Distribution of activated caspase-3 in relation with apoptosis in human malignant gliomas

doi:10.1016/S0304-3940(01)01546-4

Neuroscience Letters

Volume 300, Issue 1, 2 March 2001, Pages 37-40

https://doi.org/10.1016/S0304-3940(01)01546-4 Get rights and content

Abstract

Activated caspase-3 has been immunohistochemically studied in 30 glioblastomas. Its distribution has been compared with that of apoptotic nuclei demonstrated by terminal dUTP nick-end labeling (TUNEL) and morphology. The best procedure for the demonstration of caspase-3 requires formalin fixation, followed by Carnoy fixation, with microwave irradiation. The number of positive cells is lower than that of apoptotic nuclei shown by TUNEL technique, especially in perinecrotic pseudo-palisadings, and there are also qualitative variations. Positive staining occurs in nuclei, cytoplasms or in both cell compartments. The interpretation of Caspase-3 positive staining is based on its crucial position in the final pathway to apoptosis and on the mechanisms by which it cleaves cytoplasmic and nuclear proteins among which inhibitory/caspase-activated DNase system is included.

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Acknowledgements

Suppported by AIRC (Milan) and MURST (Rome).

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Distribution of activated caspase-3 in relation with apoptosis in human malignant gliomas

Abstract

Section snippets

Acknowledgements

Cell

Trends Biochem. Sci.

Neurosci. Lett.

Immunohistochemical localization of caspase-3 correlates with clinical outcome in B-cell diffuse large-cell lymphoma

Cancer Res.

Reply to [10]

Lab. Invest.

The biochemistry of apoptosis

Nature

Immunohistochemical analysis of in vivo patterns of expression of CPP32 (caspase -3), a cell death protease

Cancer Res.

A study of apoptosis in normal and pathologic nervous system after in situ end-labeling of DNA strand breaks

J. Neuropathol. Exp. Neurol.

The two in situ techniques do not differentiate between apoptosis and necrosis but rather reveal distinct patterns of DNA fragmentation in apoptosis (Letter)

Lab. Invest.