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  • 1985-1989  (2)
  • 1986  (2)
  • Gibberellin and enzyme secretion  (1)
  • thromboxane sensitivity  (1)
Material
Years
  • 1985-1989  (2)
Year
  • 1986  (2)
  • 1
    ISSN: 1432-0428
    Keywords: Platelets ; thromboxane sensitivity ; cAMP ; proliferative retinopathy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Platelet aggregation to collagen in 12 Type 1 (insulin-dependent) diabetic patients with background retinopathy and 12 Type 1 diabetic patients with proliferative retinopathy was compared with an age- and sex-matched control group. An analogue of prostaglandin H2, 11,9 epoxymethano-prostaglandin H2, which directly stimulates thromboxane receptors, and EP 092, which is a competitive thromboxane A2 receptor antagonist, were used to investigate changes at platelet thromboxane receptor level in these groups. The concentration of collagen (EC50) required to give 50% of maximum aggregation did not differ between the two diabetic groups and the control group. However, platelets from the proliferative retinopathy group were significantly more sensitive to the thromboxane mimetic (11,9 epoxymethano-prostaglandin H2) (p 〈 0.005) than the background retinopathy and control groups. This change may be a factor in the development of proliferative retinopathy.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-2048
    Keywords: Aleurone (enzyme secretion) ; α-Amylase ; Gibberellin and enzyme secretion ; Hordeum (enzymes) ; Monensin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The effect of monensin on the secretion of α-amylase and other enzymes from the aleurone layer of barley (Hordeum vulgare L. cv. Himalaya) was studied by electrophoresis followed by fluorography and by pulse-chase and organelle-isolation experiments. Monensin markedly inhibits the secretion, but not the synthesis, of α-amylase, acid phosphatase, and at least four other proteins from the aleurone layer. Monensin treatment causes α-amylase to accumulate within the protoplast, but its effect on the different α-amylase isoenzymes is not equal. The accumulation of isoenzyme 2 is not influenced by monensin while isoenzymes 1, 3 and 4 are not secreted but rather accumulate in the cell when monensin is included in the incubation medium. The α-amylase and acid-phosphatase activities which accumulate within the aleurone cells following treatment with monensin are localized in an organelle having a buoyant density greater than that of endoplasmic reticulum and less than that of mitochondria. In pulse-chase experiments with [35S]methionine, labelled proteins accumulate in this organelle in the presence of monensin and do not appear in the incubation medium. We conclude that monensin inhibits the secretion of proteins from the barley aleurone layer by influencing their intracellular transport.
    Type of Medium: Electronic Resource
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