Immunocytochemical localization of reserve protein in the endoplasmic reticulum of developing bean (Phaseolus vulgaris) cotyledons

Planta ◽  
1980 ◽  
Vol 150 (5) ◽  
pp. 419-425 ◽  
Author(s):  
Bruno Baumgartner ◽  
K. T. Tokuyasu ◽  
Maarten J. Chrispeels
Keyword(s):  
Endoplasmic Reticulum ◽  
Phaseolus Vulgaris ◽  
Immunocytochemical Localization ◽  
Reserve Protein

Immunocytochemical localization of wheat prolamins in the lumen of the rough endoplasmic reticulum

1991 ◽  
Vol 69 (11) ◽  
pp. 2574-2577 ◽  
Author(s):  
Hari B. Krishnan ◽  
Jerry A. White ◽  
Steven G. Pueppke
Keyword(s):  
Triticum Aestivum ◽  
Endoplasmic Reticulum ◽  
Key Words ◽  
Rough Endoplasmic Reticulum ◽  
Protein A ◽  
Triticum Aestivum L ◽  
Soluble Proteins ◽  
Immunocytochemical Localization ◽  
Specific Antibodies ◽  
Days After Anthesis

Antibodies raised against gliadins, the alcohol-soluble proteins of wheat (Triticum aestivum L.) seeds, were used to localize gliadins within the lumen of the endoplasmic reticulum. Endosperm cells at 20 days after anthesis contain extensive rough endoplasmic reticulum that is fragmented and dilated. The dilated endoplasmic reticulum encloses aggregates of proteinaceous material that reacts strongly with gliadin-specific antibodies. Key words: gliadins, immunocytochemistry, protein A – gold, rough endoplasmic reticulum, wheat.

scholarly journals Laminin in cultured mouse C1300 neuroblastoma cells: immunocytochemical localization by pre- and postembedding electron microscope procedures.

1983 ◽  
Vol 31 (6) ◽  
pp. 755-764 ◽  
Author(s):  
P Liesi
Keyword(s):  
Electron Microscopy ◽  
Endoplasmic Reticulum ◽  
Electron Microscope ◽  
Plasma Membranes ◽  
Neuroblastoma Cells ◽  
Immunocytochemical Localization ◽  
Adhesion Protein ◽  
Antibody Method ◽  
Ultrathin Sections ◽  
Intercellular Connections

Laminin was localized in cultured mouse C1300 neuroblastoma cells by applying the peroxidase-antiperoxidase technique in preembedding electron microscopy. The results were compared to those obtained by indirect immunofluorescence and by the colloidal gold second antibody method on Epon-embedded ultrathin sections. Laminin was found in the cell membranes and within the rough endoplasmic reticulum as well as in intracytoplasmic vacuoles. Plasma membranes of the neuroblastoma cells showed a patchy localization of laminin that was apparently involved in cell-to-substrate attachment and in gap junction-like intercellular connections. Under normal conditions, the Golgi cisternae contained no laminin. Pretreatment of cells with micromolar concentrations of monensin, however, lead to an accumulation of laminin within the Golgi cisternae. These results support a role for laminin as an adhesion protein in cultured neuroblastoma cells and indicate that laminin is transported through the Golgi complex.

Seed reserve-protein glycosylation in an in vitro preparation from developing cotyledons of Phaseolus vulgaris

Planta ◽  
1979 ◽  
Vol 146 (4) ◽  
pp. 513-520 ◽  
Author(s):  
H. Maelor Davies ◽  
Deborah P. Delmer
Keyword(s):  
Phaseolus Vulgaris ◽  
Protein Glycosylation ◽  
Reserve Protein

scholarly journals Immunocytochemical localization of procollagen and fibronectin in human fibroblasts: effects of the monovalent ionophore, monensin.

1980 ◽  
Vol 87 (3) ◽  
pp. 663-671 ◽  
Author(s):  
P W Ledger ◽  
N Uchida ◽  
M L Tanzer
Keyword(s):  
Endoplasmic Reticulum ◽  
Rough Endoplasmic Reticulum ◽  
Immunofluorescence Microscopy ◽  
Human Fibroblasts ◽  
Subsequent Development ◽  
Immunocytochemical Localization ◽  
Intracellular Accumulation ◽  
Golgi Compartment ◽  
Golgi Zone ◽  
Ionophore Monensin

The monovalent ionophore monensin inhibits the secretion of both procollagen and fibronectin from human fibroblasts in culture. The distribution of these proteins in control and inhibited (5 x 10(-7) M monensin) cells has been studied by immunofluorescence microscopy. In control cells, both antigens are present throughout the cytoplasm and in specific deposits in a region adjacent to the nucleus, which we identify as a Golgi zone by electron microscopy. Treatment of cells with monensin causes intracellular accumulation of procollagen and fibronectin, initially in the juxta-nuclear region and also subsequently in peripheral regions. Electron microscope studies reveal that in such cells the juxta-nuclear Golgi zone becomes filled with a new population of smooth-membraned vacuoles and that normal Golgi complexes are not found. Immunocytochemically detected procollagen and fibronectin are localized in the region of these vacuoles, whereas more peripheral deposits correspond to the dilated cisternae of rough endoplasmic reticulum, which are also caused by monensin. Procollagen and fibronectin are often codistributed in these peripheral deposits. Accumulation of exportable proteins in Golgi-related vacuoles is consistent with previous analyses of the monensin effect. The subsequent development of dilated rough endoplasmic reticulum also containing accumulated proteins may indicate that there is an additional blockade at the exit from the endoplasmic reticulum, or that the synthesized proteins exceed the capacity of the Golgi compartment and that their accumulation extends into the endoplasmic reticulum.

Immunocytochemical localization of ingested kidney bean (Phaseolus vulgaris) lectins in rat gut

1980 ◽  
Vol 12 (2) ◽  
pp. 201-208 ◽  
Author(s):  
T. P. King ◽  
A. Pusztai ◽  
E. M. W. Clarke
Keyword(s):  
Phaseolus Vulgaris ◽  
Kidney Bean ◽  
Immunocytochemical Localization ◽  
Rat Gut
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