BACKGROUND: The hydrolysis enzymes of the acetylcholine, acetylcholinesterase, and butyrylcholinesterase are involved in non-cholinergic functions such as proliferation processes and cellular adhesion. These enzymes have been found in several tumors other from brain tumors. METHODS: Thirty fresh brain tumor specimens were obtained from biopsies taken during neurosurgical procedures. The specimens were cut in two parts, one designated for routine histopathological control and the other for histochemical and growth studies. The formalin fixed specimens were serially cut at 10 microm in a freezing cryostat, mounted in gelatin-coated slides, and processed for sensitive histochemical detection of acetylcholinesterase and butyrylcholinesterase. The other specimens were processed for a HMEM cell growth culture. RESULTS: The results show the coexistence of acetylcholinesterase and butyrylcholinesterase in all tumors studied. Type II and III gliomas and oligodendrogliomas show moderate activity of both cholinesterases, whereas in type IV glioma and meningiomas the labeling of both cholinesterases was high. In the craniopharyngiomas a high acetylcholinesterase activity was observed and low level of butyrylcholinesterase labeling. The cell growth was high only in the cases in which butyrylcholinesterase activity was high, such as type IV glioma. In type II and III gliomas, oligodendroglioma, and craniopharyngioma the growth rate was slow. CONCLUSIONS: These results could indicate a possible relationship between the presence of butyrylcholinesterase and acetylcholinesterase in brain tumor tissue and cellular proliferation in tumorigenesis.
BACKGROUND: The hydrolysis enzymes of the acetylcholine, acetylcholinesterase, and butyrylcholinesterase are involved in non-cholinergic functions such as proliferation processes and cellular adhesion. These enzymes have been found in several tumors other from brain tumors. METHODS: Thirty fresh brain tumor specimens were obtained from biopsies taken during neurosurgical procedures. The specimens were cut in two parts, one designated for routine histopathological control and the other for histochemical and growth studies. The formalin fixed specimens were serially cut at 10 microm in a freezing cryostat, mounted in gelatin-coated slides, and processed for sensitive histochemical detection of acetylcholinesterase and butyrylcholinesterase. The other specimens were processed for a HMEM cell growth culture. RESULTS: The results show the coexistence of acetylcholinesterase and butyrylcholinesterase in all tumors studied. Type II and III gliomas and oligodendrogliomas show moderate activity of both cholinesterases, whereas in type IV glioma and meningiomas the labeling of both cholinesterases was high. In the craniopharyngiomas a high acetylcholinesterase activity was observed and low level of butyrylcholinesterase labeling. The cell growth was high only in the cases in which butyrylcholinesterase activity was high, such as type IV glioma. In type II and III gliomas, oligodendroglioma, and craniopharyngioma the growth rate was slow. CONCLUSIONS: These results could indicate a possible relationship between the presence of butyrylcholinesterase and acetylcholinesterase in brain tumor tissue and cellular proliferation in tumorigenesis.
Authors: Elżbieta Studzińska-Sroka; Aleksandra Majchrzak-Celińska; Przemysław Zalewski; Dominik Szwajgier; Ewa Baranowska-Wójcik; Barbara Kaproń; Tomasz Plech; Marcin Żarowski; Judyta Cielecka-Piontek Journal: Pharmaceuticals (Basel) Date: 2021-12-10