The presence of alpha-1-antichymotrypsin, a serine proteinase inhibitor with a high affinity for cathepsin G , is demonstrated in the normal human central nervous system (CNS) by immunohistochemical techniques. Paraffin-embedded normal human CNS tissue from five adult, two fetal, one neonatal and th
Immunohistochemical demonstration of alpha-1-proteinase inhibitor in brain tumors
✍ Scribed by Mario Zuccarello; Raymond Sawaya; Mukunda B. Ray
- Publisher
- John Wiley and Sons
- Year
- 1987
- Tongue
- English
- Weight
- 965 KB
- Volume
- 60
- Category
- Article
- ISSN
- 0008-543X
No coin nor oath required. For personal study only.
✦ Synopsis
Using light microscopy and immunoperoxidase methods (PAP), the presence of alpha-1-proteinase inhibitor (API) was studied in seventeen brain tumors and four normal brain samples. The brain tumors included four glioblastomas, five low-grade gliomas, two metastatic lung carcinomas, two acoustic schwannomas, and four meningiomas. Normal brain displayed a finely granular intracytoplasmic staining confined to neuronal cells. Glial cells were negative for API. Fifteen of the 17 brain tumors were positive for API. Only two of five low-grade gliomas were negative for API. Glioblastoma and metastatic tumors exhibited the strongest positivity followed by acoustic neuroma, meningioma, and lowgrade glioma. All positive samples exhibited finely granular intracytoplasmic API, and 50% exhibited extracellular API positivity. Metastatic and glioblastoma tumors demonstrated prominent extracellular API staining. Our results support the concept of a local production of API by brain tumors.
Cancer 602304-809, 1987.
LPHA-I -PROTEINASE INHIBITOR (API), known pre-
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