scholarly journals Cloning of an [alpha]-Amylase cDNA from Aleurone Tissue of Germinating Maize Seed

1994 ◽  
Vol 105 (2) ◽  
pp. 759-760 ◽  
Author(s):  
T. E. Young ◽  
D. A. DeMason ◽  
T. J. Close
Keyword(s):  
Alpha Amylase ◽  
Maize Seed ◽  
Aleurone Tissue

scholarly journals Gibberellic acid-stimulated α-amylase secretion and phospholipid metabolism in wheat aleurone tissue

1982 ◽  
Vol 208 (1) ◽  
pp. 93-100 ◽  
Author(s):  
R B Mirbahar ◽  
D L Laidman
Keyword(s):  
Gibberellic Acid ◽  
Phospholipid Metabolism ◽  
The Other ◽  
Alpha Amylase ◽  
Amylase Secretion ◽  
Pulse Labelling ◽  
Hormone Response ◽  
Animal Tissues ◽  
Endomembrane Flow ◽  
Aleurone Tissue

1. Turnovers of [14C]glycerol-labelled phospholipids in wheat aleurone tissue have been measured by using a pulse-decay technique. The most metabolically active phospholipids were phosphatidylcholine, phosphatidylinositol, phosphatidylethanolamine and phosphatidylglycerol. 2. Gibberellic acid action on the tissue led to breakdown of phosphatidylcholine and stimulated turnover of the other phosphatides concomitant with the secretion of alpha-amylase from the tissue. After pulse-labelling of the aleurone tissue with [14C]glycerol, radioactivity was lost from the phospholipids and appeared quantitatively in triacylglycerols, suggesting a stoichiometric metabolism of the former into the latter. Although 1,2-diacylglycerol is an expected intermediate in such a conversion, the patterns of radioactivity in diacylglycerols gave no indication of this. 3. Several aspects of the response of aleurone tissue to gibberellic acid resemble the responses of exocytotic animal tissues to external agonists. In particular, our results and previous reports in the literature suggest that endomembrane flow, exocytosis, phosphatidylinositol turnover and a requirement of Ca2+ for enzyme secretion are common to both plant and animal systems. Although considerable differences also exist between the two, the similarities are sufficient to warrant further consideration that plants and animals might have conserved a similar hormone response-secretion mechanism.

Immunohistochemical localization of alpha-amylase in barley aleurone cells

1976 ◽  
Vol 20 (1) ◽  
pp. 183-198
Author(s):  
R.L. Jones ◽  
R.F. Chen
Keyword(s):  
Cell Wall ◽  
Wall Layer ◽  
Immunohistochemical Localization ◽  
Alpha Amylase ◽  
Perinuclear Region ◽  
Nuclear Region ◽  
Aleurone Cells ◽  
Rabbit Igg ◽  
Barley Aleurone ◽  
Aleurone Tissue

Alpha-Amylase was localized in aleurone cells of barley using immunohistochemical methods. Anti-alpha-amylase antibody was produced by rabbits immunized with enzyme purified from malt diastase and Himalaya variety barley seeds. Immunoelectrophoresis showed that the antibodies to both antigens were immunologically similar, therefore, they were used interchangeably in the localization of alpha-amylase. Fluorescence of 8–10 mum sections of freeze-substituted and paraffin embedded, gibberellic acid (GA)-treated aleurone tissue incubated with rabbit anti-alpha-amylase IgG and rhodamine-conjugated goat-anti-rabbit IgG is localized in the cytoplasm, the nuclear region and the innermost portion of the cell wall. Cytoplasmic immunofluorescence is not associated with a specific organelle but rather is diffusely distributed. The fluorescence of the nuclear region, however, is intense and in thinner (4-5 mum) sections is associated not with the nucleoplasm but with the nuclear envelope and perinuclear region of the cytoplasm. Fluorescence of the cell wall is confined to the inner boundary of the wall corresponding to the resistant wall layer. The immunofluorescent properties of non-GA-treated cells are quantitatively different; fluorescence of these sections is low and diffuse and is particularly reduced in the nuclear region. Electron microscopy shows that GA-treatment results in the proliferation of endoplasmic reticulum (ER) in the perinuclear region of the cell. We suggest that the alpha-amylase localized by immunofluorescence in the perinuclear region of the cell is localized in this ER produced in response to GA treatment. Immunohistochemical localization of alpha-amylase in cells zonated by centrifugation also suggests that the enzyme is intimately associated with the perinuclear area.

Alpha-Amylase/Trypsin Inhibitors, novel activators of innate immunity in ex-vivo tissue explants

2013 ◽  
Vol 51 (08) ◽  
Author(s):  
V Zevallos ◽  
P Olinga ◽  
Y Junker ◽  
PB Tung ◽  
N Volz ◽  
...  
Keyword(s):  
Innate Immunity ◽  
Ex Vivo ◽  
Trypsin Inhibitors ◽  
Alpha Amylase ◽  
Tissue Explants ◽  
Ex Vivo Tissue
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