Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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

Ras oncogene expression of malignant melanoma and melanocytic nevus has been immunohistochemically analyzed using monoclonal antibodies which were generated against ras oncogene products (p21ras) derived from Harvey sarcoma virus. Freshly frozen tissues from 11 melanomas and 8 melanocytic nevi were examined by immunofluorescence method, and also, formalin-fixed and paraffin-embedded tissues from 26 melanomas and 24 melanocytic nevi by ABC method. There existed differences of p21ras expressions by the type of melanoma that nodular melanoma, epithelioid cell type melanoma, and deeply invaded melanoma revealed higher reactivity with anti-p21ras monoclonal antibody than the other types. The reactivity of melanomas were, thus, well correlated to the degree of malignancy of melanomas. In melanocytic nevi, dermally located nevus cells had relatively strong reactivity with anti-p21ras monoclonal antibody in contrast to junctional type nevi and the nevus cells located in the epidermis in compound type nevi which did not show the positive reaction. p21ras expressions in both melanomas and melanocytic nevi may represent a marker of the immature state of cells corresponding to early stages of the melanocyte evolution as well as the morphologic and enzymologic characteristics.
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PMID:[Immunohistochemical analysis of ras gene expression in human melanomas and melanocytic nevi]. 267 Jul 26

Normal human skin, malignant melanoma, nevocellular nevus, blue nevus, nevus of Ota and mongolian spot were immunohistochemically investigated on the localization of S-100 protein and neuron specific enolase (NSE). Tissues were fixed with buffered-formalin, processed with routine procedure and examined by the ABC technique. All cases of malignant melanoma and nevocellular nevus showed a relatively high amount of S-100 protein, but NSE was scantly demonstrated on about the half cases of these tumors. Blue nevus, nevus of Ota and mongolian spot revealed the presence of a small amount of S-100 protein and NSE on the half cases. Normal melanocytes were devoid of S-100 protein and NSE. Our results suggest that S-100 protein is the useful marker for diagnosis of malignant melanoma, and immunoreactive intensity for S-100 protein represents the differentiation of neural crest derived melanogenic cells and tumors.
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PMID:Immunohistochemical study of S-100 protein and neuron specific enolase (NSE) in melanocytes and the related tumors. 310 77

MHC antigen expression on 20 nevi, and 35 primary and 95 metastatic melanomas was studied by immunoperoxidase techniques using monoclonal antibodies to identify the antigens on frozen tissue sections. DR antigens were not detected on nevi but were detected on 71% of primary melanomas and 56% of metastases, suggesting that this antigen may be a useful marker of malignant transformation of nevi. Expression of class II antigen could not be related to other prognostic histological features of primary melanoma such as tumour thickness, but comparison of the common phenotypes of primary and metastatic melanoma suggested that expression of DR antigens alone in the absence of DP, DQ and ABC antigens may be an indicator of metastatic potential. Class I (HLA-A,B,C) antigens were also expressed infrequently on nevi but were detected on 43% of primary melanomas and 34% of metastases. HLA-A,B,C expression was inversely related to thickness of the primary melanoma. This as well as the lower expression of class I antigens on metastases, may indicate that growth and spread of melanoma may be inhibited by MHC (class I) dependent cytotoxic T cell responses. Expression of class I MHC antigens was unrelated to class II antigens. Expression of DR was more common than DP or DQ, but the latter with one exception, were not expressed in the absence of DR antigens. Significant differences were not found in MHC antigen expression on metastases in lymph nodes compared to those in subcutaneous sites, but further studies are needed to determine whether such differences may exist between metastases in other visceral sites.
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PMID:Immunohistological evaluation of MHC class I and II antigen expression on nevi and melanoma: relation to biology of melanoma. 332 39

Chondroitin sulfate is known to be present in normal and leukemic myeloid cells; however, its definitive subcellular location and association with other glycosaminoglycans (GAGs) has not been demonstrated. We have studied the type and distribution of GAGs in neutrophil granule subpopulations of normal and leukemic myeloid cells using ultrastructural, cytochemical, immunologic, and biochemical methods. At the ultrastructural level, high-iron diamine-thiocarbohydrazide-silver proteinate (HID-TCH-SP) stained sulfated glycoconjugates selectively in immature primary granules of normal promyelocytes and Auer rods and immature granules of leukemic myeloblasts. Staining was weak or absent in mature primary granules, whereas tertiary granules stained moderately. Primary granule staining with HID-TCH-SP was greatly diminished by prior treatment of the specimens with chondroitinase ABC and/or nitrous acid, indicating the presence of chondroitin sulfate and N-sulfated glycosaminoglycan. Immunostaining of myeloid cells with a rabbit antichondroitin 4-sulfate and ferritin-conjugated goat anti-rabbit IgG sequence resulted in staining of most primary granules. Biochemical analysis of GAGs from leukemic myeloblasts containing primary granules and Auer rods, but lacking secondary and tertiary granules, revealed 8 x 10(-17) mole of uronic acid/cell and electrophoretic and sulfaminohexose analysis showed 60%-70% chondroitin sulfate AC of heterogeneous molecular weight, 20%-30% of a GAG that most closely resembled heparan sulfate, and 10% dermatan sulfate. The lack of significant HID-TCH-SP staining of sulfate iin sites other than Auer rods and primary granules in leukemic myeloblasts indicates that these granules contain the chondroitin, dermatan, and heparan sulfate isolated from the same specimen. Similar GAGs are present in primary granules of normal cells as evidenced by their cytochemical and immunostaining properties. Thus, these studies demonstrate a heterogeneous population of GAGs not previously identified and localize these substances to the primary granule of leukemic and normal cells.
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PMID:Glycosaminoglycans in human neutrophils and leukemic myeloblasts: ultrastructural, cytochemical, immunologic, and biochemical characterization. 640 32

Purified proteoglycan subunits from human articular, bovine articular and nasal cartilages, and a rat chondrosarcoma were phosphorylated in vitro by beef heart cAMP-dependent protein kinase in the presence of gamma 32P-ATP. In these experiments, a maximum of 1.7 moles of 32P were incorporated per mole of proteoglycan from human cartilage. Phosphorylation was dependent on the presence of cAMP. Analysis by autoradiography revealed that serine residues in the core protein of the proteoglycan were the sites of phosphorylation. Treatment of proteoglycan subunits with chondroitinase ABC and alkaline phosphatase prior to reaction with cAMP-dependent protein kinase increased the incorporation of 32P by 12-30% when compared with untreated proteoglycans. These data indicate that proteoglycans in cartilage can be phosphorylated by cAMP-dependent protein kinase.
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PMID:Phosphorylation of proteoglycans from human articular cartilage by a cAMP-dependent protein kinase. 647 53

The effect of morphine-3-glucuronide (M3G) on noxious stimulus-evoked Fos protein-like immunoreactivity in the rat spinal cord were assessed by ABC method. It was found that a dose-dependent increase of Fos-like immunoreactive neurons could be induced by M3G intrathecal injection followed by formaline injection into hindpaw. With high dosage M3G (1.1 x 10(-7) mole), dense Fos-like labelling was found in the superficial and the deep dorsal horn bilaterally, While with low dosage M3G (5.4 x 10(-8) and 1.1 x 10(-8) mole), most of the positively labelled neurons were only found in laminae I and II of the ipsilateral dorsal horn to the injured paw. The above results revealed that M3G exerts a potentiating effect on the noxious stimulus-evoked Fos protein-like immunoreactivity in the rat spinal cord.
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PMID:[Morphine-3-glucuronide (M3G) potentiates noxious stimulus-evoked Fos protein-like immunoreactivity in the rat spinal cord]. 778 1

The expression of oestrogen and progestogen receptors, as well as Cathepsin D, an oestrogen-induced protease, in trophoblastic cells of 12 cases of complete hydatidiform mole, 12 cases of partial mole and nine cases of spontaneous abortions, were studied in an attempt to elucidate their possible roles in the pathogenesis of the diseases. The immunohistochemical studies were performed on formalin-fixed paraffin-embedded tissue using the ABC immunoperoxidase method. The intensity of staining and proportion of cells stained were assessed and compared in the three categories of lesions. Immunoreactivity for Cathepsin D was noted in both the syncytio- and cytotrophoblastic cells in all three lesions. Statistical analysis showed consistently stronger and more extensive staining for Cathepsin Din complete moles when compared with abortions. Staining for oestrogen and progestogen receptors was found to be weak in the tissues studied. The strong expression of Cathepsin D in trophoblastic cells of all three lesions, especially in complete mole, suggests that it might be important in the control of trophoblastic cell activities and involved in the pathogenesis of hydatidiform mole. The associated weak expression of sex hormone receptors also suggests that the expression of Cathepsin D in trophoblastic cells may be controlled by modes of regulation other than sex hormones.
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PMID:The expression of cathepsin D, oestrogen receptor and progestogen receptor in hydatidiform mole--an immunohistochemical study. 884 64