Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0149521 (chronic pancreatitis)
 7,199 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Expression of intermediate filaments (IF) is regulated during development and differentiation. The authors have studied the expression of vimentin and cytokeratins (CK) 4, 7, 8, 13, 18, 19 in normal pancreas, chronic pancreatitis, and pancreas cancer using monoclonal antibodies. Immunohistochemical assays were performed on fresh frozen tissue sections and on cultured pancreas cancer cells using the streptavidin-peroxidase method. In normal pancreas, acinar cells expressed CK 8 and 18, whereas ductal cells expressed CK 7, 8, 18, and 19. CK 4 was expressed by 5-10% of pancreas duct cells in all specimens of normal pancreas. CK 13 was not detected in any epithelial cells of normal pancreas or pancreatitis. CK 7, 8, 18, and 19 were homogeneously expressed in all pancreas cancers, whereas CK 4 was expressed only in 5-50% of cells in 10/16 tumors. Foci of squamous metaplasia expressed CK 13 but showed partial loss of expression of CK 7, 8, 18, and 19. Thirteen pancreas cancer cell lines examined showed homogeneous expression of CK 7, 8, 18, and 19; 2/11 lines expressed CK 4 weakly, and 6/11 expressed vimentin. CK 13 was not detected in any of the lines. These results indicate that pancreas cancer cells consistently express cytokeratin polypeptides characteristic of ductal epithelial cells and that this phenotype is retained in pancreas cancer cell lines. In addition, squamous metaplasia is associated with a coordinate change in the expression of CK polypeptides.
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PMID:Intermediate filaments as differentiation markers of normal pancreas and pancreas cancer. 137 55

A monoclonal antibody designated RWP1.1 was produced against a human pancreatic carcinoma cell line RWP1. This antibody was shown to recognize an epitope of carcinoembryonic antigen. The reactivity of the antibody was evaluated on formalin-fixed normal tissues, 86 malignant neoplasms, 10 colonic polyps, and 6 cases of chronic pancreatitis using the peroxidase anti-peroxidase technique. RWP1.1 did not react with normal tissues apart from weak staining of fetal pancreatic ducts. This antibody preferentially reacted with primary and metastatic adenocarcinomas of the colon, stomach, pancreas, and colonic polyps but not with most adenocarcinomas from other sites nor with other types of tumors or cases of chronic pancreatitis. It also reacted with colon adenocarcinomas on frozen sections. The restricted specificity of this antibody could be used in differentiating gastrointestinal adenocarcinomas from other types of tumors including adenocarcinomas from other sites and most pancreatic adenocarcinomas from chronic pancreatitis.
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PMID:Monoclonal antibody to a human pancreatic carcinoma cell line recognizes gastrointestinal neoplasms. 246 6

The ductular accumulation of "abnormal mucus" is the key histologic feature in cystic fibrosis. This material is periodic acid-Schiff positive and diastase resistant, suggesting that it is glycoprotein in nature. We used the avidin-biotin-peroxidase method to identify this material using antibodies to the serum glycoproteins carcinoembryonic antigen, alpha 1-antitrypsin, and alpha-fetoprotein on paraffin sections of pancreas obtained from a total of 21 patients: 9 with cystic fibrosis, 5 with chronic pancreatitis, and 7 controls. The control patients had normal pancreatic histologic findings, no alpha 1-antitrypsin or alpha-fetoprotein was demonstrated, and only the ductular epithelium reacted weakly for carcinoembryonic antigen. The pancreas in pancreatitis showed fibrosis, acinar atrophy, and ectasia of the ducts that contained only a small amount of periodic acid-Schiff-positive material. This material reacted weakly for carcinoembryonic antigen and alpha 1-antitrypsin. The appearance of the pancreas in cystic fibrosis was similar to that in chronic pancreatitis. However, the ducts contained a greater amount of periodic acid-Schiff-positive material, mostly in the form of globules that reacted strongly for carcinoembryonic antigen and alpha 1-antitrypsin and weakly for alpha-fetoprotein, as did the ductular epithelium. This study shows that the periodic acid-Schiff-positive material in cystic fibrosis contains at least the three serum glycoproteins and that the accumulation may represent a possible defect in cellular synthesis, assembly, or transport of glycoproteins in the ducts.
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PMID:Carcinoembryonic antigen, alpha 1-antitrypsin, and alpha-fetoprotein in the pancreas of patients with cystic fibrosis. 247 7

A retrospective analysis of 25 primary adenocarcinomas of the pancreas, 16 metastatic pancreatic tumors, 8 cases of chronic pancreatitis, and 3 adult normal pancreas was performed to ascertain the reactivity of monoclonal antibody (MAb) B72.3 to malignant and nonneoplastic pancreatic lesions. Formalin-fixed, paraffin-embedded sections of pancreas were evaluated by immunohistochemical techniques (avidin-biotin-peroxidase complex [ABC] method). Twenty-one of 25 malignant primary tumors were reactive, and all 16 metastatic sites expressed the B72.3 antigen. In contrast, all cases of pancreatitis and normal pancreas were either weakly reactive or nonreactive. Ten malignant and two benign pancreatic fine-needle aspirates provided results similar to those seen with fixed tissues. Because MAb B72.3 has selective reactivity for primary and metastatic pancreatic cancer, it may be of value as a diagnostic adjunct in cytologic examination or for radioimmunodetection of regional and/or distant metastases of adenocarcinoma of the pancreas.
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PMID:A tumor-associated antigen in carcinoma of the pancreas defined by monoclonal antibody B72.3. 327 79

Lectin peroxidase histochemical analysis was carried out on pancreatic tissue from patients with pancreatic carcinoma and chronic pancreatitis and from subjects with normal pancreas to find a tumour specific pattern of lectin binding that would aid histological and cytological diagnosis. There were striking differences between the lectin binding characteristics of the different cell types in the normal pancreas. Acinar cells were uniformly positive for binding with wheat germ agglutinin and soy bean agglutinin while islet cells were usually negative for these lectins. Ulex europaeus I lectin however, was found not to be specific for endothelium, showing positivity also for acinar and ductal tissue. Griffonia simplicifolia II lectin was found to be highly specific for ductal epithelium, and because of this was tested in a hamster pancreatic cancer model where it was not specific for ductal epithelium, reflecting differing carbohydrate expression in the hamster pancreas. Pancreatic carcinomas and chronic pancreatitis bound all five lectins without any qualitative distinction from each other or from normal pancreatic tissue, but there was increased intensity of peanut agglutinin binding to secreted mucins in pancreatic carcinoma, which may be of potential use in radiolabelled lectin scanning.
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PMID:Use of lectin histochemistry in pancreatic cancer. 328 74

For the quantitative measurement of pancreatic oncofetal antigen (POA), an enzyme immunoassay for POA has been developed, and is based on the sandwich method using antibody-coupled glass beads and enzyme (peroxidase)-labelled antibody. Serum POA concentrations were increased significantly in patients with pancreatic cancer, but not in those with chronic pancreatitis or other miscellaneous diseases, or in normal subjects. It is concluded that the enzyme immunoassay could be used for the assay of POA and our results show that the determination of serum POA would be useful in the diagnosis of pancreatic cancer.
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PMID:Enzyme immunoassay of pancreatic oncofetal antigen (POA) as a marker of pancreatic cancer. 388 88

Phospholipase A2 was localized with peroxidase anti-peroxidase (PAP)-technique in pancreatic tissue resected from normal portions of tumor-bearing glands of 4 patients and from pancreases of 16 patients suffering from either acute or chronic pancreatitis. In acute pancreatitis the enzyme immunoreactivity was detected in the apical zymogen granule portion of acinar cells and in ductal secretory material similarly as in normal tissue. At the border of necrotic and non-necrotic exocrine parenchyma the staining reaction was evenly dispersed throughout the cytoplasm or localized in small cell fragments. There was no reaction in necrotic acinar cell remnants. Some dilated acinar lumina contained intensively stained plugs. Fat necroses were stained but surrounding neutrophil leukocytes were unstained. Thrombosed small vessels were also unstained. In chronic pancreatitis, diminished staining characterized small acinar cells at the border of lobules. Some macrophages stained positively. It was concluded that during acute inflammation in pancreas, localization of phospholipase A2 in pancreatic tissue is abnormal, and that phospholipases A2 of neutrophil leukocytes and platelets are not crossreactive with the secretory enzyme.
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PMID:Immunohistochemical localization of phospholipase A2 in human pancreas in acute and chronic pancreatitis. 634 33

Immunoreactive trypsin was localized with the peroxidase-antiperoxidase technique in normal human pancreatic tissue and in the glands of patients suffering from acute or chronic pancreatitis. In the normal pancreas and in the histologically normal areas of the inflamed pancreas, trypsin was detected in the zymogen granules of acinar cells and in ductal secretory material. During acute pancreatitis, three characteristic changes were observed: (1) separate acinar cell fragments in early lesions; (2) decreased and evenly dispersed staining in necrotic acinar cells, and (3) intensive reaction in plugs in acinar lumina in advanced lesions. In chronic pancreatitis, the localization of trypsin in acinar cells was similar to that in normal pancreas. Some proteinaceous plugs in dilated pancreatic ducts were weakly immunoreactive. The results show that the tissue distribution of immunoreactive trypsin is altered in acute pancreatitis.
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PMID:Immunohistochemical localization of trypsinogen and trypsin in acute and chronic pancreatitis. 635 76

The c-fos gene product is a 55 kd nuclear protein bound to a cellular protein, p39. Expression of the c-fos oncogene is complex in that increased expression occurs in cultured cells during undifferentiated growth but decreased during terminal differentiation. We studied c-fos gene expression by streptavidin-biotin-peroxidase immunohistochemistry in pancreatic adenocarcinoma (N = 20), chronic pancreatitis (N = 9) and normal pancreas (N = 5). One islet cell tumour was included in the study. There was positive staining for c-fos oncoprotein in 15 of the 20 (75%) adenocarcinomas examined (9/12 moderate to poorly differentiated, 6/8 poorly differentiated). The single islet cell tumour investigated was also positive. Only 2 of 9 (22%) cases of chronic pancreatitis and 2 of 5 (40%) normal pancreata were positive. Stromal immunoreactivity was noted in all cancer cases while 5 of 9 (56%) chronic pancreatitis and 3 of 5 (60%) normal pancreas cases showed such staining. In conclusion, c-fos oncoprotein overexpression occurs more frequently in pancreatic cancers compared to chronic pancreatitis and normal pancreas. These findings are consistent with in vitro cell line studies of other cancers which showed increased expression of c-fos during undifferentiated growth.
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PMID:Immunohistochemical localisation of the c-fos oncoprotein in pancreatic cancers. 794 35

Aberrant c-Src protein kinase activation has been identified as one of the molecular alterations involved in human pancreatic carcinogenesis. It has been postulated that c-Src may induce transformation by causing the overexpression of the insulinlike growth factor-1 receptor (IGF-1R) in pancreatic tumor cell lines. To further study the interaction between c-Src and IGF-1R proteins in human pancreatic cancer, we examined their coexpression in 47 human pancreatic ductal adenocarcinomas (PDA). Formalin-fixed, paraffin-embedded sections from 47 cases of PDA were stained using the immunohistochemical avidin-biotin-peroxidase method. We used an anti-human IGF-1R mouse monoclonal antibody (dilution 1:100 with antigen retrieval), and an anti-c-Src mouse monoclonal antibody (dilution 1:100 with antigen retrieval). The stains were semiquantitatively evaluated using the Allred score system, assessing intensity of stain and percentage of positive tumor cells. High cytoplasmic c-Src expression (Allred score 7-8) was seen in 33/47 (70%) tumors. In only 4 cases was c-Src either negative or low (Allred score 3). Strong and diffuse membranous IGF-1R stain (Allred score 7-8) was identified in 30/47 (64%) tumors. IGF-1R staining was low (Alled score 2-4) in 2 cases and negative in 1. Interestingly, in 40/47 (85%) cases c-Src and IGF-1R stains had similar scores. An inverse staining pattern was detected in only 6/47 (13%) tumors. Normal pancreatic ducts as well as areas of chronic pancreatitis were negative for IGF-1R. In conclusion, our data support the role of IGF-1R and c-Src in human pancreatic carcinogenesis; the coexpression of both these molecules may play an important role in transformation of pancreatic ductal cells.
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PMID:Coexpression of IGF-1R and c-Src proteins in human pancreatic ductal adenocarcinoma. 1462 43


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