Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0007097 (carcinoma)
 152,788 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Ninety-three cases of various types of human primary lung carcinomas have been studied by immunohistochemical technique and 5 cases of human primary lung adenocarcinomas by immunoelectron microscopic method with biotinized peanut lectin (PNA). The results showed that PNA staining was weak positive or negative in the normal bronchial epithelial cells which are adjacent to the carcinoma studied but strong or moderate positive in the carcinoma proper (P less than 0.05). The total positive rate of the lung carcinoma in this series is 81%. About 85% of the positive adenocarcinoma the PNA receptors were distributed along the luminal border, which corresponded with the linear electron-dense deposits on the luminal surface of the adenocarcinoma cell's membrane by immunoelectron microscopy. Squamous cell carcinoma, large cell carcinoma and small cell carcinoma, large cell carcinoma and small cell carcinoma were dominant in PNA cytoplasmic positive, while clear cell carcinoma in whole cell membrane positive. Some of the squamous cell carcinoma, large and small cell carcinoma showed microlumen by PNA staining that could not be found easily by conventional HE staining. It is suggested that these carcinomas mentioned above were poorly-differentiated adenocarcinoma or other types of carcinomas combined with adenocarcinoma. The results also assumed that the increasing of PNA receptor may be proportional to the differentiation of lung carcinoma cell. Therefore PNA receptor may be considered as a marker of carcinoma cell differentiation. It could be helpful in early diagnosis of lung carcinoma and prediction of the prognosis.
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PMID:[Immunohistochemical and immunoelectron microscopic observation of human lung carcinomas using biotinized peanut lectin (PNA)]. 239 36

Two estrogen-sensitive (ZR 75.1 and 734 B) and two estrogen-independent (BT 20 and Hs 578 T) human breast cancer cell lines, and one larynx carcinoma cell line (Hep. 2), were investigated immunocytochemically for the occurrence of lectin binding sites. Peroxidase-labeled peanut agglutinin (PNA) was used. PNA binding sites could be observed in estrogen-sensitive cell lines only. In ZR 75.1, the most estrogen-sensitive cell line, PNA binding sites were also observed without neuraminidase pretreatment. In our study, PNA binding is associated with the biological estrogen dependence of the tumor cells.
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PMID:Lectin binding sites in cultured human breast cancer cells. 241 14

Histochemical alterations of lectin binding and keratin distribution in experimental carcinomas of the hamster cheek pouch were obtained following cryotreatment. Cryotreated carcinoma cells showed a characteristic reduction in lectin binding and keratin staining shortly following cryosurgery. Tumor tissue, on the 2nd and 3rd days after cryotreatment, displayed destruction and necrosis with almost a complete loss of lectin binding and keratin staining. The remaining neoplastic cells located in the deeper layer showed positive reaction for both lectin binding and keratin, which is indicative of tumor recurrence. Histochemical staining of lectin binding and keratin proteins were useful markers in cryotreated tumor cells to identify either destruction and necrosis or vital activity of neoplastic growth.
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PMID:Effects of cryosurgery in experimental carcinoma on lectin binding and keratin distribution. 241 11

Hybridoma generation, using specifically, maximally desialylated human blood group O erythrocytes (T RBC) as immunogen, and biochemical studies suggested the presence of immunogenic Tn epitopes. GalNAc alpha-O, on T RBC. We therefore investigated by immunochemical means whether or not Tn-specific epitopes immunoreactive with anti-Tn antibodies present in ordinary human sera occur on T RBC and on Thomsen-Friedenreich (T) antigen prepared from them. We did detect the Tn epitope with such antibodies, in addition to the T epitope, on isolated T antigen. T RBC absorbed specifically, under standard conditions, 25-60% of the heterogeneous anti-Tn antibody populations in ordinary human sera of appropriately adjusted titer score. The anti-Tn eluted from T RBC had scores ranging from 6.5 to 35% of those of the unabsorbed parent sera. The varying fine specificities of eluted anti-Tn were demonstrated by inhibition of Tn RBC agglutination with putative haptens and antigens. Tn-specific haptens and antigens were the most powerful inhibitors. Depending on the serum used to prepare the anti-Tn eluates, the antibodies could be divided into those that were inhibited well exclusively by GalNAc alpha-O derivatives and those that were also inhibited by Gal, notably by Gal alpha-O derivatives and more strongly by GalNAc and Me-alpha-GalNAc. In the two reciprocal hemagglutination inhibition systems used, Tn-specific haptens were considerably more active than the T-hapten Gal beta 1----3GalNAc alpha-O, and desialylated ovine submaxillary mucin (AS-OSM) had higher activity than T antigen. Inhibition of Tn RBC agglutination by haptens was uniformly more efficient than that of T RBC; this is, at least in part, due to the much higher negative charge of Tn as opposed to T RBC. In microprecipitin tests, Helix pomatia lectin was nearly as powerful a precipitin of T antigen as of AS-OSM. The importance of the terminal GalNAc alpha of T antigen for its precipitation with the Helix lectin was demonstrated by the very high and virtually exclusive inhibitory activity of Me-alpha-GalNAc and GalNAc. Our findings may contribute to comprehension of the significance of uncovered Tn in most carcinomas, and the role of anti-Tn as a "natural" anti-carcinoma antibody. They may also help illuminate the rare heterozygous, autosomal, apparently premalignant spot mutation that leads to Tn RBC in vivo.
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PMID:Tn epitopes, immunoreactive with ordinary anti-Tn antibodies, on normal, desialylated human erythrocytes and on Thomsen-Friedenreich antigen isolated therefrom. 241 12

A lectin reactivity specific to human bowel carcinoma is reported. Twenty-six cases of carcinoma of the large intestine were examined. Normal as well as transitional mucosa and carcinoma tissues were removed from surgical specimens, and paraffin sections were stained with a battery of histochemical methods to characterize glycoconjugates, including high iron diamine-Alcian blue pH 2.5, modified PAS reaction to detect various sialic acids, paradoxical concanavalin A (Con A) staining, and stainings with 10 species of lectins labeled with horseradish peroxidase (HRP). Among the techniques employed, only Griffonia simplicifolia agglutinin-II (GS-II, specific to glucosamine)-HRP staining revealed highly selective affinity to the carcinoma tissues; the apical surface of the carcinoma cells stained most intensely. GS-II reactivity of the cells persisted after prior periodate oxidation, but was significantly enhanced by neuraminidase digestion. Comparison with two other lectin stainings with the same sugar specificity, viz. paradoxical concanavalin A staining and wheat germ agglutinin (WGA)-HRP staining, showed that the GS-II reactive sites lacked class III Con A reactivity but were possibly included in WGA reactive sites. The GS-II-HRP staining should be helpful in the identification of carcinoma tissue and for analysis of carcinoma-associated antigens.
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PMID:Large bowel carcinoma-specific antigens detected by the lectin, Griffonia simplicifolia agglutinin-II. 241 1

Human squamous carcinoma (COLO-16) cells release factors which specifically stimulate the synthesis of major acute-phase plasma proteins in human and rodent hepatic cells. Anion exchange, hydroxyapatite, lectin, and gel chromatography of conditioned medium of COLO-16 cells result in separation into three distinct forms of hepatocyte-stimulating factors (designated HSF-I, HSF-II, and HSF-III) with apparent molecular weights of 30,000, 50,000 and 70,000, respectively. None of the preparations contains detectable amounts of thymocyte-stimulating activity. Each of the three HSF forms stimulates the accumulation of mRNA for alpha 1-antichymotrypsin in the human hepatoma cell line, HepG2. When the same factors were added to primary cultures of adult rat hepatocytes, the expression of the same set of plasma proteins was modulated as by nonfractionated medium. The hormonally induced accumulation of mRNA for acute phase proteins is qualitatively comparable to that occurring in the liver of inflamed rats. Unlike in human cells, in rat liver cells dexamethasone acts additively and synergistically with HSFs. The only functional difference between the three HSF forms lies in the level of maximal stimulation. HSF-I represents the predominant form produced by normal human keratinocytes and closely resembles in molecular size and isoelectric point the activity produced by activated peripheral blood monocytes while the larger molecular weight forms are more prevalent in human as well as mouse squamous carcinoma cells. The observation that HSFs from different sources elicit essentially the same pleiotropic response in hepatic cells led to the hypothesis that the species-specific reaction of adult liver cells to inflammatory stimuli is pre-programmed and that the function of any HSF is to trigger and tune the execution of this fixed cellular process.
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PMID:Regulation of major acute-phase plasma proteins by hepatocyte-stimulating factors of human squamous carcinoma cells. 241 29

Serum alpha fetoprotein (AFP) is heterogeneous, one form binding to the lectin concanavalin A (conA) and the other not. The relative amounts, of the two forms in the serum of patients has diagnostic applications in differentiating between primary hepato-cellular carcinoma and metastatic liver disease. In 36 patients with primary hepatocellular carcinoma, the conA-nonreactive form of AFP comprised less than 20% of the total (range 1.6%-19.2%; median 8.7%), whereas in 13 patients with metastatic liver disease the conA-nonreactive form comprised more than 20% of the total (range 26.6%-91.7%; median 57.6%). Four patients with primary hepatocellular carcinoma were treated with CB3717, and serial changes in the serum AFP characteristics were examined. In two patients in whom the total serum AFP concentration fell, the percentage of the conA-nonreactive fraction, initially less than 20% rose steadily. In two other patients the total serum AFP did not fall significantly and the proportion of the conA-nonreactive fraction remained below 20%.
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PMID:Serial serum AFP heterogeneity changes in patients with hepatocellular carcinoma during chemotherapy. 242 26

Recent studies indicate that intramammary lymphatic invasion represents an important prognostic parameter in breast carcinomas. However, the identification of intramammary lymphatic invasion in tissue sections is a subjective procedure, frequently hampered by factors such as fixation artefacts and interobserver variations. In this study, monoclonal antibodies to ABH isoantigens were applied on formalin-fixed, paraffin-embedded breast carcinoma tissue by using the avidin-biotin-peroxidase complex technique. In addition, the H antigen was localized using the Ulex europeus agglutinin I lectin binding technique. Isoantigen localization provided excellent delineation of lymphatics and blood vessels, in general unhampered by the retention of isoantigen expression in some breast carcinomas. In comparison, Factor VIII-related antigen localization required prior trypsin enhancement and was less sensitive and less consistent. The staining for isoantigens was more intense in vascular than in lymphatic endothelium. ABH isoantigen localization of lymphatic channels identified lymphatic tumor emboli peripheral to and within the carcinomas, and distinguished bona fide intramammary lymphatic invasion from tissue shrinkage artefacts. The applicability to routinely processed tissue permits retrospective studies and renders the identification of intramammary lymphatic invasion a more objective procedure. Further studies are needed to assess the role of this technique in evaluating the prognostic value of intramammary lymphatic invasion; the technique may be extended also to the study of other neoplasms.
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PMID:Intramammary lymphatic invasion in breast carcinomas. Evaluation using ABH isoantigens as endothelial markers. 242 60

Distribution of lectin receptors of peanut, soy-bean, wheat ovary and concanavalin A was studied in normal and tumor human breast tissue. It is established, that in dysplasia and benign neoplasms there is a shift of lectin receptors from the apical or basal pole of acinar epithelium and ducts to the whole plasmolemma surface. There appears a mild affinity of the cytoplasm to the lectins. In carcinoma homogeneous staining of tumour cell cytoplasm and plasmolemma increase. The number of lectin receptors in the cells from low differentiated tumours decreases, a major part of the cells losing the ability of binding to lectins. Malignancy is associated with an increase in mosaic staining. The earliest signs of malignancy can be revealed with the peanut lectin.
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PMID:[Lectin receptors in the breast and its tumors]. 242 39

Many tumour-specific antigens in gastrointestinal cancers have carbohydrate immuno-determinants. These epitopes can be identified by lectins and monoclonal antibodies. By using fluorescein-isothiocyanate (FITC)-conjugated peanut agglutinin (PNA) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) we have investigated glycoproteins carrying altered carbohydrate epitopes in normal and carcinomatous human colorectal mucosa. In normal mucosa PNA stained goblet cell glycoconjugates in the supranuclear (Golgi) distribution. After neuraminidase pretreatment PNA stained actual mucin goblet itself at all levels of the crypts. Colorectal carcinomas displayed a strong and direct binding of PNA to apical cell membranes of carcinomatous cells and intraluminal secretions. Analysis of the glycoproteins by SDS-PAGE and PNA-labelling revealed four carcinoma-associated glycoproteins (26kD, 32kD, 35kD and 50kD). In addition, four glycoproteins (29kD, 30kD, 33kD and 36kD) common to normal and carcinomatous colorectal mucosa could be identified. All of these glycoproteins differed in their molecular weight from those in red cell controls which bind PNA only after desialylation. The study shows that the expression of PNA-binding sites in colorectal carcinomas signifies a cancer-associated carbohydrate alteration. Four carcinoma-associated glycoprotein antigens could be detected by this lectin. The antigens we have identified might be useful in the isolation and purification of more selective reagents for the serologic detection of colorectal cancer.
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PMID:Identification of glycoproteins expressing tumour-associated PNA-binding sites in colorectal carcinomas by SDS-GEL electrophoresis and PNA-labelling. 243 45


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