Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0025202 (melanoma)
 69,561 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The peroxidase-antiperoxidase staining technique for the antigens S-100, neuron-specific enolase, and alpha 1-antichymotrypsin (alpha 1ACT) was applied to 57 intraocular tumors: 46 malignant melanomas of the uvea, seven retinoblastomas, and four tumors metastasizing to the eye. The staining characteristics of the different intraocular tumors were compared. Staining for S-100 in a fine-needle aspiration biopsy sample taken from a malignant melanoma of the choroid before enucleation of the globe was attempted. The positive staining of a few cells thus obtained suggested that this technique may be helpful in the diagnosis of melanomas. The alpha 1ACT stain used in this study has not been used previously in ophthalmology to our knowledge. We found 60% of malignant melanomas of the choroid stained positively. Another finding was the staining of the retinal pigment epithelium with alpha 1ACT in 30% of eyes with malignant melanoma of the uvea.
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PMID:Immunohistochemical staining techniques of intraocular tumors. 147 23

A reproducible and sensitive one-step enzyme immunoassay (EIA) was developed to determine total tissue-type plasminogen activator (t-PA) antigen in plasma. The EIA comprises two monoclonal catching antibodies and a polyclonal (goat) tagging antibody conjugated with horseradish peroxidase. There is an equal reactivity towards the several physiological t-PA forms, i.e., single-chain t-PA, two-chain t-PA and t-PA in complex with its naturally occurring inhibitor plasminogen activator inhibitor-type 1 (t-PA/PAI-1 complex). Additionally, the EIA does not discriminate between human melanoma t-PA and recombinant t-PA (Activase). The assay has a lower detection limit of approximately 0.5 ng t-PA per ml plasma, with a time-to-result of only 3.5 h.
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PMID:A one-step enzyme immunoassay for the determination of total tissue-type plasminogen activator (t-PA) antigen in plasma. 164 8

We examined the influence of different staining techniques [(three-step immunoperoxidase technique (IP); alkaline phosphatase-anti-alkaline phosphatase technique (APAAP)] on the quantitative evaluation of Ki-67-labeled nuclei. We studied five melanocytic skin tumors. From each case, five parallel sections were prepared and stained using the peroxidase-antiperoxidase (PAP) technique (slide 1) and the APAAP technique once (slide 2). Slide 3 consisted of a single repetition of the APAAP technique, slide 4 was a double repetition, and slide 5 was a third repetition. We assessed the volume fraction (VV) of Ki-67-positive nuclei using computer-assisted image analysis. For each staining group, the mean value and standard deviation of VV were calculated. Comparing VV values obtained from the different staining groups we did not find a statistically significant difference between the IP and the various APAAP steps (Wilcoxon test, p = less than 0.05). However, the staining procedure influenced the quantitative results to some extent. The mean VV of the five staining groups ranged in our study from 0.10 to 0.17%, which is narrow compared with the overall variability among different cases (dermal melanocytic nevus, 0.01%; metastatic malignant melanoma, 0.43%). Therefore, we can state that for a rough evaluation of Ki-67-positive nuclei, the influence of different staining methods is negligible; for a subtle quantitative analysis, however, it would nevertheless be preferable to always apply the same staining technique.
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PMID:The influence of staining procedures on the assessment of cell proliferation as defined by the monoclonal antibody Ki-67. 170 Aug 83

To compare the time course of in vitro expression of various proliferation-associated markers including Ki-67 antigen, transferrin receptors (TfR), and DNA polymerase alpha, six human tumour cell lines of different histological origin were studied under defined conditions. Proliferation markers were demonstrated by peroxidase/anti-peroxidase staining using specific monoclonal antibodies, and their expression was compared to results obtained from [3H]-thymidine incorporation assays and cell counting. Expression of all proliferation markers began to increase during the lag phase, and occurred earlier than elevations of [3H]dT incorporation and cell numbers were recorded. Maximum expression was observed before cell growth reached plateau phase. The time courses of expression of DNA polymerase and Ki-67 were almost identical. The closest correlation of [3H]dT incorporation with time course of expression of proliferation-associated markers was observed, when intranuclear staining of DNA polymerase was analysed. TfR were expressed earlier than the polymerase and Ki-67. Since TfR were also found at remarkable levels in resting cells, they seem less proliferation-specific than Ki-67 and DNA polymerase. While in rapidly growing cell lines more than 95% of the cells expressed Ki-67, TfR, and more than 75% DNA polymerase in cell nuclei, a malignant melanoma and a pleural mesothelioma line displayed fewer than 35% of cells stained for DNA polymerase in cell nuclei during log phase. Determination of growth fractions by monoclonal antibodies may thus contribute to the prediction of chemoresistance by identifying quiescent cells that are not sensitive to S-phase-specific drugs.
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PMID:Expression of the proliferation-associated Ki-67 antigen of transferrin receptors and of DNA polymerase alpha in human tumour lines: implications for in vitro chemoresistance. 173 31

A monoclonal antibody (Ki-M6) against the CD 68 antigen, which labels cells of the monocyte/macrophage system, was tested on Bouin-fixed, paraffin-embedded samples of normal, reactive and neoplastic tissues by an avidin-biotin-peroxidase complex method, with the aim of establishing its value in diagnostic pathology. In normal human tissues, Ki-M6 reactivity was confined to the so-called resident macrophages populating normal organs under physiological conditions. Moreover, restricted reactivity against cells of macrophage lineage was observed in reactive and inflammatory lesions. Granulocytes, monocyte/macrophage-related immune accessory cells, and other analysed normal tissue structures did not reveal any reactivity. Ki-M6 was strongly reactive with the cases of benign (4/4) and malignant (15/15) fibrous histiocytomas, in addition to the true histiocytic lymphomas (3/3). Cases of granular cell tumour (2/3) showed strong reactivity with Ki-M6, whereas only few immunoreactive cells, with weak staining, were seen in the other Ki-M6-positive neoplasms [neurofibroma (3/3), benign schwannoma (1/2), ganglioneuroma (1/1), malignant schwannoma (5/9), melanoma (9/28), dermatofibrosarcoma protuberans (1/1), myelomonocytic leukaemia (3/3)]. Among the epithelial malignancies tested (47 cases), Ki-M6 was positive only in renal cell carcinoma (11/14). Malignant lymphomas of the Hodgkin (56 cases) and non-Hodgkin type (67 cases) were uniformly non-reactive. From these data, Ki-M6 appears to be an excellent marker of monocyte/macrophage-related cells and appears to be a reliable indicator for fibrous histiocytomas and true histiocytic malignancies. The availability of this additional antibody capable of staining routinely processed tissue is of practical interest.
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PMID:Immunohistochemical characterization of Ki-M6 monoclonal antibody in Bouin-fixed, paraffin-embedded sections of normal and neoplastic human tissues. 185 Aug 96

A mouse monoclonal antibody, FKH1, was produced to detect cytoplasmic melanoma-associated antigen. FKH1 was raised using cultured human melanoma cell line KHm-6 as immunogen. Reactivity of this antibody was assessed by immunohistochemical techniques. Positive reactions were seen against 5 human melanoma cell lines and cultured human epidermal melanocyte. It stained cytoplasm of melanoma cells in a diffuse and granular pattern with indirect immunofluorescence. Immunoelectron microscopy showed diffuse distribution of immuno-reactant in the cytoplasm of KHm-1 cells excluding melanosomes and other subcellular organelles. In immunoblotting, FKH1 bound with proteins having molecular weight of 71 kd and 55 kd extracted from KHm-6 cells. Reactivity against frozen and alcohol-fixed paraffin-embedded melanocytic tumors was also tested with indirect immunofluorescence or ABC (avidin biotin peroxidase complex) techniques. All cases of frozen sections from benign and malignant melanocytic tumors including 2 cases of amelanotic melanoma showed positive staining with FKH1. In fixed tissues, reactivity was 16/19 (84.2%) in malignant melanoma and 30/44 (68.2%) in other melanocytic tumors. FKH1 did not react against normal melanocytes, C-type nevus cell, intradermal nevus pigmentosus with neuroid structure and neurofibroma. It was demonstrated that FKH1 recognized proliferative melanocytes originated from melanoblast or melanoblastic nevoblast. FKH1 failed to stain normal human peripheral nerves and nonmelanocytic tumors except APUDoma and malignant Merkel cell tumor. In halo nevus, nevus cells were clearly distinguished from intermingling inflammatory cell infiltrate. It was suggested that FKH1 is a useful monoclonal antibody in diagnosing human malignant melanoma, particularly in evaluating tumor thickness of Breslow more precisely.
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PMID:[Mouse monoclonal antibody (FKH1) detecting human melanoma-associated antigens: production, partial characterization and immunohistochemical analysis]. 188 56

In 353 sera (from healthy donors as well as patients suffering from rheumatoid arthritis, systemic lupus erythematosus, hepatitis, malignant melanoma) circulating immune complexes were determined by C1q-binding test and a C1q solid-phase ELISA. Using peroxidase-labelled antibodies (from rabbit) against human mu-, gamma-, and alpha-heavy chains, the immunoglobulin classes in the complexes were determined. In rheumatoid arthritis, immune complexes contain IgM more frequently (41.5%) than in systemic lupus erythematosus (10%). Immune complexes containing only IgA as immunoglobulin were found in 24 cases. Our results including binding experiments with chemically aggregated IgA suggest, that the binding of C1q to IgA is not necessarily followed by classical complement activation.
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PMID:[Determination of circulating immune complexes and of their component immunoglobulin classes M, G, and A with a C1q-ELISA]. 206 29

IFN-alpha and IFN-gamma were found to enhance monocyte-mediated activity by acting on both tumor cells and monocytes. The addition of IFN-alpha or IFN-gamma enhanced the monocyte-mediated cytotoxicity of the human melanoma cell line, A375, as well as the human colon carcinoma cell line, HT-29. However, IFN-alpha generally induced more monocyte-mediated lysis of the A375 cells, whereas IFN-gamma induced more monocyte-mediated lysis of the HT-29 cells. These differences are, in part, due to the direct effects of the IFN on the tumor cells. Pretreatment of A375 cells with either IFN-alpha or IFN-gamma significantly enhanced their susceptibility to lysis by untreated monocytes. However, only IFN-gamma pretreatment of HT-29 cells enhanced the lysis of these cells by untreated monocytes. Differences were also observed in the activation of monocytes by IFN-alpha vs IFN-gamma with respect to their ability to induce soluble cytotoxic factors. We found that the addition of IFN-gamma and tumor cells (either the A375 or HT-29 cells) to monocytes induced TNF release, whereas IFN-alpha or IFN-gamma alone or IFN-alpha and tumor cells had no effect. Despite its presence, TNF did not appear to play a major role in the killing of either tumor cell line. However, inhibitors of H2O2-myeloperoxidase system suppressed both IFN-alpha- and IFN-gamma-induced cytotoxicity of the HT-29 cells. Thus IFN-alpha and IFN-gamma can induce both similar and distinct mechanisms of cytotoxicity in monocytes. In addition, both IFN types can increase the susceptibility of tumor cells to lysis by untreated monocytes, although sensitivity to IFN-alpha vs IFN-gamma may vary with different tumor cell lines. These differences observed between IFN-alpha and IFN-gamma on monocytes and tumor cells could have important implications for the clinical use of these cytokines.
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PMID:IFN-alpha and IFN-gamma can affect both monocytes and tumor cells to modulate monocyte-mediated cytotoxicity. 215 15

Purification of monocyte-derived NAP-1/IL-8 by preparative reversed-phase (RP)-HPLC led to the detection of a second peak with polymorphonuclear leukocyte (PMNL)-activating (degranulation, chemotaxis) properties. The monokine responsible for this biological activity, which we tentatively termed NAP-3, could be purified to homogeneity by three different RP-HPLC steps. Tricine-SDS-PAGE analysis gave a single line at Mr 5.3 kD (NAP-1/IL-8 = 5.8 kD). NH2-terminal amino acid sequence analysis read as a major sequence (ASVATELRXCXLQT. .), which shows greater than 40% homology to that of NAP-1/IL-8. The sequence is identical to that found for the 13-kD moiety of melanoma growth stimulating activity (MGSA) and the product of the oncogene gro. Determination of neutrophil chemotactic activity of NAP-3 revealed a typical bell-shaped dose-response curve (ED50 = 2 ng/ml) with no significant neutrophil chemotactic activity at doses greater than 200 ng/ml. Also, in cytochalasin B-pretreated PMNL, NAP-3 elicited release of myeloperoxidase and beta-glucuronidase. Crossdesensitization studies in PMNL enzyme release revealed crossreactivities with the NAP-1/IL-8-R on PMNL. NAP-3 (MGSA/gro) appears to represent the first member of the novel supergene family of beta-thromboglobulin-like host defense cytokines, which expresses both mitogenic as well as proinflammatory properties at the nanogram level.
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PMID:Lipopolysaccharide-stimulated human monocytes secrete, apart from neutrophil-activating peptide 1/interleukin 8, a second neutrophil-activating protein. NH2-terminal amino acid sequence identity with melanoma growth stimulatory activity. 218 61

A new immunohistochemical assay was developed for the detection of human monoclonal antibody (HuMAb) bound to human biopsied tumor tissues. A murine anti-idiotype monoclonal antibody, alpha type, 18C6 (IgGl), was raised against an IgM HuMAb, L612, defining a tumor-associated ganglioside antigen (GM3) and used as a probe in a three step cell-binding assay (HuMAb + anti-id + biotinylated anti-mouse Ig). Anti-id 18C6 has an exclusive binding specificity for HuMAb L612, but does not interfere with the binding of L612 to antigen positive melanoma cell lines or to a purified antigen, GM3. The applicability of 18C6 in the three step cell-binding assay was tested first using a melanoma cell line, UCLASO-M12. L612 bound to M12 cells was specifically detected by 18C6 without any background reactivity in ELISA. When this assay was compared with the standard two-step cell-binding assay (HuMAb + peroxidase-conjugated anti-human IgM) using various cultured tumor cell lines, parallel reactivity was observed. The three-step cell-binding assay was then applied to various fresh-frozen human tumor sections. Positive reactivity was demonstrated on various histologic types of human tumor tissues: primary melanoma (10/10), metastatic melanoma (4/4), nevus (10/10), lung cancer (3/6), breast cancer (2/6), and colon cancer (1/1). Adjacent normal tissues were unstained. Control experiments included the cell-binding assay with L612 alone, 18C6 alone. L612 + unrelated mouse IgG, and unrelated IgM HuMAb (L72) + 18C6; but biotinylated anti-mouse IgG did not react with these control preparations. The results indicate that anti-id 18C6 is a highly specific probe to assess the expression of the ganglioside antigenic epitope recognized by the L612 HuMAb on biopsied human tumor tissues.
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PMID:Murine monoclonal anti-idiotype antibody (alpha) as a probe to detect human monoclonal antibody bound to human tumor tissues. 223 Jan 46


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