myelin-basic-protein and Teratoma

myelin-basic-protein has been researched along with Teratoma* in 2 studies

Other Studies

2 other study(ies) available for myelin-basic-protein and Teratoma

ArticleYear
Human teratomas express differentiated neural antigens. An immunohistochemical study with anti-neurofilament, anti-glial filament, and anti-myelin basic protein monoclonal antibodies.
    The American journal of pathology, 1984, Volume: 115, Issue:3

    Monoclonal antibodies specific for neurofilament proteins, glial filament protein, or myelin basic protein were used with immunohistochemistry for evaluation of a series of 14 human benign and malignant teratomas for the presence of these neural specific antigens. The results indicate that human teratomas can express all of these neural antigens, reflecting the presence of differentiated neurons, astrocytes, and oligodendroglia, respectively. Although the tumors were selected because neural tissue had been noted on microscopic examination, 2 of the 15 cases lacked all of these neural antigens, and both were malignant teratomas. In the remaining cases, 2 or 3 of these neural antigens were detected. The presence of all 3 was correlated with the presence of mature, and the absence of immature, neural elements. The immunohistochemical detection of these antigens allows the confident recognition of neural elements in human teratomas, and their presence may be of prognostic significance.

    Topics: Adolescent; Adult; Antibodies, Monoclonal; Antigens, Neoplasm; Astrocytes; Epitopes; Female; Histocytochemistry; Humans; Intermediate Filament Proteins; Male; Myelin Basic Protein; Neurons; Oligodendroglia; Ovarian Neoplasms; Teratoma; Testicular Neoplasms

1984
Reactivity in the MEM-test of cancer patients' lymphocytes incubated with brain-derived preparations and extracts from malignant teratomas.
    Archiv fur Geschwulstforschung, 1981, Volume: 51, Issue:4

    A batch of human encephalitogenic protein (HEP) was compared to preparations of microtubulin and associated proteins (MST) from guinea pig brain by serological techniques and the macrophage electrophoretic mobility (MEM) method. HEP consisted mainly of A1 protein and MST showed the characteristic double band in the 55,000 MW region and some additional weak protein bands. No cross-reactivity could be detected between HEP and MST by rabbit hyperimmune sera to these substances. The MEM test, however, revealed human lymphocyte reactivity to HEP and MST in both cancer and multiple sclerosis patients, but no remarkable responses in other patients. A synthetic nonapeptide (114-122 region of A1 protein) led to lymphokine release in 2 of 5 multiple sclerosis patients, in 1 of 13 cancer patients, and in none out of 13 control individuals. From these findings it is concluded that a minor component (contaminant?) present in both HEP and MST might induce lymphocyte responses in cancer patients. The A1 protein of HEP preparations is, if at all, not the only protein responsible for the so-called HEP-response of cancer patients. Continuing the MEM test experiments with extracts from single organ cancers, it could be shown that patients with malignant teratomas respond to a more or less broad spectrum of extracts bearing organ cancer specificity. On the other side, extracts made from 2 malignant teratoma tissues led to MEM responses in 8 of 13 cancers, in 2 of 11 control persons and in none of 5 multiple sclerosis patients. These findings underline the concept that tumour-associated antigens (possibly oncofetal antigens) do exist, which bear organ cancer specificity and will lead to a specific sensitization of the host. Such antigens may be expressed in teratomas in different qualities and amounts depending on the tissue differentiation capacity of a given teratoma.

    Topics: Cross Reactions; Female; Humans; Immunologic Techniques; Lymphocytes; Macrophages; Male; Multiple Sclerosis; Myelin Basic Protein; Teratoma; Tubulin

1981