Ultrastructural localization of activity of phosphatases by low temperature incubation of unfixed cryostat sections

Histochemistry and Cell Biology
J Y SongW M Frederiks

Abstract

In the present study, we demonstrate the activity of several phosphatases ultrastructurally in long-term (up to 24 months) cold-stored (-80 degrees C) rat tissues. Phosphatase activity was histochemically studied with the use of unfixed cryostat sections in combination with low temperature (4 degrees C) incubation conditions in order to prevent inactivation of enzyme activity and to limit the loss of ultrastructure. 5'-Nucleotidase activity was observed at plasma membranes, mainly at bile canalicular membranes of hepatocytes in liver. Thiamine pyrophosphatase activity was detected not only in trans side cisternae but also in medial and cis side cisternae of Golgi complexes in the parotid gland. Glucose-6-phosphatase activity was localized in endoplasmic reticulum as well as at the outer membrane of the nuclear envelope. Acid phosphatase reaction product was found in lysosomes. Furthermore, the localization patterns of 5'-nucleotidase and thiamine pyrophosphatase activity were compared with those obtained after different fixation procedures such as immediate chemical fixation of tissues or fixation of tissues after freezing and thawing. The results showed similar localization patterns of these enzymes after the different pretrea...Continue Reading

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Citations

Feb 4, 2010·The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society·C J F Van Noorden
Sep 17, 2009·Journal of Microscopy·I M C VogelsC J F Van Noorden
Jan 5, 2002·The American Journal of Forensic Medicine and Pathology·K PsaroudakisM N Michalodimitrakis
May 2, 2020·Clinical Oral Investigations·Ketelin Juliane Dal PráAna Maria Pires Soubhia

Related Concepts

Acid Phosphatase
Metazoa
Melting
Glucosephosphatase
Liver
Lysosomes
Electron Microscopy
Nuclear Envelope
Parotid Gland
Thiamine Pyrophosphatase

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