ACID PHOSPHATASE ACTIVITY IN THE PANCREATIC ISLETS OF RATS OF DIFFERENT AGES

1962 ◽  
Vol 40 (4) ◽  
pp. 604-612 ◽  
Author(s):  
Claes Hellerström ◽  
Sven Brolin ◽  
Stig Larsson ◽  
Bo Hellman

ABSTRACT Histochemical methods for acid phosphatase and glucose-6-phosphatase were applied to the islets of Langerhans in rats of different ages. It was not possible to demonstrate any specific glucose-6-phosphatase activity, since at the pH optimum of this enzyme, both glucose-6-phosphate and sodium-β-glycerophosphate were hydrolyzed; the more intense reaction occurring with the latter substrate. At the end of the intrauterine life there was a marked acid phosphatase reaction, which appeared unchanged during the first 10 days of postnatal life but was considerably weaker in adult rats. The occurrence of a smaller number of non-reacting cells in the islet periphery was assumed to be evidence that there was no demonstrable acid phosphatase activity in one or both types of A cells. The considerable reaction found in the islets of foetuses and young rats might reflect the maturation and rapid proliferation of these cells during early stage of life.

1986 ◽  
Vol 64 (12) ◽  
pp. 2887-2895
Author(s):  
Louis Genevès ◽  
Jacques Rutin

Protein bodies were characterized at an early stage of their maturation in thin green cotyledons of developing radish embryos. They appeared as granules in the cytoplasm of meristematic cells. Their diameter (0.5 to 1 μm) was in the range of that of mitochondria. They were distinguished from vacuoles by their morphology, size, and structure. Some appeared to be associated with cisternae of endoplasmic reticulum or dictyosomes (permanganic fixations). Their evolution was synchronous in the cell and also in the cotyledonary tissue. Compact in appearance, they were constituted of thin packed fibrillar structures, limited by a denser peripheral layer. It is difficult to know whether or not they had a limiting membrane. Some possessed thin dense crystals or globoids (aldehydic fixations). During this early phase, several types of organelles seemed to contribute to the development of protein bodies, including saccules of rough endoplasmic reticulum and dictyosomes. Polyribosomes constituted a network around their surface. They did not exhibit any acid phosphatase activity. In this respect, they differed from the vacuoles, saccules of endoplasmic reticulum, and several neighbouring vesicles.


1964 ◽  
Vol 45 (3) ◽  
pp. 476-486 ◽  
Author(s):  
Claes Hellerström ◽  
Inge-Bert Täljedal ◽  
Bo Hellman

ABSTRACT Quantitative studies of non-specific acid phosphatases were performed on isolated pancreatic islets from obese-hyperglycaemic mice. The islets of these animals are composed of a rather pure population of B cells. The following observations were made: Acid phosphatases originating in the islet tissue, showed maximal enzyme activities at about pH 3.5 and 5.3 using p-nitrophenyl phosphate as substrate. The acid phosphatase activity of the exocrine tissue showed a single distinct maximum at about pH 5.3. The islet acid phosphatases were inhibited by sodium fluoride, sodium tartrate and formaldehyde. They were stable against storage in crude tissue homogenates at + 4° C and + 20° C for 48 hours. The pancreatic islets exhibited a significantly higher acid phosphatase activity than the exocrine parenchyma. Starvation for 7 days did not alter the enzyme levels in the islets or acini when measured at pH 5.3, while a probably increased enzyme activity was obtained in both these regions at pH 3.5. There was no evidence for a relationship between the insulin secretion and the acid phosphatase activity of the B cells.


1969 ◽  
Vol 22 (4) ◽  
pp. 1051 ◽  
Author(s):  
S-Y Zee

Acid phosphatase activity has been detected within the sieve-tube members of plants by many workers using the Gomori technique and light microscopy (Lester and Evert 1965; Flinn and Smith 1967). Unfortunately the limited resolution makes it difficult to determine the specific sites of activity of the reaction product of the enzyme; recent advances in histochemical techniques for electron microscopy have made it possible to investigate more specifically the sites of localization of the acid phosphatase reaction product by using the Gomori lead nitrate technique (Goldfischer, Essner, and Novikoff 1964; Catesson and Czanenski 1967; Bowen 1968; Figier 1968; Wardrop 1968).


1987 ◽  
Vol 65 (7) ◽  
pp. 626-634 ◽  
Author(s):  
Sherry A. Marts ◽  
George M. Padilla ◽  
Vladimir Petrow

6-Methylene progesterone (6MP) is an irreversible in vitro kcat inhibitor of rat prostate 5α-reductase, the enzyme which converts testosterone (T) to dihydrotestosterone (DHT). Treatment of adult rats with 6MP or diethylstilbestrol (DES) decreased the weight of the ventral prostate (VP) by 45%, while castration reduced it by 86%. Histologically, the 6MP-treated VP were indistinguishable from those of controls, while the VP from DES-treated rats showed fibrous stromal hypertrophy as in castrated rats. The prostatic hydroxyproline content, an index of collagen levels, was enhanced by castration or DES, but was not significantly increased by 6MP. Within 2 days of 6MP treatment, the 5α-reductase activity was reduced by 46% and ornithine decarboxylase (ODC) activity was lowered by 27%. During this time the prostatic acid phosphatase activity increased 42% and remained elevated with continued exposure to 6MP up to 13 days. The castration-induced involution of the VP was accompanied by a reduction in serum T and an increase in serum luteinizing hormone (LH). 6MP had no effect on T and LH serum levels but reduced the DHT content within the VP by 64%. Our results indicate that the structure and secretory acid phosphatase activity of the VP are less sensitive to changes in the ratio of T: DHT than is cell proliferation. Thus, the relative amounts of DHT and T within the VP may prove to be more significant than the absolute amount of either androgen in controlling prostate growth or its attendant neoplasms.


Author(s):  
O. T. Minick ◽  
E. Orfei ◽  
F. Volini ◽  
G. Kent

Hemolytic anemias were produced in rats by administering phenylhydrazine or anti-erythrocytic (rooster) serum, the latter having agglutinin and hemolysin titers exceeding 1:1000.Following administration of phenylhydrazine, the erythrocytes undergo oxidative damage and are removed from the circulation by the cells of the reticulo-endothelial system, predominantly by the spleen. With increasing dosage or if animals are splenectomized, the Kupffer cells become an important site of sequestration and are greatly hypertrophied. Whole red cells are the most common type engulfed; they are broken down in digestive vacuoles, as shown by the presence of acid phosphatase activity (Fig. 1). Heinz body material and membranes persist longer than native hemoglobin. With larger doses of phenylhydrazine, erythrocytes undergo intravascular fragmentation, and the particles phagocytized are now mainly red cell fragments of varying sizes (Fig. 2).


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