Histochemical demonstration of acid phosphatase activity in terminal Schwann cells associated with Ruffini endings in the periodontal ligament of rat incisors

1993 ◽  
Vol 38 (7) ◽  
pp. 611-617 ◽  
Author(s):  
Takeyasu Maeda ◽  
Osamu Sato ◽  
Ichiro Kawahara ◽  
Yoshiro Takano
1959 ◽  
Vol 7 (1) ◽  
pp. 39-41 ◽  
Author(s):  
M. S. BURSTONE

High acid phosphatase activity was observed in osteoclasts of several species using a reproducible azo-dye technique. High activity of two distinct enzymes, acid and alkaline phosphatase, are associated with osteoclasts and osteoblasts respectivey. Althouth frozen-dried tissues are recommended for definitive studies, the enzyme techniques used give satisfactory results with cold acetone-fixed tissues. The most accurate localization of acid phosphatase in osteoclasts in controlled comparative studies is obtained with double-embedded frozen-dried undecalcified tissues in conjunction with naphthol AS-phosphates.


1973 ◽  
Vol 21 (1) ◽  
pp. 34-41 ◽  
Author(s):  
ELENA CITKOWITZ ◽  
ERIC HOLTZMAN

Bodies with the morphologic and cytochemical characteristics of peroxisomes have been identified in the satellite and Schwann cells of rat dorsal root ganglia. They are membrane-delimited, round or oval structures which contain a moderately electron-dense matrix but lack a crystalline core. On incubation of the tissue in a cytochemical medium for demonstration of peroxisomes, these bodies show heavy deposits of reaction product. The reaction is inhibited by heating the tissue or by incubation in the presence of aminotriazole or dichlorophenolindophenol. In tissue incubated for acid phosphatase activity the bodies are not reactive, although lysosomes show reaction product.


1986 ◽  
Vol 34 (10) ◽  
pp. 1317-1323 ◽  
Author(s):  
F P van de Wijngaert ◽  
E H Burger

Fixed, undecalcified mouse long bones were embedded in glycol methacrylate (GMA), sectioned, and incubated for acid phosphatase in the presence or absence of tartrate, to investigate the feasibility of tartrate-resistant acid phosphatase as a histochemical marker for osteoclast identification. Naphthol AS-BI phosphate was used as the substrate and hexazonium pararosanaline as coupler. Cytocentrifuge preparations of mouse, rat, and quail bone marrow or frozen and GMA sections of mouse splenic tissue were used as controls to specify acid phosphatase activity. After adequate fixation, acid phosphatase activity sensitive to tartrate inhibition (TS-AP) was demonstrated in macrophages from spleen, bone marrow, and loose connective tissue surrounding bone rudiments. Acid phosphatase activity resistant to tartrate inhibition (TR-AP), was detected in multi-nuclear osteoclasts and in some mononuclear cells from bone marrow and periosteum. In cytocentrifuge preparations and frozen sections of mouse spleen, TR-AP was demonstrated after simultaneous incubation with substrate and tartrate. In GMA sections, however, TR-AP could only be demonstrated after pre-incubation with tartrate before application of substrate. We suggest that histochemical demonstration of TR-AP versus TS-AP on GMA-embedded bone sections by means of a pre-incubation method can be used as an identification marker of (pre)osteoclasts. Plastic embedding is recommended for its excellent preservation of morphology and enzyme activity.


1966 ◽  
Vol 14 (2) ◽  
pp. 171-176 ◽  
Author(s):  
G. W. EVANS ◽  
CECILIA L. WHINNEY ◽  
K. C. TSOU

5-Iodoindoxyl phosphate has been found to be a useful indigogenic substrate in the histochemical demonstration of acid phosphatase activity. Its superiority to other indoxyl phosphates is apparently due to a rapid oxidation of 5-iodoindoxyl to 5,5'-diiodoindigo in the acid pH range. A redox system of ferri-ferrocyanide enhances the oxidation and improves the localization. This method can be applied to calcium-formol-fixed tissues or to fresh frozen sections, although fixed tissues yield better results. The method is not recommended for the demonstration of enzyme activity in lipid-rich tissues because of the complexing property of lipids with 5,5'-diiodoindigo that results in crystal formation. The distribution of acid phosphatase activity with this method is generally similar to that obtained using azo dye methods.


1965 ◽  
Vol 13 (6) ◽  
pp. 448-453 ◽  
Author(s):  
RICHARD C. GRAHAM ◽  
MORRIS J. KARNOVSKY

The histochemical demonstration of uricase activity in rat and guinea pig liver is described. The technique depends upon the generation of H2O2 during the uricase reaction. The liberated H2O2 participates in a coupled peroxidatic oxidation of 3-amino-9-ethylcarbazole, resulting in the deposition of an insoluble red oxidation product at the sites of uricase activity. This activity appeared as small, discrete red granules througout the cytoplasm of hepatic parenchymal cells of the rat and guinea pig. The distribution was clearly different from that of acid phosphatase activity in similar sections, which appeared typically pericanalicular. These results are consistent with other data indicating that uricase is associated with microbodies in the rat liver, and that microbodies and lysosomes are separate entities.


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