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)

Levels of glycoprotein-associated carbohydrates (neutral hexoses, hexosamine, sialic acid and fucose) were determined in the serum of patients with either local, regional or metastatic cancer, patients clinically cured of cancer, and controls (smokers and nonsmokers). Total protein-bound carbohydrates were compared with levels of 17 normal serum glycoproteins, carcinoembryonic antigen (CEA), and with lymphocyte reactivity to phytohemagglutin (PHA). Tumor burden was directly related to protein-bound carbohydrate levels in patient groups. Levels of bound carbohydrates reflect the sum of all the changes in serum glycoproteins, but primarily changes in the acute-phase proteins (alpha 1-acid glycoprotein, alpha 1-antitrypsin, haptoglobin, ceruloplasmin) found in the alpha-globulin fraction of serum. Increases in protein-bound carbohydrates in tumor-bearers were not related to increases in CEA. Increased levels of the acute-phase proteins occurred in individuals with depressed in vitro lymphocyte reactivity to PHA. A significant positive correlation was found between lymphocyte reactivity and level of alpha 2HS-glycoprotein. The results suggest that serum protein-bound carbohydrates or glycoproteins may be of adjunctive value is assessing tumor burden and immune reactivity in cancer patients.
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PMID:Correlations among serum protein-bound carbohydrates, serum glycoproteins, lymphocyte reactivity, and tumors burden in cancer patients. 92 66

CEA is a beta1-glycoprotein (mol. w. approx. 200 000) which in embryonic life is usually found as a cell membrane associated antigen in the gastrointestinal (GI) tract and pancreas. Furthermore, it is secreted into body fluids. In healthy adults a very low serum concentration may be found. The clinical significance of CEA lies in its increased formation in primary and secondary adenocarcinomas of colon and rectum and pancreatic carcinoma, where values of 20 ng/ml and more are observed. However, other gastrointestinal (e.g. oesophagus, stomach, gall-bladder) and extragastrointestinal tumors (e.g. lung, breast, urogenital, prostatic, ovarial carcinomas) as well as non-malignant diseases mainly of the GI tract (e.g. hepatitis, cirrhosis, pancreatitis, colitis, diverticulitis) may provoke less frequent and lower increases in the CEA level. Healthy smokers also tend to show a slight increase in CEA concentration. A certain relationship exists between the CEA level and the size and extent of the tumor so that a decrease following operation may account for complete tumor removal, whereas a persistent or recurring increase in the CEA level is highly suspicious of metastases and/or recurrent tumor. Difficulties in proving and purifying CEA are mainly caused by multiple cross-reactions of CEA with other substances, e.g. blood group substances (A, B, Lea, Leb) and normal or other antigens (NGP, NCA, CEX, CCEA 2, NCA 2, CCA-III, FSA, BCGP). The radioimmunoassay is the most suitable method to determine CEA levels in body fluids. The 3 procedures used differ in the precipitation of the specific immune complex by ammonium sulphate (AS), Z-gel (ZG) or a second antibody (SA). Depending on the method, the upper normal limit in serum or plasma corresponds to approximately 2.5 (AS, ZG) or 12.5 (SA) nanogramme/milliliter. CEA determination in the urine is of interest in patients suffering from bladder carcinoma.
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PMID:[Carcinofetal antigens. II. Carcinoembryonic antigen (CEA). (author's transl)]. 108 Feb 18

Carcinoembryionic antigen (CEA) a glycoprotein extracted from colonic cancer tissue (beta-globulin electrophoretic mobility, sedimentation coefficient 7 to 8S, and mol wt approximately 200,000) can be detected and measured by radioimmunoassay. Clinical evaluations of CEA determination have given the following results: In health: (1) Serum CEA level is not influenced by sex, age, blood type, time of blood sampling, or family history of cancer; (2) serum CEA level is influenced by a history of smoking or inflammatory disease of the bowel, lung, pancreas, and other organs (occasionally, a CEA level as high as 10 ng/ml is noted); and (3) currently, CEA positivity is defined as greater than 2.5 ng/ml, however, 5 ng/ml may be more realistic. In cancer: (1) CEA level may be increased in primary cancer of the gastrointestinal (GI) tract as well as in non-GI neoplasia; (2) the CEA test is not recommended for screening to detect early cancer; (3) serum CEA level depends on the stage of the neoplasia and usually is not influenced by the grade of differentiation; and (4) markedly increased (greater than 25 ng/ml serum CEA values are highly suggestive of metastatic cancer, particularly hepatic metastasis. In biological fluid: The CEA or CEA-like activity can be measured in gastrointestinal secretions. Quantitative studies of CEA levels in such fluids may yield more information than is obtainable from studies of serum. However, this possibility needs more study at present. Therefore, the currently available CEA tests cannot replace any of the now standard diagnostic methods for cancer detection. This use for assessment of therapy in selected patients or for following those known to be a high risk for cancer appears promising in preliminary studies, but clinical value, if any, remains to be determined.
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PMID:Carcinoembryonic antigen: clinical application. 124 82

This study reports on biological response modification induced by prolonged continuous subcutaneous (s.c.) infusion of recombinant interferon-gamma (rIFN-gamma) with particular attention to changes of soluble CD14. This glycoprotein with an unknown function is derived from myeloid cells carrying membrane CD14, which is the receptor for lipopolysaccharide (LPS)-LPS-binding protein (LBP) complexes. Fifteen metastatic cancer patients received weekly escalating doses of rIFN-gamma starting at either 50 or 100 micrograms/24 h and increasing up to 400 micrograms/24 h for a median duration of 6 weeks. The maximum tolerated dose was higher (200 micrograms/24 h) with the lower (50 micrograms/24 h) starting dose. Biological activity of rIFN-gamma was evaluated by weekly measurements of CD14, neopterin, and beta 2-microglobulin concentrations in serum as well as monocyte HLA class I and II antigen expression and tumor cytotoxicity. Serum IFN-gamma concentrations increased 20-fold within 4 weeks of therapy. The levels were correlated to the mean dose (r = 0.95, p less than 0.05). Among the biological markers, two patterns were observed. First, serum CD14 concentration and expression of monocyte HLA class II antigens increased significantly during the first week, and marker expression correlated with serum IFN-gamma levels (p less than 0.05); CD14 and HLA class II antigens thereafter returned to pretreatment levels within 4 weeks of therapy despite persistently elevated serum IFN-gamma concentrations. Second, serum neopterin and beta 2-microglobulin concentrations as well as monocyte HLA class I expression also increased significantly within the first week, but remained elevated thereafter without any further dose relationship.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Prolonged interferon-gamma application by subcutaneous infusion in cancer patients: differential response of serum CD14, neopterin, and monocyte HLA class I and II antigens. 137 54

Prostatic specific antigen (PSA) can be detected in normal and benign hypertrophic prostates, as well as in prostatic cancer and its metastases. Since it appears in the serum, this glycoprotein has become an established marker for the detection and monitoring of prostate cancer. Using a radioimmunoassay (CIS--Biointernational, France), we found serum PSA levels higher than 4 ng/ml in 55 of 58 patients with prostatic cancer. The concentrations were proportional to tumor stage: significantly higher in stages C and D than in stages A and B (p less than 0.002). In all 6 cases with occult prostatic carcinoma (stage A), levels were higher than 15 ng/ml. PSA was found to be a good indicator of response to therapy, as well as a marker of tumor progression during follow-up. After radical prostatectomy serum PSA levels decreased to below 1 ng/ml. Following radiotherapy levels returned to normal within 1-6 months in 8 of 11 patients. In 21 of 23 with metastases serum PSA decreased during hormonal treatment. In 3 who responded initially to hormonal therapy, levels increased before clinical manifestation of tumor progression. We conclude that PSA is a sensitive serum marker for the diagnosis of prostatic cancer in cases of metastatic disease of unknown origin, as well as for monitoring the response to treatment of prostatic carcinoma. The use of PSA serum levels for screening for prostatic cancer is still controversial.
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PMID:[Prostatic specific antigen for detection and monitoring of prostatic cancer]. 137 29

Bone scintigraphy is the most sensitive imaging technique for the initial detection of bone metastases and is widely used in the staging of prostatic cancer. This study was performed to assess whether the development of further bone metastases can be detected by serial measurements of the serum glycoprotein prostate-specific antigen (PSA) as an alternative to follow-up scintigraphy. The bone scintigrams and PSA levels of 101 patients with metastatic prostate cancer entered into two therapeutic trials have been reviewed. Serial results of both investigations were available in 59 cases. In three cases new bone deposits were observed without a corresponding rise in PSA. In two other cases the scintigrams were considered to be suspicious of progression with no change in PSA levels; however, further follow-up indicated that these changes were not due to metastases. In 13 cases PSA levels were rising in advance of new deposits on the scintigrams. In the remaining 41 cases the PSA levels and scintigraphic findings paralleled each other. We conclude that serial estimation of PSA levels is a simpler marker for disease progression than bone scintigraphy in metastatic prostatic cancer, but that neither technique in isolation gives complete accuracy.
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PMID:Can serum prostate-specific antigen replace bone scintigraphy in the follow-up of metastatic prostatic cancer? 138 17

Thrombospondin (TSP) is a 450 kDa adhesive glycoprotein. It is present in high concentrations in the platelet alpha-granule and can readily be secreted following platelet activation where local concentrations can be increased by 3-4 orders of magnitude. TSP is also synthesized by a variety of other cells and is incorporated into their extracellular matrix. TSP is a homotrimer with a number of functional domains, at least four of which might serve as receptor recognizing regions. The amino-terminal heparin binding domain interacts with heparin, other glycosaminoglycans and glycolipids and likely recognizes specific cell surface proteoglycans. The central disulfide cross-linked region, 210 kDa non-reduced and 70 kDa reduced, contains a peptide motif CSVTCG which is apparently responsible for binding to glycoprotein IV (CD36) with high affinity. Immediately adjacent to the calcium binding region of TSP, which undergoes considerable molecular relaxation in the absence of calcium, is an RGDA sequence. TSP has been demonstrated to bind to integrins of the alpha v beta 3 and alpha IIb beta 3 class. The carboxy-terminal region of TSP also contains at least one binding epitope for a cell receptor. There are 2 well characterized genes for TSP and truncated forms of TSP have been detected which have inhibitory effects on angiogenesis. Finally, TSP can interact with fibrinogen and fibronectin, perhaps on cellular surfaces, which might serve as secondary receptor-like mechanisms for TSP binding and subsequent mediation of cell adhesion.
Cancer Metastasis Rev 1992 Nov
PMID:Thrombospondin as a mediator of cancer cell adhesion in metastasis. 138 98

Certain metastatic tumor cells successfully form metastases at particular organ sites, and their organ colonization properties cannot be explained by mechanical or anatomic factors. These tumor cells possess the ability to colonize such sites through preferential adhesion to organ microvessel endothelial cells, preferential organ invasion by expression of particular degradative enzymes and response to organ motility factors, and preferential organ growth by response to growth factors present at relatively higher concentrations in the target organ. The likelihood that target organ-associated growth factors exist and are important in metastatic colonization has been approached by studying the mitogenic effects of target organ extracts, fragments, or conditioned media on poorly and highly metastatic tumor cells that show organ preference of metastasis. We previously described the isolation of a major organ-derived (paracrine) growth factor from lung tissue-conditioned medium. Characterization of this mitogen has demonstrated that it is a transferrin or a transferrin-like glycoprotein, and antibodies to transferrin can remove significant growth activity from lung tissue-conditioned medium. Further demonstration of the existence and characterization of metastasis-associated organ (paracrine) growth factors and their receptors will be helpful in understanding the organ preference of metastasis.
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PMID:Differential stimulation of the growth of lung-metastasizing tumor cells by lung (paracrine) growth factors: identification of transferrin-like mitogens in lung tissue-conditioned medium. 138 88

Reliable discriminatory tests to predict metastatic disease would clearly facilitate the management of cancer in the elderly. We have recently identified a 90-110-kilodalton (kDa) cell surface glycoprotein that is differentially expressed in benign and malignant murine adrenal carcinoma cells. In view of the proteins highly glycosylated nature, we have tested its ability to bind to a panel of agarose-bound lectins. Wheat germ agglutinin (WGA), a lectin specific for terminal sialic acid and N-acetylglucosamine (G1cNAc), had a strong affinity for the metastasis-related protein but failed to detect such a glycoprotein in nonmetastatic cells. Treatment of cells with sialidase to remove terminal sialic acids did not affect the affinity of the protein for the lectin, indicating the presence of terminal G1cNAc. We show by in situ that this metastatic binding protein (MBP) is regionally concentrated on the surface of invasive cells but absent in cells unable to invade. We postulate that MBP plays an active role in cell migration through interactions with beta-1,4 galactosytransferase and basement membrane glycoproteines.
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PMID:A murine model for evaluating metastatic potential: characterization of a 90-110-kDa metastasis-binding protein. 142 83

Zinc-alpha 2-glycoprotein, gross cystic disease fluid protein 15, and estrogen receptors are expressed in a great proportion of breast carcinomas. These markers were investigated by immunohistochemistry in 28 metastases from breast carcinomas and for comparison on 24 metastases from other carcinomas. A group of 83 primary nonmammary tumors was also studied. Most (> 96%) breast carcinoma metastases expressed one or several markers, while all metastases of other origins were negative. This sensitive and apparently specific immunostaining proved to be of great utility in cases in which the mammary origin of metastases was difficult to establish. In four axillary lymph node metastases, it even led to the discovery of an occult homolateral breast carcinoma that was not detectable by clinical and mammographic investigations. This study indicates that the combined use of zinc-alpha 2-glycoprotein, gross cystic disease fluid protein 15, and estrogenic receptors represents a useful immunostaining technique that can help the pathologist in determining the origin of breast carcinoma metastases.
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PMID:Mammary origin of metastases. Immunohistochemical determination. 144 49


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