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Variability of laminin immunoreactivity in human autopsy brain
S Mori1, N H Sternberger, M M Herman
1Department of Neurology, University of Maryland School of Medicine, Baltimore 21201.
Histochemistry
|January 1, 1992
Summary
Postmortem proteolysis unmasks laminin antigen in brain tissue, similar to enzymatic digestion. This unmasking can also occur through tissue damage during cryostat sectioning of fresh brain samples.
Area of Science:
- Neuroscience
- Immunohistochemistry
- Proteomics
Background:
- Laminin immunoreactivity is often masked in formalin-fixed brain sections.
- Proteolytic treatment is typically required to reveal laminin antigen in fixed tissues.
Purpose of the Study:
- To investigate the masking of laminin immunoreactivity in formalin-fixed brain sections.
- To analyze the effect of postmortem delay on laminin antigen unmasking.
- To compare antigen unmasking in human and rat brain tissues.
Main Methods:
- Analysis of frozen and formalin-fixed human autopsy brains at various postmortem intervals.
- Examination of unfixed frozen sections and formalin-fixed vibratome sections.
- Investigation of rat brains processed with and without postmortem delay.
Main Results:
- Intense laminin immunoreactivity was observed in unfixed frozen sections of both human and rat brains.
- Formalin fixation did not diminish immunoreactivity in unfixed sections.
- In fixed vibratome sections, immunoreactivity varied with postmortem delay and was enhanced by tissue damage.
Conclusions:
- Postmortem proteolysis effectively unmasks laminin antigen, mimicking enzymatic digestion.
- Tissue damage during cryostat sectioning can also induce laminin antigen unmasking.
- Understanding these processes is crucial for accurate immunohistochemical analysis of laminin in brain tissue.
