scholarly journals NONSPECIFIC ESTERASES IN RAT PROSTATIC EPITHELIAL CELLS

1967 ◽  
Vol 15 (10) ◽  
pp. 589-595 ◽  
Author(s):  
JAMES L. FROST ◽  
DAVID BRANDES
Keyword(s):  
Endoplasmic Reticulum ◽  
Acid Phosphatase ◽  
Epithelial Cells ◽  
Protective Effect ◽  
Ribonucleic Acid ◽  
Esterase Activity ◽  
Ribosomal Ribonucleic Acid ◽  
The Difference ◽  
Nonspecific Esterases

Prostates from normal and recently castrated rats were examined for the localization of esterase activity using Holt's indoxyl acetate method. Tissue fixed in formalin mixtures containing sucrose showed preservation of abundant cytoplasmic esterase activity while tissue fixed in formalin mixtures lacking sucrose had little cytoplasmic esterase activity. Esterase activity in droplets was abundant after both fixations. The difference could not be explained by ferroferricyanide inhibition, pH or osmolality of the fixative, and is attributed to a protective effect of sucrose during fixation. E600 greatly reduced cytoplasmic esterase activity in normal and castrated rats. Esterase activity in droplets was resistant to E600 in both normals and castrates. Ribonuclease extraction reduced cytoplasmic esterase activity in both normal and castrated rats only slightly, indicating no association of cytoplasmic esterases with ribosomal ribonucleic acid. Cytoplasmic esterase activity is reduced in castrates in which the epithelial cells of the prostate also show a decrease in endoplasmic reticulum and ribosomes. Similarity of location of droplet esterase activity and of lysosomes marked by acid phosphatase and reduction in droplet esterase activity by saline extraction are cited as evidence for a lysosomal localization of E600-resistant esterase.

scholarly journals Demonstration of lysosomal and extralysosomal sites for acid phosphatase in mouse kidney tubule cells with p-nitrophenylphosphate lead-salt technique.

1975 ◽  
Vol 23 (6) ◽  
pp. 439-451 ◽  
Author(s):  
H Miyayama ◽  
R Solomon ◽  
M Sasaki ◽  
C W Lin ◽  
W H Fishman
Keyword(s):  
Endoplasmic Reticulum ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Epithelial Cells ◽  
Normal Mouse ◽  
Plasma Membranes ◽  
Mouse Kidney ◽  
Lead Salt ◽  
Acetate Buffer ◽  
Electron Microscopic

Dual localization of acid phosphatase in lysosomal and extralysosomal sites of the tubule epithelial cells of normal mouse kidney was observed at the light and electron microscope level using a modified Gomori lead-salt method with p-nitrophenylphosphate (pNPP) as substrate. Based on previous biochemical and cytochemical findings, we developed optimal conditions for the enzyme activity in extralysosomal sites. The conditions used for the light microscopic level consisted of 1.5 mM PNPP, 2.0 MM Pb(NO3)2 and 0.05 M acetate buffer (pH 5.8). Those for the electron microscopic study required 3.0 mM PNPP, 3.6 MM Pb(NO3)2 and 0.1 M acetate buffer (pH 5.8). This modified lead-salt technique was highly specific and provided a suitable method for the demonstration of nonlysosomal as well as lysosomal sites of acid phosphatase activity in the tubule epithelial cells of normal mouse kidney. As expected, the enzyme activity appeared in the lysosomes, but the prominent reaction in the brush border, the rough endoplasmic reticulum and basal infolding plasma membranes was not anticipated. We were able to demonstrate in situ organelle precursors of microsomal acid phosphatase such as endoplasmic reticulum, plasma membrane and basal infolding membranes showing the same substrate preference, which had been observed previously in biochemical studies in our laboratory. Since the possible participation of alkaline phosphatases, K+-pNPPase or Na+-K+-adenosine triphosphatase was ruled out by use of appropriate inhibitors, the enzyme-reactive sites can be interpreted as reflecting nonspecific acid phosphatase.

Ultrastructural Changes Associated with Alcoholic Hyalin in Hepatocytes and Biliary Epithelial Cells

1971 ◽  
Vol 29 ◽  
pp. 572-573
Author(s):  
Odell T. Minick ◽  
Hidejiro Yokoo ◽  
Fawzia Batti
Keyword(s):  
Endoplasmic Reticulum ◽  
Epithelial Cells ◽  
Liver Biopsy ◽  
Alcoholic Hepatitis ◽  
Ultrastructural Changes ◽  
Main Mass ◽  
Biliary Epithelial Cells ◽  
Biopsy Specimens ◽  
Alcoholic Hyalin

To learn more of the nature and origin of alcoholic hyalin (AH), 15 liver biopsy specimens from patients with alcoholic hepatitis were studied in detail.AH was found not only in hepatocytes but also in ductular cells (Figs. 1 and 2), although in the latter location only rarely. The bulk of AH consisted of a randomly oriented network of closely packed filaments measuring about 150 Å in width. Bundles of filaments smaller in diameter (40-90 Å) were observed along the periphery of the main mass (Fig. 1), often surrounding it in a rim-like fashion. Fine filaments were also found close to the nucleus in both hepatocytes and biliary epithelial cells, the latter even though characteristic AH was not present (Figs. 3 and 4). Dispersed among the larger filaments were glycogen, RNA particles and profiles of endoplasmic reticulum. Dilated cisternae of endoplasmic reticulum were often conspicuous around the periphery of the AH mass. A limiting membrane was not observed.

Study of Thrombin-Coagulase

1967 ◽  
Vol 17 (03/04) ◽  
pp. 321-334 ◽  
Author(s):  
J. P Soulier ◽  
Odette Prou-Wartelle ◽  
Liliane Hallé ◽  
Keyword(s):  
Esterase Activity ◽  
Adsorption Chromatography ◽  
The Difference

SummaryThe preparation of thrombin-coagulase is described. The properties of thrombin-coagulase are compared with those of biothrombin: kinetics, thermostability, adsorption, chromatography, esterase activity, clotting activity, action on platelets and on factors V and VIII, susceptibility to inhibitors.Biothrombin and thrombin-coagulase are closely related but distinct. Both apparently derive from prothrombin. Prothrombin and coagulase combine to form a complex: thrombin-coagulase wherein both factors are necessary for its activity. Possible explanations for the difference between thrombin-coagulase and biothrombin are proposed.

Testicular Injury Attenuated by Rapamycin Through Induction of Autophagy and Inhibition of Endoplasmic Reticulum Stress in Streptozotocin- Induced Diabetic Rats

2019 ◽  
Vol 19 (5) ◽  
pp. 665-675 ◽  
Author(s):  
Wenjiao Shi ◽  
Zhixin Guo ◽  
Ruixia Yuan
Keyword(s):  
Oxidative Stress ◽  
Endoplasmic Reticulum ◽  
Endoplasmic Reticulum Stress ◽  
Protective Effect ◽  
Er Stress ◽  
B Cell Lymphoma ◽  
Diabetic Rats ◽  
Pathological Changes ◽  
Rapamycin Treatment ◽  
Related Proteins

Background and Objective: This study investigated whether rapamycin has a protective effect on the testis of diabetic rats by regulating autophagy, endoplasmic reticulum stress, and oxidative stress. Methods: Thirty male Sprague-Dawley rats were randomly divided into three groups: control, diabetic, and diabetic treated with rapamycin, which received gavage of rapamycin (2mg.kg-1.d-1) after induction of diabetes. Diabetic rats were induced by intraperitoneal injection of streptozotocin (STZ, 65mg.Kg-1). All rats were sacrificed at the termination after 8 weeks of rapamycin treatment. The testicular pathological changes were determined by hematoxylin and eosin staining. The protein or mRNA expression of autophagy-related proteins (Beclin1, microtubule-associated protein light chain 3 (LC3), p62), ER stress marked proteins (CCAAT/enhancer-binding protein (C/EBP) homologous protein (CHOP), caspase-12), oxidative stress-related proteins (p22phox, nuclear factor erythroid2-related factor 2 (Nrf2)) and apoptosis-related proteins (Bax, B cell lymphoma-2 (Bcl-2)) were assayed by western blot or real-time fluorescence quantitative PCR. Results: There were significant pathological changes in the testes of diabetic rats. The expression of Beclin1, LC3, Nrf2, Bcl-2 were significantly decreased and p62, CHOP, caspase12, p22phox, and Bax were notably increased in the testis of diabetic rats (P <0.05). However, rapamycin treatment for 8 weeks significantly reversed the above changes in the testis of diabetic rats (P <0.05). Conclusion: Rapamycin appears to produce a protective effect on the testes of diabetic rats by inducing the expression of autophagy and inhibiting the expression of ER-stress, oxidative stress, and apoptosis.

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