data are consistent with a rapid association of haem with the endoplasmic reticulum fraction prior to its accumulation in the cytosol and at the mitochondrion.

scholarly journals Prohibitin: A Novel Molecular Player in KDEL Receptor Signalling

2015 ◽  
Vol 2015 ◽  
pp. 1-13 ◽  
Author(s):  
Monica Giannotta ◽  
Giorgia Fragassi ◽  
Antonio Tamburro ◽  
Capone Vanessa ◽  
Alberto Luini ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Complex ◽  
Membrane Trafficking ◽  
Transmembrane Domain ◽  
Cell Cycle Control ◽  
Retrograde Transport ◽  
Multifunctional Protein ◽  
G Protein Coupled ◽  
Kdel Receptor ◽  
Prohibitin 1

The KDEL receptor (KDELR) is a seven-transmembrane-domain protein involved in retrograde transport of protein chaperones from the Golgi complex to the endoplasmic reticulum. Our recent findings have shown that the Golgi-localised KDELR acts as a functional G-protein-coupled receptor by binding to and activating Gs and Gq. These G proteins induce activation of PKA and Src and regulate retrograde and anterograde Golgi trafficking. Here we used an integrated coimmunoprecipitation and mass spectrometry approach to identify prohibitin-1 (PHB) as a KDELR interactor. PHB is a multifunctional protein that is involved in signal transduction, cell-cycle control, and stabilisation of mitochondrial proteins. We provide evidence that depletion of PHB induces intense membrane-trafficking activity at the ER–Golgi interface, as revealed by formation of GM130-positive Golgi tubules, and recruitment of p115,β-COP, and GBF1 to the Golgi complex. There is also massive recruitment of SEC31 to endoplasmic-reticulum exit sites. Furthermore, absence of PHB decreases the levels of the Golgi-localised KDELR, thus preventing KDELR-dependent activation of Golgi-Src and inhibiting Golgi-to-plasma-membrane transport of VSVG. We propose a model whereby in analogy to previous findings (e.g., the RAS-RAF signalling pathway), PHB can act as a signalling scaffold protein to assist in KDELR-dependent Src activation.

scholarly journals The Lamellar Systems of Cytoplasmic Membranes in Dividing Spermatogenic Cells of Drosophila virilis

1960 ◽  
Vol 7 (3) ◽  
pp. 433-441 ◽  
Author(s):  
Susumu Ito
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Complex ◽  
Light And Electron Microscopy ◽  
Primary Spermatocyte ◽  
Drosophila Virilis ◽  
Spermatogenic Cells ◽  
Membrane Systems ◽  
Cytoplasmic Membranes ◽  
Pas Reaction ◽  
Staining Methods

Spermatogenic cells of Drosophila virilis were studied by light and electron microscopy. The persistence of a "nuclear wall" during the meiotic divisions has been reported by a number of early cytologists, but this interpretation has been a subject of debate. Electron micrographs of dividing spermatocytes reveal the presence of multiple layers of paired membranes surrounding the nuclear region. These lamellar membrane systems are not typical of the nuclear envelope, but were interpreted as such by light microscopists. The membranes constituting a pair are separated by an interspace of ∼ 100 A and successive pairs are 200 to 400 A apart. These spacings are similar but not identical to those found in the lamellar systems of the Golgi complex. The cisternae of the endoplasmic reticulum in this material are devoid of attached ribonucleoprotein particles, are more precisely ordered than in vertebrate cells, and show a uniform, narrow intracisternal space of ∼ 100 A. The conspicuous asters appear to be made up of similar paired membranes radiating from the centriolar region. The primary spermatocyte has numerous dictyosomes and a well developed endoplasmic reticulum in cisternal form, but no typical Golgi complex or endoplasmic reticulum is found during the meiotic division stages of metaphase to telophase. Evidence is presented that these cytoplasmic organelles contribute to the formation of the extensive lamellar systems that appear during meiosis. The results of the Golgi silver staining methods and staining tests for phospholipids, basophilia, and the PAS reaction, indicate that the lamellar arrays of membranes present during meiosis are indistinguishable from the Golgi complex in their tinctorial properties.

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