Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0023890 (cirrhosis)
 42,195 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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

Two mouse monoclonal antibodies (MoAbs), KM-93 raised against human lung adenocarcinoma and KM-231 raised against human gastric cancer, were useful in serum diagnosis of several human cancer. KM-93 and KM-231 recognize sialyl Lex epitope and sialyl Lea epitope, respectively, expressed on glycoprotein and glycolipid. We established a new "cocktail" sandwich enzyme-linked immunosorbent assay system using the two MoAbs and the advantage of this assay system, which can simultaneously detect sialyl Lex and sialyl Lea antigens, is assessed in the present study. The new assay system is composed of a mixture of KM-93 and KM-231 as 1st antibodies and a mixture of biotinylated two MoAbs as 2nd antibodies. We evaluated the concentration of MoAbs and optimized it to gain high cancer-positivity. This assay system covered sialyl Lex positive and/or sialyl Lea-positive sera and gave a high rate of positive results in lung adenocarcinoma (62.3%), gastric cancer (32.5%), colon cancer (37.5%), pancreatic cancer (83.3%), bile duct and gall bladder cancer (66.7%) and hepatoma (76.9%), whereas positive results in healthy adults remained low. Positive results in benign diseases of lung (12.5%), pancreas (10.8%), gall bladder and bile duct (9.1%) were very low, but were higher in liver cirrhosis (33.3%), hepatitis and liver injury (34.8%). Simultaneous detection of two carbohydrate antigens, sialyl Lex and sialyl Lea was clearly superior to single detection.
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PMID:Advantage of cocktail-use of two anti-tumor monoclonal antibodies, KM-93 and KM-231, in serum diagnosis of cancer. 247 31

The expression of the carbohydrate antigens related to type 1 chain N-acetyllactosamine (1NAcLc) in the proliferated bile ductules was immunohistochemically examined in liver tissues of 10 cases of chronic hepatitis (CH), 9 of liver cirrhosis (LC) and 8 of alcoholic hepatitis. The ductular expression of the examined blood group antigens was essentially the same among these pathological conditions. The backbone structure, i.e., 1NAcLc (Gal beta 1----3GlcNAc beta 1----3Gal beta 1----3R), was not detected in the proliferated ductules as in the normal bile ductules. Its fucosylated structures (Le(a), Le(b) and type 1 chain H) were more strongly expressed in the proliferated ductules than in the normal ductules. Sialyl-Le(a) which was not found in the normal ductules was detected weakly but definitely in the proliferated ductules. Besides proliferated ductules, single or small numbers of epithelial cells expressing the 1NAcLc-related antigens were found intralobularly. This suggests possible migration of biliary epithelial cells into the hepatic lobules. In conclusion, within the proliferated bile ductules (a) synthesis of the 1NAcLc-related antigens is increased compared to the normal ductules, (b) the backbone structure is completely sialylated or fucosylated as in the normal ductules and (c) alpha 1----4fucosylation of sialyl-1NAcLc, i.e., sialyl-Lea, formation occurs despite its absence in the normal ductules.
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PMID:Blood group antigens in the intrahepatic biliary tree. II. Type 1 chain N-acetyllactosamine-related carbohydrate antigens in the proliferated bile ductules. 273 47

Hepatic expression of sialylated difucosyl Lex antigen (SDLex, NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc beta 1-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc beta 1-) was studied with monoclonal antibody FH6, which defines this structure. Hepatocytes in the severe form of chronic active hepatitis and liver cirrhosis strongly expressed SDLex. The antigen was only weakly and focally detected in chronic persistent hepatitis. The mild form of chronic active hepatitis showed intermediate expression. SDLex expressed along the liver cell membranes displayed a honeycomb pattern when extensively expressed in the severe form of chronic active hepatitis or in liver cirrhosis. Cytoplasmic expression was faint and focal. Preferential tissue distribution was at the periphery of the hepatic lobules where the distruction of the limiting plate was present. The antigen was also expressed in sinusoidal lining cells and polymorphonuclear cells but not in the biliary epithelia. Hepatocytes expressing SDLex did not express related carbohydrate antigens, ie, Type 2 chain N-acetyllactosamine, Lex, and sialylated Lea. On subcellular fractionation, the microsome fraction contained the majority of the antigen activity. SDS-PAGE and Western blot analysis revealed one major SDLex-active glycoprotein with an apparent molecular weight of 110 kilodaltons. This glycoprotein was different from SDLex-active glycoproteins found in the sera of cancer patients. No ganglioside showed FH6 reactivity. These results indicate that liver cells in active inflammatory lesion expressed a novel glycoprotein carrying SDLex antigen in honeycomblike membrane-associated pattern.
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PMID:Hepatocellular expression of a novel glycoprotein with sialylated difucosyl Lex activity in the active inflammatory lesions of chronic liver disease. 334 53