Organization of intracellular calcium regulatory proteins in the neuronal endoplasmic reticulum

1994 ◽  
Vol 52 ◽  
pp. 26-27
Author(s):  
Maryann E. Martone ◽  
Victoria M. Edelman ◽  
Saul A. Alba ◽  
Thomas J. Deerinck ◽  
Mark H. Ellisman
Keyword(s):  
Endoplasmic Reticulum ◽  
Intracellular Calcium ◽  
Dendritic Spines ◽  
Calcium Binding ◽  
Smooth Endoplasmic Reticulum ◽  
Membrane System ◽  
Regulatory Proteins ◽  
Purkinje Neurons ◽  
Storage Site ◽  
Ip3 Receptor

The smooth endoplasmic reticulum (SER) has been established as an intracellular calcium storage site in neurons. Although the SER appears to form a continuous membrane system within neurons, immunolocalization studies suggest that calcium regulatory proteins are not evenly distributed within the SER but are selectively concentrated or excluded from certain domains. The subcompartmenalization of the SER has been clearly demonstrated in Purkinje neurons where two proteins involved in the release of calcium from intracellular stores, the IP3 and ryanodine receptor, were differentially localized within dendrites. Both proteins were found associated with the SER in cell bodies and dendrites of chick Purkinje neurons but only labeling for the IP3 receptor was found within dendritic spines. A similar differential localization was described in Purkinje cell dendrites for the SER Ca++ATPase and calsequestrin, a lumenal calcium binding protein. The Ca++ATPase was found throughout dendrites and dendritic spines while calsequestrin was restricted to membranous profiles within the dendritic shaft.

scholarly journals Inositol 1,4,5 trisphosphate releases calcium from specialized sites within Limulus photoreceptors

1987 ◽  
Vol 104 (4) ◽  
pp. 933-937 ◽  
Author(s):  
R Payne ◽  
A Fein
Keyword(s):  
Endoplasmic Reticulum ◽  
Injection Site ◽  
Intracellular Calcium ◽  
Subcellular Distribution ◽  
Smooth Endoplasmic Reticulum ◽  
Image Intensifier ◽  
Photoreceptor Cells ◽  
Calcium Stores ◽  
Inositol 1,4,5 Trisphosphate ◽  
Probable Site

We have investigated the subcellular distribution and identity of inositol trisphosphate (InsP3)-sensitive calcium stores in living Limulus ventral photoreceptor cells, where light and InsP3 are known to raise intracellular calcium. We injected ventral photoreceptor cells with the photoprotein aequorin and viewed its luminescence with an image intensifier. InsP3 only elicited detectable aequorin luminescence when injected into the light-sensitive rhabdomeral (R)-lobe where aequorin luminescence induced by light was also confined. Calcium stores released by light and InsP3 are therefore localized to the R-lobe. Within the R-lobe, InsP3-induced aequorin luminescence was further confined around the injection site, due to rapid dilution and/or degradation of injected InsP3. Prominent cisternae of smooth endoplasmic reticulum are uniquely localized within the cell beneath the microvillar surface of the R-lobe (Calman, B., and S. Chamberlain, 1982, J. Gen. Physiol., 80:839-862). These cisternae are the probable site of InsP3 action.

scholarly journals Properties of membrane-bound bilirubin UDP-glucuronyltransferase in rough and smooth endoplasmic reticulum and in the nuclear envelope from rat liver

1989 ◽  
Vol 259 (3) ◽  
pp. 659-663 ◽  
Author(s):  
F Vanstapel ◽  
L Hammaker ◽  
K Pua ◽  
N Blanckaert
Keyword(s):  
Endoplasmic Reticulum ◽  
Nuclear Envelope ◽  
Rat Liver ◽  
Smooth Endoplasmic Reticulum ◽  
Membrane System ◽  
Permeability Barrier ◽  
Membrane Bound ◽  
Marker Studies ◽  
High Degree ◽  
Regulatory Properties

We examined regulatory properties of bilirubin UDP-glucuronyltransferase in sealed RER (rough endoplasmic reticulum)- and SER (smooth endoplasmic reticulum)-enriched microsomes (microsomal fractions), as well as in nuclear envelope from rat liver. Purity of membrane fractions was verified by electron microscopy and marker studies. Intactness of RER and SER vesicles was ascertained by a high degree of latency of the lumenal marker mannose-6-phosphatase. No major differences in the stimulation of UDP-glucuronyltransferase by detergent or by the presumed physiological activator, UDPGlcNAc, were observed between total microsomes and RER- or SER-enriched microsomes. Isolated nuclear envelopes were present as a partially disrupted membrane system, with approx. 50% loss of mannose-6-phosphatase latency. The nuclear transferase had lost its latency to a similar extent, and the enzyme failed to respond to UDPGlcNAc. Our results underscore the necessity to include data on the integrity of the membrane permeability barrier when reporting regulatory properties of UDP-glucuronyltransferase in different membrane preparations.

scholarly journals Myosin-Va transports the endoplasmic reticulum into the dendritic spines of Purkinje neurons

2010 ◽  
Vol 13 (1) ◽  
pp. 40-48 ◽  
Author(s):  
Wolfgang Wagner ◽  
Stephan D. Brenowitz ◽  
John A. Hammer
Keyword(s):  
Endoplasmic Reticulum ◽  
Dendritic Spines ◽  
Purkinje Neurons ◽  
Myosin Va

scholarly journals Biogenesis of peroxisomes: immunocytochemical investigation of peroxisomal membrane proteins in proliferating rat liver peroxisomes and in catalase-negative membrane loops.

1989 ◽  
Vol 108 (6) ◽  
pp. 2221-2231 ◽  
Author(s):  
E Baumgart ◽  
A Völkl ◽  
T Hashimoto ◽  
H D Fahimi
Keyword(s):  
Endoplasmic Reticulum ◽  
Membrane Proteins ◽  
Smooth Endoplasmic Reticulum ◽  
Gradient Centrifugation ◽  
Normal Liver ◽  
Membrane System ◽  
Peroxisomal Membrane ◽  
Lowicryl K4m ◽  
Membrane Reservoir ◽  
Liver Peroxisomes

Treatment of rats with a new hypocholesterolemic drug BM 15766 induces proliferation of peroxisomes in pericentral regions of the liver lobule with distinct alterations of the peroxisomal membrane (Baumgart, E., K. Stegmeier, F. H. Schmidt, and H. D. Fahimi. 1987. Lab. Invest. 56:554-564). We have used ultrastructural cytochemistry in conjunction with immunoblotting and immunoelectron microscopy to investigate the effects of this drug on peroxisomal membranes. Highly purified peroxisomal fractions were obtained by Metrizamide gradient centrifugation from control and treated rats. Immunoblots prepared from such peroxisomal fractions incubated with antibodies to 22-, 26-, and 70-kD peroxisomal membrane proteins revealed that the treatment with BM 15766 induced only the 70-kD protein. In sections of normal liver embedded in Lowicryl K4M, all three membrane proteins of peroxisomes could be localized by the postembedding technique. The strongest labeling was obtained with the 22-kD antibody followed by the 70-kD and 26-kD antibodies. In treated animals, double-membraned loops with negative catalase reaction in their lumen, resembling smooth endoplasmic reticulum segments as well as myelin-like figures, were noted in the proximity of some peroxisomes. Serial sectioning revealed that the loops seen at some distance from peroxisomes in the cytoplasm were always continuous with the peroxisomal membranes. The double-membraned loops were consistently negative for glucose-6-phosphatase, a marker for endoplasmic reticulum, but were distinctly labeled with antibodies to peroxisomal membrane proteins. Our observations indicate that these membranous structures are part of the peroxisomal membrane system. They could provide a membrane reservoir for the proliferation of peroxisomes and the expansion of this intracellular compartment.

Structure and function of the neuronal endomembrane system

1993 ◽  
Vol 51 ◽  
pp. 98-99
Author(s):  
Maryann E. Martone ◽  
Victoria M. Simpliciano ◽  
Ying Zhang ◽  
Thomas J. Deerinck ◽  
Mark H. Ellisman
Keyword(s):  
Intracellular Calcium ◽  
Calcium Release ◽  
Smooth Endoplasmic Reticulum ◽  
Ryanodine Receptors ◽  
Cell Types ◽  
Calcium Stores ◽  
Endomembrane System ◽  
Ip3 Receptor ◽  
And Function ◽  
Cerebellar Purkinje Neurons

Components of the endomembrane system in a variety of cell types appear to function in the storage and release of calcium similar to the muscle sarcoplasmic reticulum. Many proteins involved in intracellular calcium regulation in skeletal or smooth muscle, e.g. Ca++ ATPase, calsequestrin, the inositol l,4,5,trisphosphate (TP3) receptor and the ryanodine binding protein, are found in the nervous system where they are particularly abundant within the smooth endoplasmic reticulum (SER) of cerebellar Purkinje neurons. Immunolocalization studies suggest, however, that calcium regulatory proteins are not uniformly distributed within the SER but are concentrated in or excluded from certain domains. For example, the IP3 and ryanodine receptors, two distinct calcium channels which mediate calcium release by different ligands, are found associated with the SER in cell bodies and dendrites of chick cerebellum but only the IP3 receptor is found within dendritic spines. These results are consistent with evidence that cells may possess multiple intracellular calcium stores that are pharmacologically, spatially and perhaps physically distinct.

Complex envelope system. Membrane systems of plant cells

1974 ◽  
Vol 268 (891) ◽  
pp. 119-128 ◽  
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Smooth Endoplasmic Reticulum ◽  
Plant Cells ◽  
Membrane System ◽  
Cellulose Microfibrils ◽  
Membrane Systems ◽  
Complex Envelope ◽  
Pectic Substances ◽  
The Matrix

The membrane system is made up of the nuclear envelopes, rough and smooth endoplasmic reticulum, Golgi apparatus and plasmalemma. Interconnexions between the various parts of the system are shown and these probably represent a flow of membrane from the endoplasmic reticulum through the Golgi apparatus to the plasmalemma. Membrane fractions have been isolated from broken cells and their function in the synthesis of polysaccharides established. It has been shown that the matrix polysaccharides of the wall (pectic substances and hemicelluloses) are formed within the membranes and that the pattern of synthesis of these polymers changes during differentiation of the cells. Cellulose microfibrils are probably synthesized at the plasmalemma which is formed by incorporation of membrane bounded vesicles from the Golgi apparatus. Thus the assembly of the polymers takes place either when the membrane is within the cytoplasm or when it is incorporated as the plasmalemma of the cell.

Zoospore ultrastructure of Phlyctochytrium plurigibbosum (Chytridiales)

1979 ◽  
Vol 57 (1) ◽  
pp. 48-53 ◽  
Author(s):  
D. J. S. Barr ◽  
V. E. Hadland-Hartmann
Keyword(s):  
Endoplasmic Reticulum ◽  
Smooth Endoplasmic Reticulum ◽  
Anterior Part ◽  
Membrane System ◽  
Double Membrane

The zoospore of Phlyctochytrium plurigibbosum Barr is globular to amoeboid while swimming and posteriorly uniflagellate. Mitochondria are in the posterior and are petal-like in their arrangement. The nucleus and one or more lipid globules are in the centre to anterior part of the cell. Morphologically, microbodies are intimately associated with lipid globules and loosely associated with mitochondria. There is a conspicuous double membrane system of smooth endoplasmic reticulum, and free ribosomes are dispersed throughout the cytoplasm. Microtubules radiate into the zoospore body from the proximal face of the kinetosome.

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