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Peanut lectin: a histochemical marker for phaeochromocytomas.
1Division of Pathology, School of Pathological Sciences, University of Newcastle upon Tyne, UK.
Virchows Archiv. A, Pathological Anatomy and Histopathology
|January 1, 1991
Summary
Neuroendocrine and adrenocortical tumors were analyzed for neuron-specific enolase (NSE), chromogranin, and synaptophysin. Peanut lectin (PNA) staining revealed masked binding sites in certain tumors after neuraminidase treatment, aiding in their characterization.
Area of Science:
- Endocrinology
- Oncology
- Histopathology
Background:
- Neuroendocrine tumors (NETs) and adrenocortical tumors (ACTs) require accurate diagnostic markers.
- Neuron-specific enolase (NSE), chromogranin, and synaptophysin are established markers for neuroendocrine differentiation.
- Peanut lectin (PNA) binding can identify specific cell surface glycans, potentially aiding in tumor subtyping.
Purpose of the Study:
- To investigate the expression of NSE, chromogranin, and synaptophysin in NETs and ACTs.
- To evaluate the utility of PNA staining, with and without neuraminidase pre-treatment, in characterizing these tumors.
- To compare PNA staining patterns with established neuroendocrine markers.
Main Methods:
- Immunohistochemistry was performed on 55 neuroendocrine tumors and 6 adrenocortical tumors.
- Staining for neuron-specific enolase (NSE), chromogranin, and synaptophysin was conducted.
- Peanut lectin (PNA) staining was employed using a streptavidin-biotin technique, with and without neuraminidase pre-incubation to reveal masked binding sites.
Main Results:
- NSE was expressed in most neuroendocrine tumors. Higher proportions of tumors showed positivity for chromogranin than synaptophysin.
- PNA staining was negative in phaeochromocytomas, medullary thyroid carcinomas, islet cell tumors, and paragangliomas, but became positive after neuraminidase treatment, indicating masked binding sites.
- Adrenocortical tumors and neuroblastomas were PNA-negative regardless of neuraminidase treatment. Carcinoid tumors showed PNA positivity only in tubular areas, unaffected by neuraminidase.
Conclusions:
- Neuraminidase-sensitive PNA binding can help differentiate certain neuroendocrine tumors by unmasking specific carbohydrate structures.
- Combined use of NSE, chromogranin, synaptophysin, and PNA staining offers a more comprehensive approach to classifying neuroendocrine and adrenocortical neoplasms.
- The differential PNA reactivity suggests distinct glycosylation patterns in various neuroendocrine tumor subtypes.