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Query: UMLS:C0027651 (tumor)
 685,946 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A clone of natural killer (NK) cells (JTB18) was found to be ultrastructurally similar to peripheral blood large granular lymphocytes (LGL). These cells incorporated [35S]sulfate into cell-associated proteoglycan molecules, which were then isolated by CsCl density gradient centrifugation. As assessed by gel filtration chromatography, the native 35S-labeled proteoglycan and its beta-eliminated 35S-labeled glycosaminoglycans were of Mr approximately 200,000 and 50,000, respectively. The 35S-labeled proteoglycans were resistant to proteolysis, since their Mr were apparently not altered by incubation with either pronase or S. aureus V8 protease. The purified NK cell 35S-labeled proteoglycans were degraded by approximately 90% to 35S-labeled disaccharides with either chondroitinase ABC or AC. High performance liquid chromatographic analysis of the digests revealed these disaccharides to be composed entirely of chondroitin sulfate A (glucuronic acid----N-acetylgalactosamine-4SO4). Whole 35S-labeled cells incubated with chondroitinase ABC failed to release 35S-labeled disaccharides into the supernatant, and x-ray energy-dispersive analysis revealed that sulfur-containing molecules were present in the intracellular granules, thereby localizing the NK cell-associated proteoglycan primarily in the granules of the cell, rather than on the plasma membrane. The 35S-labeled cloned NK cells incubated for 30 min to 4 h with K562 tumor cell targets at a 0.5:1 ratio exocytosed a mean of 49% of the granular 35S-labeled proteoglycans during the first 60 min of the culture. Proteoglycan release was maximal with an effector/target cell ratio of 0.5:1 for JTB18:K562. Significant proteoglycan release from JTB18 NK cells was also obtained with other sensitive target cells such as REX, Molt4, and CEM, but not with cells such as KG1 and Laz156, which have been shown previously to be resistant to killing by this NK cell. Thus, protease-resistant intracellular proteoglycans with chondroitin sulfate A side chains are specifically exocytosed from the granules of human NK effector cells upon contact with sensitive targets, suggesting that these proteoglycans may be involved in the mechanism of cytotoxicity.
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PMID:Proteoglycans in cell-mediated cytotoxicity. Identification, localization, and exocytosis of a chondroitin sulfate proteoglycan from human cloned natural killer cells during target cell lysis. 393 16

The murine monoclonal antibody (MAb) designated DF3 has defined a high m.w. antigen detectable in human breast carcinomas and in human milk. DF3 antigen is detectable on apical borders of secretory mammary epithelial cells and in the cytosol of less differentiated malignant cells. DF3 antigen expression has been shown to correlate with the degree of human breast tumor differentiation, and the detection of a cross-reactive species in human milk has suggested that DF3 antigen might be useful as a biochemical marker of differentiated mammary epithelial cells. To further characterize DF3 antigen, we have developed an approach to purify the cross-reactive species by using gel filtration and antibody affinity chromatography. The affinity column-purified DF3 antigen was absorbed by wheat germ agglutinin and peanut agglutinin, but not by concanavalin A or lentil lectin. In contrast, wheat germ agglutinin inhibited MAb DF3 reactivity with the purified antigen, whereas there was little, if any, inhibition when using peanut agglutinin. These findings are thus consistent with the involvement of terminal N-acetyl-D-neuraminic acid and/or N-acetylglucosamine residues in the antigenic site. DF3 antigenicity was also sensitive to neuraminidase, but not chondroitinase ABC, chondroitinase AC, chondroitin-4-sulfatase, or hyaluronidase. Furthermore, DF3 antigen was sensitive to Pronase, subtilisin BPN', and alpha-chymotrypsin. The presence of O-glycosidic linkages between carbohydrate and protein in the DF3 antigenic site was further supported by the presence of NaBH4-sensitive sites. Together, these results suggest that sialyl oligosaccharides present on a peptide backbone are required for maintaining DF3 antigenicity. Similar findings have been demonstrated for DF3 antigen purified from both human milk and breast cancer effusions. However, the DF3 antigen in human milk consisted of a single high m.w. species, whereas the tumor-associated antigen consisted of two distinct glycoproteins with m.w. of 330,000 and 450,000. These findings may be relevant to the recent demonstration that distinct high m.w. DF3 antigens are elevated in the circulation of patients with breast carcinoma.
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PMID:Purification and characterization of a high molecular weight glycoprotein detectable in human milk and breast carcinomas. 404 99

A monoclonal antibody, 9.2.27, with a high specificity for human melanoma cell surfaces has been utilized for biosynthetic studies in M21 human melanoma cells to define a unique antigenic complex consisting of a 250-kilodalton N-linked glycoprotein and a high molecular weight proteoglycan component larger than 400 kilodaltons. The 250-kilodalton glycoprotein has endoglycosidase H-sensitive precursors and shows a lower apparent molecular weight after treatment with neuraminidase. The biosynthesis of the proteoglycan component is inhibited by exposure of M21 cells to the monovalent ionophore monensin, this component can be labeled biosynthetically with 35SO4, is sensitive to beta-elimination in dilute base, and is degraded by both chondroitinase AC and ABC lyases, suggesting that it is a chondroitin sulfate proteoglycan. These data demonstrate that the antigenic determinant recognized by monoclonal antibody 9.2.27 is located on a glycoprotein-proteoglycan complex which may have unique implications for the interaction of glycoconjugates at the human melanoma tumor cell surface.
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PMID:Unique glycoprotein-proteoglycan complex defined by monoclonal antibody on human melanoma cells. 617 65

Immunization of mice with a plasma membrane-enriched fraction from human malignant melanoma cells and subsequent generation of hybridomas resulted in the isolation of an IgG1 monoclonal antibody, 155.8, that recognizes chondroitin sulfate proteoglycans. By cell binding analysis, 155.8 was shown to react with seven of eight cultured melanoma cell lines, but not with a variety of lymphoblastoid cell lines or cultured tumor cells derived from other solid tumor types. Indirect immunoprecipitation of the 155.8 antigen from intrinsically labeled melanoma cells revealed a glycoprotein of Mr = 250,000 and a sulfated molecule of Mr greater than 400,000. The antigen was identified as a chondroitin sulfate type A/C proteoglycan synthesized by melanoma cells on the basis of its sensitivity to chondroitinase ABC digestion and the identification of sulfated glycosaminoglycans released from the antigen immunoprecipitated by 155.8. The determinants recognized by antibodies 155.8 and 9.2.27, another anti-chondroitin sulfate proteoglycan, immunoprecipitate only a proteoglycan from high density cesium chloride gradient fractions, (1.487 g/liter); however, they immunoprecipitate a free glycoprotein of Mr = 250,000 from low density fractions (1.317 g/liter). This demonstrated that the 155.8 and 9.2.27 determinants, both of which reside on the glycoprotein of Mr = 250,000, are also present in the proteoglycan, suggesting that this glycoprotein is the proteoglycan core protein. Monoclonal antibody 155.8 reacts with a determinant on the core protein distinct from that recognized by 9.2.27. Proteoglycans bearing 155.8 determinants are distributed on the surface of cultured melanoma cells in a punctated fashion that apparently resolves to short, filamentous structures at high magnification. Immunohistochemical analysis demonstrated that 155.8-defined proteoglycans are found in freshly biopsied melanoma tissue, suggesting that these antigens are also synthesized in vivo by melanoma cells.
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PMID:Characterization of monoclonal antibody 155.8 and partial characterization of its proteoglycan antigen on human melanoma cells. 619 23

Aspiration biopsy by fine needle from the major salivary glands has been an under-utilized technic in the United States. To evaluate this form of biopsy, 69 patients with salivary gland enlargement were examined by this technic; 47 had confirmative histology. Characteristic ABC patterns were seen in the benign mixed tumor, the papillary cystadenoma lymphomatosum, the mucoepidermoid carcinoma, and malignancy metastatic to the salivary gland. These findings are described. The method proved complication-free and accurate and is recommended for all tumors of the salivary gland.
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PMID:Aspiration biopsy cytology of the salivary gland. 626 19

Twenty seven patients with malignant lymphoma of lymphocytic type/B-chronic lymphocytic leukaemia (ML, L/B-CLL, Kiel classification) diagnosed from lymph node and splenectomy specimens were studied histologically and immunologically. Lymph node biopsies showed a diffuse effacement of normal architecture by small round lymphocytes usually with scattered proliferation centres (PC). A1 spleens showed white pulp with or without red pulp involvement, sometimes with tumour nodules present. PC-like cells or PC were only found in the white pulp or tumour nodules. Studies of 13 specimens using the ABC immunoperoxidase technique on frozen sections with a large panel of monoclonal antibodies showed that although a part of the monoclonal B cell neoplasm, the proliferation centres or splenic white pulp have a different phenotype from the surrounding cells. Some of these phenotypic changes are similar to those reported with in vitro induction of "maturation" of ML, L/B-CLL cells. The implications for normal B-cell development are discussed. In contrast to reported peripheral blood findings, T cells, predominantly of T helper phenotype in lymph nodes, were present but usually not numerous.
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PMID:Lymphocytic lymphoma/B-chronic lymphocytic leukaemia--an immunohistopathological study of peripheral B lymphocyte neoplasia. 638 14

The authors describe a recurrent nasal glioma of the nasal septum in a new-born boy. Histologically, the nodular tumor tissue resembled normal glial tissue. Immunohistochemical studies with the immunoperoxidase (PAP and ABC) techniques revealed the presence of both S-100 protein and glial fibrillar acidic protein (GFAP), indicating the glial nature of the tumor.
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PMID:An immunohistochemical analysis of S-100 protein and glial fibrillary acidic protein in nasal glioma. 639 Oct 84

The expression and core protein structure of two proteoglycans, the major cartilage proteoglycan isolated from a rat chondrosarcoma and a small molecular weight chondroitin sulfate proteoglycan isolated from a rat yolk sac tumor, have been compared. The cartilage proteoglycan was not detectable in the cartilage tissue of cartilage matrix deficient (cmd/cmd) neonatal mice by immunofluorescence, but the cmd cartilage did react with antibodies against the core protein of the yolk sac tumor proteoglycan. Radioimmunoassays showed that the core proteins of these proteoglycans are not cross-reactive with each other. Analysis of the core proteins by sodium dodecyl sulfate/polyacrylamide gel electrophoresis after chondroitinase ABC treatment of the proteoglycan revealed a large difference in their sizes. The cartilage proteoglycan core protein had a molecular weight of about 200,000 while the yolk sac tumor proteoglycan core protein migrated with an apparent molecular weight of about 20,000. In addition, the cultured yolk sac tumor cells that make the small proteoglycan did not react with antiserum against the cartilage proteoglycan. These results indicate that the proteoglycan isolated from the yolk sac tumor is similar to the small chondroitin sulfate proteoglycan species found in cartilage and support the existence of at least two dissimilar and genetically independent chondroitin sulfate proteoglycan core proteins.
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PMID:Immunological evidence for two distinct chondroitin sulfate proteoglycan core proteins: differential expression in cartilage matrix deficient mice. 640 83

This report consists of 2 parts. Part I: The usefulness of computed tomography (CT) in the diagnosis of rotator cuff tear was assessed. The rotator cuff could not be visualized in detail by CT unless introduction of contrast material into the joint cavity was performed. CT arthrography was performed on 21 cases of rotator cuff tears. The most detailed information was obtained when a relatively low concentration of contrast material (3.25% Angiografin) was filled in the joint cavity, and when the shoulder joint was rotated to the maximum outwards at the side. CT arthrography proved to be the most reliable method for assessing the extent and portion of the rotator cuff tears, so that it demonstrated conclusive evidence of diagnosis and management in 89% of patients studied. Part II: The usefulness of CT in the diagnosis of bone and soft tissue tumors was assessed. CT examination provided unique preoperative information which could imagine a more precise histological characteristics and anatomical localization of the lesion. Contrast enhancement (CE), when used, proved to be helpful in predicting the nature of tumors. The CE by intra-arterial infusion, or intravenous bolus injection of contrast material during the scan was more useful than that by intravenous drip infusion of the material. The information regarding change of tumor size, CT number and CE were appropriate indicators which directly corresponded to responsiveness of the tumor to the chemotherapy and radiotherapy performed. Preoperative ABC classification of the tumor by information regarding its size, location, definition and anatomical relation of tumors to vital structures (neural, vascular, and visceral) was done by using CT. The classification clearly corresponded to the status of patients regarding the treatment required for the patients.
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PMID:[The value of computed tomography in the diagnosis of the rotator cuff tears and bone and soft tissue tumors]. 650 79

Regarding the event of an adenocarcinoma of the colic type of the cecal appendix, operated on at the ABC Medical College Hospital, the authors summarize the subject stating that, among the appendiceal carcinoma, this particular one tends to spread, by the veins or lymphatics, besides spreading by contiguity. This carcinoma hardly presents a symptomology of its own. It appears fairly often as acute appendicitis. The authors also state the difficulty for a macroscopic diagnosis. Thus, its real nature is determined, in general, only after the histologic exam of the removed part. The right hemicolectomy is the most indicated surgery and best results are obtained in the first surgery or 30 days afterwards. About the reported case the patient was operated on with the pre and intra operatory diagnosis of appendicitis and the histologic exam, on top of confirming it, pointed out the presence of neoplasm. After the indication for reoperation, the prompt spreading of the neoplastic disease offered no means to perform any other surgery disclosing its malignant potential.
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PMID:[Adenocarcinoma of the cecal appendix. Report of a case of the colic type]. 653 38


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