人碳酸酐酶同工酶II在脑肿瘤中的免疫组织化学证明。

The Histochemical Journal Pub Date : 1995-12-01
A K Parkkila, R Herva, S Parkkila, H Rajaniemi
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引用次数: 0

摘要

碳酸酐酶(CA)是中枢神经系统(CNS)中一种功能重要的酶,它参与控制酸碱平衡并调节脑脊液(CSF)的产生。同工酶II (caii)是中枢神经系统中分布最广泛的CA,至少存在于髓磷脂、少突胶质细胞、星形胶质细胞和脉络膜丛中。本研究旨在检查31例不同脑肿瘤患者中CA II的存在。肿瘤标本免疫过氧化物酶染色采用识别CAⅱ的特异性抗体。以抗ca I、VI血清和正常兔血清为对照。所有星形细胞瘤(n = 9)、少突胶质细胞瘤(n = 3)和成神经管细胞瘤(n = 3)均可见CAⅱ阳性,其中以恶性肿瘤染色最强。此外,4例听神经瘤、1例丛状神经纤维瘤、1例脉络膜丛状乳头状瘤、1例室管膜母细胞瘤和1例室管膜下瘤表达该酶。脑膜瘤(n = 4)和神经元肿瘤(n = 4),包括小脑发育不良神经节细胞瘤(Lhermitte-Duclos),均为阴性。抗ca I、VI和正常兔血清在肿瘤细胞中未见特异性染色。Western blotting证实了CA II在星形细胞瘤中的存在,发现了一个与CA II对应的29 kDa多肽带。抗ca I血清显示出类似的单个29 kDa带,识别出红细胞中大量存在的酶。目前的结果表明,尽管细胞发生恶性转化,CA II在星形细胞瘤、少突胶质细胞瘤、室管膜和脉络膜丛肿瘤以及神经鞘细胞源性肿瘤中持续表达。我们的研究结果表明,一些肿瘤含有丰富的CA II,可能会渗漏到脑脊液中。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Immunohistochemical demonstration of human carbonic anhydrase isoenzyme II in brain tumours.

Carbonic anhydrase (CA) is a functionally important enzyme in the central nervous system (CNS), where it is involved in the control of the acid-base balance and regulates the production of cerebrospinal fluid (CSF). Isoenzyme II (CA II) is the most widely distributed CA in the CNS, being present in at least myelin, oligodendrocytes, astrocytes and the choroid plexus. This study was undertaken to examine the presence of CA II in different brain tumours from 31 patients. Specific antibodies recognizing CA II were used in immunoperoxidase staining of tumour specimens. Anti-CA I and VI sera and normal rabbit serum were used as controls. CA II-positive staining was observed in all the astrocytic tumours (n = 9), oligodendrogliomas (n = 3) and medulloblastomas (n = 3). The most malignant tumours exhibited the strongest staining. In addition, four acoustic neurinomas, one plexiform neurofibroma, one choroid plexus papilloma, one ependymoblastoma and one subependymoma expressed the enzyme. Meningiomas (n = 4) and neuronal tumours (n = 4), including one dysplastic gangliocytoma of the cerebellum (Lhermitte-Duclos), were negative. Anti-CA I, VI and normal rabbit sera showed no specific staining in tumour cells. The presence of CA II in the astrocytomas was confirmed by Western blotting, which revealed a distinct 29 kDa polypeptide band corresponding the CA II. Anti-CA I serum showed similarly a single 29 kDa band, recognizing the enzyme which is abundantly present in the erythrocytes. The present results demonstrate that despite the malignant transformation of the cells, the expression of CA II is sustained in astrocytic tumours, oligodendrogliomas, ependymal and choroid plexus tumours and tumours of nerve sheath cell origin. Our results suggest that some tumours contain abundant CA II, which might leak into the CSF.

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