Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027627 (metastases)
 103,950 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The fetoacinar pancreatic (FAP) protein is a specific component of the human exocrine pancreas associated with the differentiation and proliferation of acinar cells. FAP expression is enhanced in cases of pancreatic exocrine cancer and it is found in relatively high concentrations in pathological pancreatic juices. However, tumor cell lines do not secrete FAP into the culture medium. In this paper we analyze the intracellular localization of FAP in cell lines and compare some biological properties of the tumoral FAP with the normal adult and fetal forms. Immunocytological experiments performed using Mab J28 which characterizes FAP, gave a staining pattern suggestive of FAP localization in the ER. Subcellular fractionation corroborated this localization and established that FAP is tightly associated with the microsomal membranes. The absence of reactivity of the tumoral FAP with wheat germ agglutinin lectin and its strong reactivity with concanavalin A is consistent with the idea that FAP in tumor cells does not reach the Golgi apparatus and it is consequently retained in the endoplasmic reticulum (ER). FAP contained in hepatic metastasis derived from pancreatic adenocarcinoma appeared to be similar, if not identical, to that expressed by cell lines. This supports the hypothesis that FAP retention in the ER of malignant cells is a physiological phenomenon and not the result of a modification of cell lines due to the culture conditions. FAP expressed by cancer cell lines and metastases appeared by sodium dodecyl sulfate polyacrylamide gel electrophoresis a homogeneous protein with a M(r) of 120,000. Instead, the secreted mature protein consists of a main component of M(r) 110,000 and shows pronounced polymorphism (dispersion from M(r) 110,000 to 80,000). Increased size of the ER-retained protein is likely due to elongation of the peptide chain. Defective processing in the ER as a result of amino acid mutation could therefore explain the behavior of this protein in tumors.
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PMID:Retention of the fetoacinar pancreatic (FAP) protein to the endoplasmic reticulum of tumor cells. 846 90

Previous studies have suggested that thyroid nodules found in patients with Graves' disease (GD) have a higher likelihood of being malignant, and that thyroid cancer behaves more aggressively when associated with GD, although both of these assertions remain controversial. The purpose of this study was to assess the frequency of cold scintiscan (SC) defects in patients with GD, and to determine the prevalence of thyroid cancer in such patients. Our secondary objective was to determine if there are any risk factors for developing cold defects by comparing clinical characteristics of both GD patients with cold SC defects and age and gender-matched GD patients without cold defects. We included in this analysis patients with a confirmed diagnosis of GD for whom SC results and adequate follow-up information were available. Clinic records were available in 772 patients with GD. Of these, 325 patients met eligibility criteria. Cold defects were found in 39 of 325 (12.0%) patients. Among these, 22 (56.4%) were referred for surgery, of whom 6 (1.85% of all GD patients, 15.2% of GD patients with cold nodules, 25% of GD patients with palpable nodules, and 27.3% of those undergoing surgery) had papillary thyroid cancer (PTC) in the location corresponding to the SC defect. In 2 PTC patients, no palpable abnormality corresponded to the cold defect found to contain cancer at surgery. One PTC patient was found to have metastatic disease to bone, and 2 additional PTC patients required multiple therapies with radioiodine. Compared to age and gender-matched control patients with GD and without cold SC defects, there were no differences in radioactive iodine uptake (RAIU), goiter size, duration of disease, degree of elevation in microsomal antibody (MA) titers, or thyroid-stimulating immunoglobulin (TSI). We conclude that thyroid scintigraphy is an important preliminary test in the evaluation of patients with GD, and that the prevalence of thyroid cancer in the location corresponding to a focal cold SC defect provides justification for further diagnostic evaluation or surgical management.
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PMID:Thyroid cancer yield in patients with Graves' disease selected for surgery on the basis of cold scintiscan defects. 1203 55

To investigate the components of the prostaglandin biosynthetic pathway, the characteristics of cyclooxygenase (COX)-1, COX-2, hematopoietic prostaglandin D synthase (hPGDS), microsomal prostaglandin E synthase (mPGES), and thromboxane synthase (TXS) were examined for autopsied cases with small cell lung cancer (SCLC) and non-small cell lung cancer (NSCLC). Autopsied patients (n=120) with lung cancer were examined, of whom 25 had SCLC and 95 had NSCLC. Immunostaining was performed for COX-1, COX-2, hPGDS, mPGES, TXS, CD34, vascular endothelial growth factor (VEGF), and basic fibroblastic growth factor (bFGF). The immunostaining scores of the prostaglandin biosynthetic pathway markers were significantly higher for adenocarcinoma than for SCLC (p<0.0001). In addition, there were significant correlations between two markers of the prostaglandin biosynthetic pathway for cases with SCLC and NSCLC. For NSCLC, the mean immunostaining scores for the prostaglandin biosynthetic pathway markers were significantly higher for cases with high count groups than low count groups for MVD, VEGF and bFGF, except COX-2 and MVD, and COX-2 and bFGF. The mean immunostaining scores for COX-1, COX-2, mPGES, and TXS were significantly higher for cases with more metastatic organs who had NSCLC. Prostaglandin biosynthetic pathway markers may act synergistically and enhance tumor angiogenesis, the expression of angiogenic factors, and metastases in patients with NSCLC.
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PMID:Characterization of the prostaglandin biosynthetic pathway in non-small cell lung cancer: a comparison with small cell lung cancer and correlation with angiogenesis, angiogenic factors and metastases. 1587 Sep 20

Highly purified human liver microsomes were processed by a combination of the biochemical and proteomic methods. Microsomes were purified from the morphologically normal liver tissue obtained from the resected and discarded masses of surrounding liver upon surgical treatment for hemangioma (control) or hepatic metastases arising from colon cancer (pathology). Proteins of each sample were separated by two-dimensional (2-DE) and one-dimensional electrophoresis (1-DE); selected gel regions were excised, in-gel digested and analyzed by matrix-assisted laser desorption-ionization time-of-flight (MALDI-TOF) mass spectrometry. Analysis of collected fingerprints has revealed a total of 13 microsomal membrane proteins involved in the biotransformation of xenobiotics. These were disulfide isomerase, flavine monooxygenase, NADPH-cytochrome P450 reductase and 10 cytochrome P450 forms, namely: CYPs 1B1, 2A6, 2E1, 2C8, 2C9, 2C10, 2D6, 3A4, 4A11, 4F2. These same samples were characterized by the enzymatic assays using the marker substrates for CYPs 1A, 2B, 3A4, 2C and 2E1. Correlations between mass spectrometric data and enzymatic activities were investigated to demonstrate the manner in which the functional and structural aspects of proteomics meet each other in the field of cytochromes P450.
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PMID:Characterization of human liver cytochromes P450 by combining the biochemical and proteomic approaches. 1653 90


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