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

Rabbit antiserum to Pre-S1 protein was used to establish peroxidase-antiperoxidase (PAP) and avidin-biotin-peroxidase complex (ABC) immunohistochemical techniques for detection of Pre-S1 protein in paraffin-embedded liver tissue. Pre-S1 protein could be expressed in hepatocyte cytoplasm and on membrane in some cases with chronic viral hepatitis, cirrhosis and hepatocellular carcinoma (HCC), and its expression was intimately associated with HBsAg, HBcAg in liver and HBV DNA in serum, indicating that pre-S1 protein may represent the essential component of hepatitis B virus (HBV) and also serve as one of the markers of HBV infection. The incidence of Pre-S1 protein was slightly lower in nontumorous liver of HCC than in other cases and Pre-S1 protein could not be detected in tumorous tissue of HCC suggesting that expression of pre-S1 protein may be suppressed in HCC cases.
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PMID:A preliminary study on expression and significance of pre-S1 protein in liver tissue of patients with HBV infection. 276 Sep 66

Implications of P-450 in human hepatic disorders were immunohistochemically examined. We first confirmed that an antibody against P-450-HM1, an isozyme of cytochrome P-450 which was purified from human livers at autopsy, detects only P-450 on immunoblots. In a study of 79 consecutive autopsied livers using the avidin-biotin-peroxidase complex method, the antibody reacted strongly with fetal hepatocytes, the reaction being more intense in the left lobe than in the right lobe. In normal livers, immunoreactivity was confined to centrilobular hepatocytes, decreasing in the periportal zone. Enhanced expression was occasionally found in scattered hepatocytes and in hepatocytes surrounding sublobular veins; this enhancement was related to longterm steroid therapy. No specific induction was observed in patients with toxic hepatitis. In patients with fibrosis, cirrhosis, or regenerative nodules, however, P-450-positive hepatocytes were observed in the periportal and middle zones as well as in the central zone. In contrast, hepatocellular carcinomas were devoid of P-450 immunoreactivity. These results suggest that P-450-HM1, which is abundant in the fetal liver, is reexpressed in regenerating hepatocytes but not in cancers.
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PMID:Distributional variation of P-450 immunoreactive hepatocytes in human liver disorders. 279 57

Using a monoclonal antibody to bromodeoxyuridine, we studied the cell kinetics of human hepatocellular carcinoma, liver cirrhosis, chronic active hepatitis and alcoholic liver fibrosis. Specimens were taken either by biopsy or surgery and immediately incubated with 0.1% bromodeoxyuridine solution at 37 degrees C for 45 min. After in vitro labeling, the bromodeoxyuridine taken up by the nuclei of S-phase cells was determined by the avidin-biotin-peroxidase complex method, using an anti-bromodeoxyuridine monoclonal antibody as the first antibody. The number of positive nuclei in 1,000 hepatic cells was counted, and the bromodeoxyuridine labeling index was expressed per thousand. The mean bromodeoxyuridine labeling index +/- S.D. of the cancerous portion of hepatocellular carcinoma, the noncancerous portion of hepatocellular carcinoma, liver cirrhosis, chronic active hepatitis and alcoholic liver fibrosis were 64.1 +/- 31.3, 33.6 +/- 14.4, 23.2 +/- 20.8, 9.1 +/- 6.1 and 21.6 +/- 13.0, respectively. The mean bromodeoxyuridine labeling index of the hepatocellular carcinoma cancerous portion was statistically higher than that of any other group. There was no statistical difference by the t test or the Wilcoxon test between the noncancerous portion of hepatocellular carcinoma and liver cirrhosis, and these two groups were proved interdependent by chi 2 test (Fisher's exact test), whether they were subdivided by bromodeoxyuridine labeling index greater than or equal to 10 or not. Bromodeoxyuridine labeling index was not significantly correlated with the usual biochemical parameters such as serum AST, ALT, gamma-GTP, alkaline phosphatase, lactate dehydrogenase, cholinesterase, albumin, and alpha-fetoprotein.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:S-phase cells in diseased human liver determined by an in vitro BrdU-anti-BrdU method. 284 68

Excessive ethanol intake may affect the intestinal mucosa functionally and morphologically. The ethanol effect could partly be the result of inflammatory mechanisms, possibly reflected by an enhanced local granulocyte turnover. This study investigated habitual alcoholics by segmental perfusion of the jejunum and analysed the perfusion fluid content of granulocyte granule constituents. The mean jejunal secretion rate of myeloperoxidase (MPO), a neutrophil granule constituent, was 152 (26) (SE) ng/min/40 cm jejunal segment in the controls (n = 16). The MPO secretion rate in non-cirrhotic habitual alcoholics (n = 7) was on average 450 (103) ng/min and significantly increased compared with controls (p less than 0.001). In contrast alcoholics with cirrhosis (n = 6) had normal MPO secretion rate. The mean secretion rate of eosinophil cationic protein (ECP), an eosinophil granule constituent, was in the controls 77 (15) ng/min/40 cm jejunal segment. Corresponding values in non-cirrhotic and cirrhotic alcoholics were 141 (38) and 130 (93) ng/min, respectively (ns). The data suggest an enhanced neutrophil granulocyte turnover in the jejunum in alcoholics, possibly contributing to the ethanol induced affection of the small bowel. The lack of increased neutrophil activity in cirrhotic alcoholics may reflect a role of the liver for granulocyte activity.
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PMID:Neutrophil and eosinophil involvement of the small bowel affected by chronic alcoholism. 285 4

Liver cell dysplasia (LCD) was found in 28 (60%) of 47 patients with hepatocellular carcinoma (HCC); 22 (79%) of them had associated liver cirrhosis. LCD was more frequently observed in posthepatitic cirrhosis (82%) than in the other forms. Carcinoembryonic antigen (CEA), alpha-1-antitrypsin (AAT) and alpha-fetoprotein (AFP), as demonstrated by the peroxidase-antiperoxidase method, were similarly expressed both in normal and in dysplastic cells. Hepatitis B surface antigen was found in eight cases (17%), six of which were associated with LCD. HBsAg was rarely found in dysplastic cells and frequently displayed a peculiar perinuclear pattern. The possible preneoplastic role of LCD is stressed.
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PMID:Liver cell dysplasia and hepatocellular carcinoma: a histological and immunohistochemical study. 298 89

We describe the simple and rapid enzyme immunoassay of protein C in human plasma with use of a Cobas Fara centrifugal analyzer. The antibody, labeled with horseradish peroxidase, is reacted with antigen (protein C) for 15 min. The peroxidase activity of the resulting antigen-antibody conjugate is measured at 500 nm for 5 min in the presence of excess H2O2, phenol, and 4-aminoantipyrine, as compared with that of free conjugates. Results are calculated from a stored standard curve and expressed as a percentage of the value determined for a pooled specimen of normal adult plasma. The standard curve is linear from 0% to 200%. The CV is generally less than 4% for different concentrations of protein C. In liver cirrhosis, hepatocellular carcinoma, therapy with warfarin, thrombosis, and disseminated intravascular coagulation, protein C concentrations are about 40-70% of normal. Results obtained with the present homogeneous enzyme immunoassay correlated well with those by enzyme-labeled immunosorbent assay (r = 0.97).
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PMID:Protein C in human plasma determined by homogeneous enzyme immunoassay with use of a centrifugal analyzer. 304 78

Liver biopsy specimens from patients positive for serum HBsAg reveal various expression patterns when properly stained by immunohistochemical techniques for the demonstration of HBsAg, HBcAg and HDAg. A negative staining for these three antigens seems to be associated with two conditions, i.e., self-limiting acute lobular hepatitis (ALH) or low amounts of intrahepatic antigens. The discrepancy between serum positivity and tissue negativity for HBsAg can be explained either by sampling error or by the higher sensitivity of the radioimmunoassay as compared with immunohistochemical methods. The use of amplification systems such as the avidin-biotin-peroxidase complex enhances the sensitivity of immunohistochemical peroxidase-antiperoxidase (PAP) techniques and makes it possible to detect very small amounts of both HBsAg and HBcAg in liver cells from paraffin-embedded tissue sections which had been negative with the conventional PAP technique. In cases with a positive staining for viral antigens, two main expression patterns (non-aggressive and aggressive) can be distinguished. The non-aggressive pattern is reflected in the HBcAg-free HBsAg-positive type (HBsAg carrier) or the generalized type of nuclear core (HBcAg carrier), while the aggressive pattern is reflected in the presence of HDAg, the presence of HDAg and HBcAg, the focal type of nuclear core or the cytoplasmic HBcAg. Superinfection of HBsAg carriers or switching from generalized to focal core, with or without cytoplasmic expression of HBcAg, results in transition from non-aggressive to aggressive pattern. The aggressive pattern occurs in association with histological features of chronic active hepatitis (CAH). When it occurs in ALH cases or in milder forms of chronic hepatitis, an evolution into CAH has to be expected. Features of severe CAH, eventually with cirrhosis, are found in association with two new expression patterns: the cytoplasmic core and the simultaneous presence of HBcAg and HDAg. When features of CAH are observed in liver tissue specimens with HBcAg-free HBsAg-positive type, the liver disease may be due to viral superinfection or to non-viral etiology, e.g., alpha 1-antitrypsin deficiency.
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PMID:Immunohistochemical techniques for the demonstration of viral antigens in liver tissue. 306 47

Immunolocalization of type III collagen and procollagen in cirrhotic human liver was studied using monoclonal antibody specific for the helical determinant of type III collagen extracted from human placenta. Deparaffinized, trypsin-treated cirrhotic liver sections from 8 autopsy cases were examined by the unlabeled peroxidase-antiperoxidase and immunofluorescence techniques. These techniques revealed the localization of this epitope shared by type III collagen and procollagen not only in the extracellular matrix of hepatocytes and sinusoidal cells but also in the cytoplasm. In hepatocellular carcinoma concurrent with cirrhosis, neoplastic cells were shown to react with this antibody as well. These results are consistent with data obtained using antiserum specific for bovine type III procollagen aminopeptide which appeared in our previous report.
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PMID:Immunolocalization of type III collagen and procollagen in cirrhotic human liver using monoclonal antibodies. 308 39

Immunocytochemical staining patterns for glial fibrillary acidic protein (GFAP) and S-100 protein (S100P) were compared in cerebral cortex, basal ganglia and white matter of eight cases with hepatic encephalopathy (HE), including four cases of Wilson's disease and four of liver cirrhosis, and of eight age-matched controls, using the peroxidase-antiperoxidase method on adjacent paraffin sections. The majority of Alzheimer type II glia (Alzg II) showed prominent immunoreactivity for S100P but not for GFAP, resembling normal astrocytes of protoplasmic type; Alzg II might be interpreted as being peculiar types of reactive astrocytes retaining characteristics of protoplasmic astrocytes. A small number of Alzg II cells showed slight perinuclear immunoreactivity for GFAP; some lacked both markers. This suggests a spectrum of metabolic changes in these two proteins in Alzg II. GFAP-positive Alzg II cells were restricted to basal ganglia and white matter adjacent to grey matter, indicating that expression of GFAP in Alzg II might be modulated by local factors. Alzheimer type I cells and Opalski cells in Wilson's disease were immunoreactive for both proteins, confirming their astroglial origin and different character from that of Alzg II. In morphometric comparison, the proportion of GFAP-positive glial cells decreased in the cortex (P less than 0.001) but not significantly in the white matter (0.05 less than P less than 0.1), confirming earlier data that the prominent reduction of GFAP in HE brains is restricted to the grey matter.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Glial fibrillary acidic protein and S-100 protein in human hepatic encephalopathy: immunocytochemical demonstration of dissociation of two glia-associated proteins. 372 31

Immunolocalization of type III procollagen (pro III) in normal and cirrhotic human liver was studied using rabbit antiserum specific for bovine type III procollagen aminopeptide. The material examined was deparaffinized, trypsin-treated hepatic tissue sections from 28 autopsy cases, including 19 cirrhotic and 9 normal liver donors. Immunostaining, performed by the unlabeled peroxidase-antiperoxidase antibody technique demonstrated that extracellular matrices corresponding to perisinusoidal reticulin, collagen in periportal areas, and blood vessel walls were the common sites of pro III antigenicity in both normal and cirrhotic liver. Moreover, in the cirrhotic liver, the fibrous septa of pseudolobules, and cytoplasm of hepatocytes and sinusoidal cells were positive when stained for pro III peptide. The differential counts of pro III positive cells in cirrhotic liver, however, revealed that the average ratio of these hepatocytes to sinusoidal cells was 25 to 1, indicating complete dominance of hepatocytes with respect to stainability for pro III peptide compared to sinusoidal cells. In hepatocellular carcinomas coexisting with cirrhosis, neoplastic cells also displayed pro III antigenicity. These data suggest that hepatocytes of cirrhotic liver and hepatocellular carcinoma cells play a significant role in type III collagen synthesis in vivo.
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PMID:Localization of type III procollagen aminopeptide antigenicity in hepatocytes from cirrhotic human liver. 393 61


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