Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0001418 (adenocarcinoma)
 68,496 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Hyaline globules (HGs), spherical intracytoplasmic eosinophilic droplets, have been associated with a variety of conditions, including hepatocellular carcinoma, lung adenocarcinoma, and Kaposi's sarcoma, but they have not been described in cartilaginous tumors. In specimens of 60 cartilaginous neoplasms we found that 22 of 33 chondrosarcomas (67%), eight of 16 enchondromas (50%), and three of seven soft tissue chondromas (43%) exhibited HGs. HGs were seen more commonly in low grade chondrosarcoma (70%) and were relatively rare in high grade chondrosarcoma (25%). No HGs were identified in three osteochondromas, one synovial chondromatosis, or 15 normal cartilaginous tissues taken from various sites. Cartilage associated HGs ranged in size from 2 to 20 microns, were diastase resistant and periodic acid-Schiff (PAS) stain positive, demonstrated autofluorescence, and variably stained with Mallory's phosphotungstic acid-hematoxylin stain (PTAH). A panel of immunostains did not show any specific staining reactions with HGs. Ultrastructurally the HGs were spherical, non-membrane-bound bodies having complex architectural features associated with profiles of rough endoplasmic reticulum. Electron probe x-ray microanalytic (EPXMA) study showed significant peaks of sulphur and calcium. We conclude that HGs represent secretory products of probable glycoprotein nature, may accumulate in a variety of cartilaginous neoplasms, and may be seen more frequently in low grade chondrosarcomas.
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PMID:Intracytoplasmic eosinophilic hyaline globules in cartilaginous neoplasms: a surgical, pathological, ultrastructural, and electron probe x-ray microanalytic study. 752 63

The host reaction is an important factor in the biological behavior of cancers. In human colon adenocarcinoma, stromal cells and some cancer cells express the urokinase receptor (uPAR), a molecule involved in the regulation of extracellular proteolysis. The present study reveals the identity of uPAR-expressing cell types and the subcellular localization of this molecule by immunoelectron microscopy in colon cancer. uPAR-positive cells were most abundant at the invasive margin of colon cancer and were identified as macrophages, fibroblasts, neutrophilic and eosinophilic granulocytes, endothelial cells and cancer cells. Of these, the most numerous were macrophages with uPAR detected along the plasma membrane, in accordance with its function in plasminogen activation on the cell surface. Fibroblasts were labeled in the lumen of rough endoplasmic reticulum, indicating its intracellular synthesis. Some granulocytes and endothelial cells expressed immunoreactivity along the plasma membrane. uPAR-positive cancer cells were stained along the plasma membrane and in rough endoplasmic reticulum. These findings suggested that a variety of non-malignant host cells play an important role in the plasmin-mediated breakdown of the extracellular matrix at the invasive margin.
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PMID:Expression of urokinase receptor in various stromal-cell populations in human colon cancer: immunoelectron microscopical analysis. 755 16

The expression of multidrug-resistance-associated protein (MRP) was assessed in various types of untreated lung cancer using an immunohistochemical technique. MRP was abundantly expressed in 28 of 59 adenocarcinoma specimens (47%) and its expression was associated with the degree of glandular differentiation of the tumor. MRP expression in well-differentiated adenocarcinomas (56%) was higher than in poorly differentiated adenocarcinomas (22%) (p < 0.01). lower--20% in squamous-cell carcinomas, 20% in large-cell carcinomas and 0% in small-cell carcinomas and carcinoids. RT-PCR showed that the MRP-positive adenocarcinomas and squamous-cell carcinomas expressed mrp mRNA significantly. Immunoelectron microscopically, MRP was localized in the plasma membrane and rough endoplasmic reticulum. It is thus important to take MRP into account when considering chemotherapy for lung cancers because levels of mdr I gene product, another multidrug-resistance gene family, are low in untreated lung cancers.
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PMID:Preferential expression of the multidrug-resistance-associated protein (MRP) in adenocarcinoma of the lung. 759 4

Gallium is a group IIIa transition metal that lowers serum calcium by an unknown mechanism and has been utilized in the treatment of cancer-associated hypercalcemia. The purpose of this study was to histomorphometrically investigate the ultrastructural effects of gallium nitrate on osteoclasts and osteoblasts in trabecular bone of normal nude mice and nude mice with humoral hypercalcemia of malignancy. Two groups of normal nude mice (n = 7 and n = 8, respectively) and two groups of hypercalcemic nude mice (n = 9) bearing a serially transplantable canine adenocarcinoma (CAC-8) were treated with vehicle or gallium nitrate. Osteoclasts were hypertrophied in vehicle-treated tumor-bearing nude mice as compared with vehicle-treated nontumor-bearing nude mice. Osteoclasts from tumor-bearing nude mice treated with gallium nitrate were significantly decreased in size and had fewer intracytoplasmic vesicles as compared with osteoclasts from vehicle-treated tumor-bearing nude mice. Degenerate osteoclasts, characterized by pyknotic nuclei and increased cytoplasmic vacuolation, were observed in both groups of gallium-treated nude mice. Osteoblasts from vehicle-treated tumor-bearing nude mice were hypertrophied and had extensive lamellar arrays of rough endoplasmic reticulum as compared with osteoblasts from vehicle-treated nontumor-bearing nude mice. Osteoblasts in gallium-treated nude mice (tumor-bearing and nontumor-bearing) were small and flattened with poorly developed cytoplasmic organelles. This investigation demonstrated that osteoclasts and osteoblasts in nude mice treated with gallium nitrate had ultrastructural evidence of decreased metabolic and functional activity. The results suggest that gallium nitrate lowers serum calcium by inhibiting osteoclastic bone resorption.
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PMID:Ultrastructural and histomorphometric evaluations of gallium nitrate on bone in nude mice bearing a canine adenocarcinoma (CAC-8) model of humoral hypercalcemia of malignancy. 772 96

Previous reports revealed a discrepancy in gelatinase A localization in human cancers; i.e., protein localization in cancer cells and mRNA localization in stromal fibroblastic cells. To clarify this, we conducted immunoelectron microscopic study of gelatinase A in cancer and stromal cells in human gastrointestinal and skin carcinomas. Although both carcinoma cells and fibroblasts were positive for gelatinase A, the subcellular localizations were different. On immunoelectron microscopy, fibroblasts showed immunoreactivity in the lumen of the rough endoplasmic reticulum (rER) or in the cytosol on the surface of rER, demonstrating synthesis of the protein. Carcinoma cells showed diffuse deposition of gelatinase A in the cytosol, suggesting the accumulation of the antigen both in adenocarcinoma and squamous cell carcinoma. Immunoreactivity along the cell membrane was demonstrated in one case of skin carcinoma. Macrophages showed also diffuse deposition of gelatinase A in the cytosol. In conclusion, we found a qualitative difference of gelatinase A localization between carcinoma cells and fibroblasts, and concluded that carcinoma cells may not be important in the secretion of gelatinase A.
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PMID:Immunoelectron microscopic localization of gelatinase A in human gastrointestinal and skin carcinomas: difference between cancer cells and fibroblasts. 774 1

The distribution of carcinoembryonic antigen (CEA) in human gastric adenocarcinoma cell lines (HPE-GAC-3 cells and HPE-GAC-2 cells) was determined immunohistochemically by indirect peroxidase-labeled antibody method at the light and electron microscopic levels. In GAC-3 cells that proliferated as non-adherent single cells, CEA was located in the perinuclear spaces, the endoplasmic reticulum, Golgi apparatus, vesicles, multivesicular body (MVB) and entire plasma membrane. Membrane CEA was shown to be internalized into MVB in GAC-3 cells. In GAC-2 cells that form an acinus, CEA was predominantly present along the microvilli of the luminal surface and in glycocalyceal bodies, the vesicles which bud from the microvilli into the lumen. These results suggest that in poorly differentiated cancer cells CEA is transported over the entire cell surface, retained on the membrane and accumulated into the cell by way of the MVB, but in well differentiated cancer cells the newly synthesized CEA is rapidly and predominantly transported to the luminal surface and rapidly released from the membrane into the lumen by way of the glycocalyceal body.
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PMID:Immunoelectron microscopic localization of carcinoembryonic antigen in gastric adenocarcinoma cell lines. 795 50

We investigated the appearance and activity of the cysteine proteinase cathepsin B and its physiological inhibitors, stefins A and B, at the cellular level in human tumor cell lines HS-24, derived from a primary lung tumor (squamous cell), and SB-3, derived from a metastasis (lung adenocarcinoma). In addition to cathepsin B, these tumor cells also expressed the immunologically and functionally related cathepsin L, but not cathepsin H. Stefin A was found in HS-24 but not in SB-3 cells; stefin B was found in both cell types. Using a specific fluorogenic cytochemical assay, the intracellular activity of the enzyme was localized and quantified. Thus, the cellular cathepsin B kinetics for the synthetic substrates Z-Arg-Arg-4M beta NA and Z-Val-Lys-Lys-Arg-4M beta NA, its pH dependence and inhibition by E64, stefins A and B, and cystatin C could be determined. From these measurements it appeared that the enzyme exhibited different cleavage rates for these substrates in the different cell types, showed considerable cleavage activity at neutral pH, which was stable under these conditions for extended time periods, and was highly sensitive to the inhibitors E64 and cystatin C but was considerably less sensitive to stefins, particularly stefin A. By conventional light microscopy, confocal laser scanning microscopy, and electron microscopy the enzymatic activity was localized in lysosomes, as expected, but also in the endoplasmic reticulum, nuclear membrane, and plasma membrane. The endoplasmic reticulum is a site at which only pre-mature enzyme forms exist, which are usually not active. The appearance of enzymatic activity at the plasma membrane confirms earlier biochemical and immunofluorescence microscopic investigations. The different sites of localization within the cells make it likely that different forms of the enzyme are expressed simultaneously, which follow alternate ways of processing and sorting. Taken together, the results support an involvement of the enzyme under extracellular conditions in degradative processes.
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PMID:Cathepsin B activity in human lung tumor cell lines: ultrastructural localization, pH sensitivity, and inhibitor status at the cellular level. 801 75

Immunohistochemical and ultrastructural investigations of thyroid C cells were conducted in male nude (athymic) mice bearing a serially transplantable canine adenocarcinoma (CAC-8) model of humoral hypercalcemia of malignancy following subcutaneous administration of gallium nitrate. The following four groups were investigated: 1) vehicle-treated non-tumor-bearing control mice; 2) non-tumor-bearing mice treated with gallium nitrate; 3) vehicle-treated hypercalcemic mice bearing CAC-8; and 4) CAC-8 tumor-bearing mice treated with gallium nitrate. Gallium nitrate-treated tumor-bearing mice had a significant decrease in serum calcium as compared with tumor-bearing controls. C cells of non-tumor-bearing mice stained intensely for calcitonin and calcitonin gene-related peptide and weakly for chromogranin A and neuron-specific enolase. In C cells of both vehicle- and gallium-treated tumor-bearing mice, immunoreactive staining was decreased for calcitonin, calcitonin gene-related peptide, and chromogranin A, whereas there was a moderate increase in staining for neuron-specific enolase. Ultrastructurally, thyroid C cells in hypercalcemic tumor-bearing control and gallium-treated mice were hypertrophic and markedly degranulated as compared with those of non-tumor-bearing controls. Hypertrophic C cells contained few mature secretory granules, a well-developed Golgi apparatus, and lamellar arrays of rough endoplasmic reticulum. There was no evidence of C-cell hyperplasia. Immunohistochemical and ultrastructural findings revealed that C cells in mice with cancer-associated hypercalcemia were primarily in the actively synthesizing phase of the secretory cycle and had diminished immunoreactivity for calcitonin, calcitonin gene-related peptide, and chromogranin A.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Effects of humoral hypercalcemia of malignancy and gallium nitrate on thyroid C cells in nude mice: immunohistochemical and ultrastructural investigations. 805 30

The authors studied the neutrophil inflammatory reaction by light and electron microscopy in 4 small early gastric cancers (three tubular adenocarcinomas and one adenocarcinoma with signet-ring cell component), selected for the absence of coagulative necrosis and ulceration. Neutrophils showed ultrastructural signs of activation such as aggregation, adhesion and lipid bodies. Some neutrophils were found to be in intimate contact with the intact tumour cells and with those that displayed a varying degree of damage. In particular, relatively early damage, such as disorganization of the intermediate filaments and dilatation of the rough endoplasmic reticulum, occurred at the contact regions. In spite of the severe damage to the tumour cells, the neutrophils themselves were intact. These findings are discussed in relationship to a number of recent studies of the neutrophil-mediated tumour cell injury, in man and animals.
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PMID:Neutrophil interaction with tumour cells in small early gastric cancer: ultrastructural observations. 807 89

We have identified four new cases of the cardiac lesion resembling a histiocytoid (epithelioid) hemangioma from the consultation and surgical pathology files of the Mayo Clinic from 1979 to 1992. The lesions occurred in two men and two women, mean age 60 yr (range, 55 to 63), three of whom had undergone previous cardiac catheterization. All were found incidentally, two as separate tissue fragments obtained by right ventricular endomyocardial biopsy during investigations for dilated cardiomyopathy, and two during mitral valve replacement (one free floating in the left atrium and the other attached to the mitral valve). The latter two lesions measured 1.0 and 0.8 cm. All were composed of histiocytes (macrophages) focally admixed with cuboidal cells which formed strips and tubular arrays in three cases. Immunohistochemistry (two cases) confirmed their biphasic nature with cytokeratin positivity of the cuboidal cells and CD68 (KP-1) positivity (macrophage-myeloid lineage) of the histiocytes. Carcinoembryonic antigen and Leu-M1 were negative for both cell types. Transmission electron microscopy (two cases) showed macrophage-like cells and cuboidal cells with intracytoplasmic intermediate filaments, desmosome-like cellular junctions, and rough endoplasmic reticulum consistent with mesothelial cells. All four patients had a benign clinical course (range, 2 mo to 13 yr). This mesothelial and monocytic (histiocytic) process is postulated to relate to previous cardiac catheterization (applicable in three of our patients). The importance of these nodules, which are likely reactive, is their potential confusion with metastatic adenocarcinoma. We propose the name mesothelial/monocytic incidental cardiac excresences (cardiac MICE) for these lesions.
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PMID:Mesothelial/monocytic incidental cardiac excrescences: cardiac MICE. 799 30


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