J Song, K S Bosch, W Tigchelaar, R J Van Den Munckhof, J P Schellens, C J Van Noorden, W M Frederiks
{"title":"用光镜和电子显微镜联合观察大鼠肝脏无固定冷冻切片中5′-核苷酸酶的活性。","authors":"J Song, K S Bosch, W Tigchelaar, R J Van Den Munckhof, J P Schellens, C J Van Noorden, W M Frederiks","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>In the present study a technique was developed to demonstrate 5'-nucleotidase activity in unfixed cryostat sections of rat liver at the light- and electron-microscope level using a semipermeable membrane. In order to retain the ultrastructure of the unfixed material as much as possible, incubations were also performed at 4 degrees C rather than at 37 degrees C. The optimized incubation medium contained 300 mM Tris-maleate buffer, pH 7.2, 5 mM adenosine monophosphate as substrate, 30 mM cerium chloride as capturing agent for liberated phosphate, 10 mM magnesium chloride as activator and 1.5% agar. At the light-microscope level, similar localizations of 5'-nucleotidase activity were obtained when incubations were performed at 37 degrees C and 4 degrees C. Enzyme activity was present mainly at bile canalicular membranes and at sinusoidal membranes of hepatocytes; total activity was higher in pericentral than in periportal areas. Cytophotometric analyses revealed that specific formation of final reaction product (FRP) (test minus control reaction) at 37 degrees C followed a hyperbolic curve with time. A linear relationship was found between specific amounts of FRP and section thickness up to 8 micrograms. 5'-Nucleotidase activity was about three-fold higher after incubation for 30 min at 37 degrees C than at 4 degrees C. At the electron-microscope level, it was demonstrated that the ultrastructure of rat liver was rather well-preserved after incubating unfixed cryostat sections attached to a semipermeable membrane and electron-dense FRP was found at bile canalicular and sinusoidal plasma membrane of hepatocytes. The most distinct changes in ultrastructure after incubation at 37 degrees C, in comparison with that at 4 degrees C, were the appearance of multi-lamellar structures at bile canaliculi at 37 degrees C. We conclude that the present method is valid for the demonstration of 5'-nucleotidase activity in unfixed cryostat sections of rat liver at both the light- and electron-microscope levels and that hypothermic incubations improve ultrastructural morphology substantially.</p>","PeriodicalId":22439,"journal":{"name":"The Histochemical Journal","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1995-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Demonstration of 5'-nucleotidase activity in unfixed cryostat sections of rat liver using a combined light- and electron-microscope procedure.\",\"authors\":\"J Song, K S Bosch, W Tigchelaar, R J Van Den Munckhof, J P Schellens, C J Van Noorden, W M Frederiks\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>In the present study a technique was developed to demonstrate 5'-nucleotidase activity in unfixed cryostat sections of rat liver at the light- and electron-microscope level using a semipermeable membrane. In order to retain the ultrastructure of the unfixed material as much as possible, incubations were also performed at 4 degrees C rather than at 37 degrees C. The optimized incubation medium contained 300 mM Tris-maleate buffer, pH 7.2, 5 mM adenosine monophosphate as substrate, 30 mM cerium chloride as capturing agent for liberated phosphate, 10 mM magnesium chloride as activator and 1.5% agar. At the light-microscope level, similar localizations of 5'-nucleotidase activity were obtained when incubations were performed at 37 degrees C and 4 degrees C. Enzyme activity was present mainly at bile canalicular membranes and at sinusoidal membranes of hepatocytes; total activity was higher in pericentral than in periportal areas. Cytophotometric analyses revealed that specific formation of final reaction product (FRP) (test minus control reaction) at 37 degrees C followed a hyperbolic curve with time. A linear relationship was found between specific amounts of FRP and section thickness up to 8 micrograms. 5'-Nucleotidase activity was about three-fold higher after incubation for 30 min at 37 degrees C than at 4 degrees C. At the electron-microscope level, it was demonstrated that the ultrastructure of rat liver was rather well-preserved after incubating unfixed cryostat sections attached to a semipermeable membrane and electron-dense FRP was found at bile canalicular and sinusoidal plasma membrane of hepatocytes. The most distinct changes in ultrastructure after incubation at 37 degrees C, in comparison with that at 4 degrees C, were the appearance of multi-lamellar structures at bile canaliculi at 37 degrees C. We conclude that the present method is valid for the demonstration of 5'-nucleotidase activity in unfixed cryostat sections of rat liver at both the light- and electron-microscope levels and that hypothermic incubations improve ultrastructural morphology substantially.</p>\",\"PeriodicalId\":22439,\"journal\":{\"name\":\"The Histochemical Journal\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1995-11-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"The Histochemical Journal\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"The Histochemical Journal","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Demonstration of 5'-nucleotidase activity in unfixed cryostat sections of rat liver using a combined light- and electron-microscope procedure.
In the present study a technique was developed to demonstrate 5'-nucleotidase activity in unfixed cryostat sections of rat liver at the light- and electron-microscope level using a semipermeable membrane. In order to retain the ultrastructure of the unfixed material as much as possible, incubations were also performed at 4 degrees C rather than at 37 degrees C. The optimized incubation medium contained 300 mM Tris-maleate buffer, pH 7.2, 5 mM adenosine monophosphate as substrate, 30 mM cerium chloride as capturing agent for liberated phosphate, 10 mM magnesium chloride as activator and 1.5% agar. At the light-microscope level, similar localizations of 5'-nucleotidase activity were obtained when incubations were performed at 37 degrees C and 4 degrees C. Enzyme activity was present mainly at bile canalicular membranes and at sinusoidal membranes of hepatocytes; total activity was higher in pericentral than in periportal areas. Cytophotometric analyses revealed that specific formation of final reaction product (FRP) (test minus control reaction) at 37 degrees C followed a hyperbolic curve with time. A linear relationship was found between specific amounts of FRP and section thickness up to 8 micrograms. 5'-Nucleotidase activity was about three-fold higher after incubation for 30 min at 37 degrees C than at 4 degrees C. At the electron-microscope level, it was demonstrated that the ultrastructure of rat liver was rather well-preserved after incubating unfixed cryostat sections attached to a semipermeable membrane and electron-dense FRP was found at bile canalicular and sinusoidal plasma membrane of hepatocytes. The most distinct changes in ultrastructure after incubation at 37 degrees C, in comparison with that at 4 degrees C, were the appearance of multi-lamellar structures at bile canaliculi at 37 degrees C. We conclude that the present method is valid for the demonstration of 5'-nucleotidase activity in unfixed cryostat sections of rat liver at both the light- and electron-microscope levels and that hypothermic incubations improve ultrastructural morphology substantially.