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  • DKFZ Publication Database  (23)
  • DISEASE  (14)
  • immunohistochemistry  (13)
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  • DKFZ Publication Database  (23)
Keywords
  • 1
    Keywords: CANCER ; EXPRESSION ; SURVIVAL ; tumor ; CELL ; Germany ; human ; COHORT ; PROTEIN ; PROTEINS ; cell line ; TISSUE ; TUMORS ; LINES ; PATIENT ; FAMILY ; CARCINOGENESIS ; TISSUES ; CELL-LINES ; LESIONS ; PROGRESSION ; immunohistochemistry ; CELL-LINE ; LINE ; LOCALIZATION ; POLYMERASE-CHAIN-REACTION ; adenocarcinoma ; ADENOCARCINOMAS ; pathology ; OVEREXPRESSION ; cell lines ; pancreatic cancer ; protein expression ; chemoresistance ; SUBCELLULAR-LOCALIZATION ; SUBSET ; pancreas ; PANCREATIC-CANCER ; FAMILIES ; DUCTAL ADENOCARCINOMA ; polymerase chain reaction ; TUMOR TISSUE ; LEVEL ; analysis ; methods ; pancreatic ; RARE ; SURVIVAL-DATA ; Reverse Transcriptase Polymerase Chain Reaction
    Abstract: AIMS: To determine the role of two antiapoptotic proteins of the IAP family, cIAP1 and cIAP2, in human pancreatic carcinogenesis. METHODS: mRNA levels were measured in pancreatic tissues and pancreatic cancer cell lines by quantitative reverse-transcriptase polymerase chain reaction (QRT-PCR). Protein expression was assessed in pancreatic cancer cell lines by immunoblotting and in pancreatic tissues by immunohistochemistry and correlated with pathological and survival data. RESULTS: cIAP1 expression was constantly high in non-neoplastic pancreatic tissues, in PanIN lesions, as well as in a subset of primary and metastatic pancreatic ductal adenocarcinomas (PDAC), and a preferential cytoplasmatic localization was observed in the tumor tissues. cIAP1 expression was rare in a cohort of cystic tumors. cIAP2 mRNA levels were significantly higher (2.4 fold) in PDAC than in the normal tissues. cIAP2 protein was overexpressed in PDAC and was detectable in low-grade and high-grade PanIN lesions. Moreover, cIAP2 was frequently expressed in pancreatic cystic tumors. cIAP1 and cIAP2 mRNA and protein were detected in all the examined cell lines. Survival analysis revealed a shorter survival in patients with cIAP1/cIAP2-positive tumors. CONCLUSIONS: cIAP1 might contribute to the regulation of the apoptotic process in the normal and in the neoplastic pancreas, depending on its subcellular localization. cIAP2 overexpression is a frequent and early event in pancreatic cancer progression and could therefore potentially influence important pathophysiological aspects of PDAC, such as anoikis or chemoresistance
    Type of Publication: Journal article published
    PubMed ID: 16775116
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  • 2
    Keywords: RECEPTOR ; CANCER ; CANCER CELLS ; CELLS ; EXPRESSION ; GROWTH ; GROWTH-FACTOR ; CELL ; Germany ; TISSUE ; LINES ; TIME ; FAMILY ; INDUCTION ; TISSUES ; CONTRAST ; CELL-LINES ; DOWN-REGULATION ; MEMBER ; MEMBERS ; PHOSPHORYLATION ; BREAST-CANCER ; antibodies ; antibody ; immunohistochemistry ; ASSAY ; CARCINOMA CELLS ; CELL-LINE ; LINE ; CANCER-CELLS ; BETA ; RT-PCR ; adenocarcinoma ; p21 ; CELL-SURFACE ; RECEPTORS ; DIFFERENTIAL EXPRESSION ; cell lines ; pancreatic cancer ; CELL-GROWTH ; signaling ; PANCREATIC-CANCER ; FAMILIES ; DUCTAL ADENOCARCINOMA ; independent growth ; ENHANCED EXPRESSION ; TGF-beta 1 ; HEPARAN-SULFATE PROTEOGLYCANS ; LEVEL ; pancreatic ; ASSAYS ; SULFATE ; downregulation ; lymph node ; LYMPH-NODE ; correlation ; VIEW ; DECREASED SURVIVAL ; activin ; bone morphogenic protein ; CONTROLS CELLULAR-RESPONSES ; glypican ; heparan sulfate proteoglycans ; SMAD PROTEINS
    Abstract: Glypican 1 (GPC1) is a cell surface heparan sulfate proteoglycan that acts as a co-receptor for heparin-binding growth factors as well as for members of the TGF-beta family. GPC1 plays a role in pancreatic cancer by regulating growth factor responsiveness. In view of the importance of members of the TGF-beta family in pancreatic cancer, in the present study, the role of GPC1 in TGF-beta, BMP and activin signaling was analyzed. Quantitative RT-PCR and immunohistochemistry were utilized to analyze GPC1 and TGF-beta, BMP and activin receptor expression levels. Panc-1 and T3M4 pancreatic cancer cells were transfected in a stable manner with a GPC1 antisense expression construct. Anchorage-dependent and -independent growth was determined by MTT and soft agar assays. TGF-beta 1, activin-A and BMP-2 responsiveness was determined by MTT assays and immunoblotting with p21, p-Smad1, and p-Smad2 antibodies. QRT-PCR demonstrated increased GPC1 mRNA levels in pancreatic ductal adenocarcinoma (PDAC) compared to normal pancreatic tissues (NPT), as described previously. There was a significant correlation between GPC1 mRNA levels and T beta RII, act-R1a, act-R1b, act-R2a, BMP-R1a, and BMP-R2 mRNA expression in NPT. In contrast, GPC1 mRNA expression correlated directly with act-R1a and BMP-R1a in NO PDAC cases and with act-R2a and BMP-R1a in lymph node positive cases. Down-regulation of GPC1 resulted in increased doubling time in Panc-1 but not in T3M4 cells, and decreased anchorage-independent growth in both cell lines. GPC1 down-regulation resulted in a slightly altered response towards TGF-beta 1, activin-A and BMP-2 in terms of growth, p21 induction and Smad2 phosphorylation. In conclusion, enhanced GPC1 expression correlates with BMP and activin receptors in pancreatic cancer. GPC1 down-regulation suppresses pancreatic cancer cell growth and slightly modifies signaling of members of the TGF-beta family of growth factors
    Type of Publication: Journal article published
    PubMed ID: 17016645
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  • 3
    Keywords: EXPRESSION ; COMBINATION ; Germany ; MODEL ; DIAGNOSIS ; DISEASE ; DISTINCT ; PROTEIN ; PROTEINS ; SAMPLE ; SAMPLES ; PATIENT ; SERA ; MARKER ; BIOMARKERS ; FORM ; IDENTIFICATION ; PROGRESSION ; PATTERNS ; DIFFERENCE ; ARRAYS ; mass spectrometry ; MASS-SPECTROMETRY ; EXCHANGE ; MULTIVARIATE ; adenocarcinoma ; sensitivity ; specificity ; REVEALS ; expression profiling ; AFFINITY ; chronic pancreatitis ; protein expression ; PROTEOMICS ; MASSES ; SERUM ; pancreas ; PATTERN ; ARRAY ; PANCREATITIS ; HEALTHY-VOLUNTEERS ; pancreolauryl test ; biomarker ; analysis ; methods ; USA ; SELDI-TOF-MS ; SET ; diagnostic marker ; NOV ; LASER-DESORPTION ; serum proteomics ; STAGE OVARIAN-CANCER ; TUMOR-MARKERS
    Abstract: Objective: Testing of serum for protein patterns to monitor progression of suspected to definite chronic pancreatitis (CP). Methods: Serum samples of CP patients and healthy volunteers were fractionated on anion exchange columns and analyzed by surface-enhanced laser desorption/ionization-time-of-flight mass spectrometry to elucidate CP-related protein alterations and to identify biomarkers for this disease. Potential biomarkers were purified and identified by mass spectrometry. Results: In total, 258 protein peaks were found that discriminated between the 2 groups. Analysis revealed 28 most prominent peaks on immobilized metal affinity capture coupled with Cu and CM10 protein chips, covering the m/z range between 3.3 and 33.3 kd. Performing multivariate pattern analysis, the best pattern model was obtained using fraction 6 on immobilized metal affinity capture coupled with Cu arrays with a sensitivity of 96% and a specificity of 84%. Using a combination of matrix-assisted laser desorption-ionization-time-of- flight mass spectrometry and immunodepletion, we identified 14-m/z peaks. The proteins were found to be significantly decreased in CP serum and were identified as retinol-binding protein, serum amyloid-alpha, apolipoprotein A-II (Apo A-II), Apo C-I, Apo C-II, Apo C-III, and transthyretin and truncated forms thereof. Conclusions: Distinct protein profile differences exist between normal and CP serum and reflect the metabolic and inflammatory condition in CP patients. The identified protein panel may eventually serve as a diagnostic marker set for CP
    Type of Publication: Journal article published
    PubMed ID: 18090239
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  • 4
    Keywords: CANCER ; SURVIVAL ; tumor ; Germany ; DEATH ; DISEASE ; MORTALITY ; NEW-YORK ; PROTEIN ; SURGERY ; TIME ; PATIENT ; IMPACT ; prognosis ; NO ; PERFORMANCE ; PROGRESSION ; DIFFERENCE ; COUNTRIES ; RATES ; DATABASE ; RESECTION ; adenocarcinoma ; PREVALENCE ; pancreatic cancer ; MULTICENTER ; pancreas ; PANCREATIC-CANCER ; WEIGHT ; LEVEL ; methods ; GASTROINTESTINAL CANCER ; USA ; CURATIVE RESECTION ; ANOREXIA ; cachexia ; ENERGY-EXPENDITURE ; HEMOGLOBIN ; DEATHS ; HEAD RESECTION ; nutritional status ; UBIQUITIN-DEPENDENT PROTEOLYSIS
    Abstract: Introduction Pancreatic cancer is the fourth leading cause of cancer-related death in Western countries with a poor prognosis (5-year survival rates, 25% in patients after tumor resection with adjuvant treatment; overall, the 5-year survival rate is about 4%; Jemal et al., CA Cancer J Clin, 55:10-30, 2005). Many patients develop a cachectic status during the progression of the disease, and this syndrome accounts for up to 80% of deaths in patients with advanced pancreatic cancer. Remarkably, there are only a few data available on the impact of cachexia in patients with pancreatic cancer scheduled for tumor resection. Material and Methods Therefore, in this study, 227 consecutive patients with ductal adenocarcinoma of the pancreas were documented over an 18-month period regarding the prevalence of cachexia and its influence on perioperative morbidity and mortality with a special interest to postoperative weight gain and survival in a prospectively designed database and followed up. Results In 40.5% of the patients, cachexia was already present at the time of operation. The cachectic patients did present in a worse nutritional status, represented by lower protein, albumins, and hemoglobin levels. Despite no significant differences in tumor size, lymph node status, and CA19-9 levels, the resection rate in patients with cachexia was reduced (77.8% vs. 48.9%) due to a higher rate of metastatic disease in patients with cachexia. The morbidity and in-hospital mortality revealed no significant difference. However, patients with and without cachexia lost weight after operation, and the weight gain started not until 6 months after operation. The survival in patients with cachexia was significantly reduced in patients undergoing tumor resection as well as in palliative treated patients. Conclusion Cachexia has a significant impact on survival and performance status in palliative patients as well as in patients operated for pancreatic cancer. But tumor-related cachexia is not necessarily dependent on tumor size or load and that metastatic dedifferentiation of the tumor might be a critical step in the development of tumor-associated cachexia
    Type of Publication: Journal article published
    PubMed ID: 18347879
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  • 5
    Keywords: CANCER ; INVASION ; tumor ; carcinoma ; evaluation ; Germany ; CT ; DIAGNOSIS ; FOLLOW-UP ; SPIRAL CT ; TOOL ; DISEASE ; TUMORS ; computed tomography ; RESOLUTION ; PATIENT ; primary ; NO ; METASTASIS ; adenocarcinoma ; COMPUTED-TOMOGRAPHY ; sensitivity ; specificity ; VESSELS ; QUESTIONNAIRE ; pancreatic carcinoma ; HELICAL CT ; HYDRO-CT ; methods ; ROW CT ; CURVED PLANAR REFORMATIONS ; invasion score ; MULTISLICE SPIRAL CT ; resectability ; VASCULAR INVASION
    Abstract: Objective: It was the aim of this study to evaluate a new infiltration score to determine the resectability of pancreatic carcinomas in preoperative planning. Materials and Methods: Eighty patients with suspected pancreatic tumor were examined prospectively using 16-row spiral CT. The scans were evaluated for the presence of pancreatic carcinoma, peripancreatic tumor extension and vascular invasion using a standardized questionnaire. Invasion of the surgically relevant vessels was evaluated using a new invasion score. The operative and histological findings and the clinical follow-up served as the gold standard. Results: Forty patients had a pancreatic carcinoma, 5 had metastasis of a different primary tumor, and in 35 patients, there was no malignant pancreatic disease. The sensitivity for tumor detection was 100%, with a specificity of 88% for differentiating between malignant and benign pancreatic tumors. Invasion of the surrounding vessels was evaluated correctly using the invasion score, with a sensitivity of 89% and a specificity of 99%. In evaluation of resectability, a sensitivity of 94% and a specificity of 89% were achieved. Conclusion: Using 16-row spiral CT, the invasion score is a valid tool for correctly assessing invasion in relevant vessels in cases of pancreatic carcinoma and for determining resectability. Copyright (C) 2008 S. Karger AG, Basel and IAP
    Type of Publication: Journal article published
    PubMed ID: 18434758
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  • 6
    Keywords: CANCER ; CANCER CELLS ; CELLS ; EXPRESSION ; tumor ; CELL ; Germany ; human ; DISTINCT ; GENES ; HYBRIDIZATION ; PROTEIN ; SAMPLE ; SAMPLES ; transcription ; TISSUE ; TUMORS ; COMPLEX ; COMPLEXES ; primary ; renal ; colon ; RATS ; TISSUES ; CONTRAST ; DOWN-REGULATION ; BREAST ; BREAST-CANCER ; IDENTIFICATION ; IN-SITU ; immunohistochemistry ; MALIGNANCIES ; UP-REGULATION ; BRCA1 ; metastases ; CANCER-CELLS ; COLON-CANCER ; LOCALIZATION ; RT-PCR ; TRACT ; RECEPTORS ; pancreatic cancer ; chronic pancreatitis ; protein expression ; HUMAN TISSUES ; F ; in situ hybridization ; colon cancer ; TGF-BETA ; gastric cancer ; MAC30 ; PRIMARY TUMORS
    Abstract: Meningioma-associated protein, MAC30, is a protein with unknown function and cellular localization that is differentially expressed in certain malignancies. In the present study, the expression of MAC30 in a variety of normal and cancerous human gastrointestinal tissues, with special emphasis on pancreatic tissues was analyzed. Quantitative RT-PCR was utilized to compare MAC30 expression levels. In situ hybridization and immunohistochemistry were carried out to localize MAC30 mRNA and protein expression in normal and cancerous tissue samples of the esophagus, stomach, colon and pancreas. Furthermore, the effects of TGF-beta on the transcription of MAC30 mRNA were examined in pancreatic cancer cells. MAC30 mRNA was expressed in a wide variety of normal human tissues, being most abundant in testicular and gastric tissue samples. MAC30 mRNA levels were significantly increased in breast and colon cancer, but significantly decreased in pancreatic and renal cancer. TGF-beta down-regulated MAC30 mRNA levels in certain pancreatic cancer cells. MAC30 protein was localized in normal pancreatic tissues, mainly in acinar and islet cells, and in normal colon, gastric and esophageal tissues especially in the mucosal cells. MAC30 was strongly present in tubular complexes in pancreatic cancer tissues but weak to absent in pancreatic cancer cells of primary tumors and metastases. In contrast, esophageal, gastric and colon tumors displayed strong MAC30 immunoreactivity in the cancer cells. In conclusion, MAC30 is expressed in various normal and diseased human tissues. MAC30 up-regulation in certain tumors and down-regulation in others suggests that this protein plays a distinct role in human malignancies
    Type of Publication: Journal article published
    PubMed ID: 15375745
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  • 7
    Keywords: APOPTOSIS ; CANCER ; CANCER CELLS ; CELLS ; EXPRESSION ; GROWTH ; INVASION ; proliferation ; SURVIVAL ; tumor ; carcinoma ; CELL-PROLIFERATION ; Germany ; human ; FOLLOW-UP ; DISEASE ; liver ; PROTEIN ; MOLECULES ; TISSUE ; TUMORS ; TIME ; PATIENT ; MARKER ; DONOR ; prognosis ; TISSUES ; MOLECULE ; BREAST-CANCER ; GLYCOPROTEIN ; IDENTIFICATION ; MALIGNANCIES ; METASTASIS ; metastases ; PCR ; CANCER-CELLS ; ADHESION ; MIGRATION ; CANCER-PATIENTS ; adenocarcinoma ; LIVER METASTASES ; CANCER PATIENTS ; HEALTHY ; pancreatic cancer ; chronic pancreatitis ; SERUM ; ELISA ; MALIGNANCY ; RECOMBINANT ; PANCREATIC-CANCER ; TUMOR-GROWTH ; DUCTAL ADENOCARCINOMA ; INCREASE ; extracellular matrix ; REAL-TIME ; cell adhesion ; cell proliferation ; LEVEL ; OSTEOPONTIN ; SERUM-LEVELS ; downregulation ; function ; BLOCKADE ; IMMUNOHISTOCHEMICAL ANALYSIS ; INVASIVENESS ; lymph node ; LYMPH-NODE ; PLASMA OSTEOPONTIN ; restricting ; serum marker
    Abstract: Pancreatic ductal adenocarcinoma ( PDAC) is one of the most aggressive malignancies, with an overall 5-year survival rate of less than 5%. Invasive tumor growth and early metastasis are two important reasons for this dismal prognosis. Osteopontin ( OPN) is a secretory protein with a variety of functions, for example in cell adhesion and migration, inflammatory reaction and apoptosis. In this study the functional role of OPN in human pancreatic cancer and its potential use as a disease marker were analyzed. By real time quantitative PCR, there was a 2.2- fold and 1.6- fold increase of OPN mRNA in pancreatic cancers (n = 23) and chronic pancreatitis samples (n = 22), respectively, compared to normal pancreatic tissues (n = 20). Immunohistochemical analysis demonstrated OPN staining in 60% of the primary pancreatic tumors and in 72% of the lymph node and liver metastases. ELISA analysis of serum samples obtained from pancreatic cancer patients (n = 70), chronic pancreatitis patients (n = 12), and healthy donors (n = 20) showed a 1.6-fold increase in OPN serum levels in patients with tumors and a 1.9-fold increase in patients with chronic pancreatitis. Recombinant human OPN significantly increased the invasiveness of pancreatic cancer cells, without having any impact on cell proliferation. In addition, downregulation of OPN by specific siRNA molecules decreased pancreatic cancer cell invasion. In conclusion, OPN serum levels in pancreatic cancer and chronic pancreatitis patients are not significantly different, thereby restricting its role as a prognostic or follow-up marker. Our results do suggest, however, that blockade of OPN might be useful as a therapeutic approach to inhibit invasion and metastasis of pancreatic cancer cells
    Type of Publication: Journal article published
    PubMed ID: 15970685
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  • 8
    Keywords: CANCER ; CANCER CELLS ; CELLS ; EXPRESSION ; GROWTH ; tumor ; carcinoma ; FACTOR RECEPTOR ; Germany ; GENES ; HYBRIDIZATION ; microarray ; PROTEIN ; TISSUE ; MICE ; TIME ; PATIENT ; COMPLEX ; COMPLEXES ; DONOR ; DOMAIN ; TISSUES ; 5-FLUOROURACIL ; TRANSPORT ; IN-SITU ; LESIONS ; immunohistochemistry ; MALIGNANCIES ; ASSAY ; UP-REGULATION ; PROSTATE-CANCER ; NUDE-MICE ; chemotherapy ; CANCER-CELLS ; LOCALIZATION ; adenocarcinoma ; sensitivity ; CISPLATIN ; MICROARRAY ANALYSIS ; OVEREXPRESSION ; expression profiling ; microdissection ; pancreatic cancer ; REGULATOR ; chronic pancreatitis ; CELL-GROWTH ; in situ hybridization ; MALIGNANCY ; GEMCITABINE ; PANCREATIC-CANCER ; DUCTAL ADENOCARCINOMA ; INCREASE ; independent growth ; TRANSFECTION ; ENHANCED EXPRESSION ; LEVEL ; ASSAYS ; downregulation ; PROLIFERATIVE ACTIVITY ; CHLORIDE ; chloride channel ; COLO-357 CELLS ; DECREASED SURVIVAL ; NA+/K+-ATPASE ; TGF-BETA RESPONSIVENESS ; TGFP
    Abstract: The expression and localization of FXYD domain containing ion transport regulator 3 (FXYD3), a transmembrane protein that acts as a chloride channel or chloride channel regulator, was analyzed in pancreatic tissues derived from donors and patients suffering from chronic pancreatitis (CP) or pancreatic ductal adenocarcinoma (PDAC) as well as in pancreatic cancer cells using QRT-PCR, laser-capture microdissection and microarray analysis, in situ hybridization and immunohistochemistry. FXYD3 antisense expressing T3M4 pancreatic cancer cells were generated and compared to control cells using anchorage-dependent and independent growth assays, and xenotransplantation into nude mice. FXYD3 mRNA levels were 3.4-fold increased in PDAC tissues compared to donor specimens (p = 0.006), and 3.9-fold increased in microdissected cancer cells compared to normal pancreatic ductal cells (p = 0.02). FXYD3 was localized in the tubular complexes and PanIN lesions of both CP and PDAC, as well as in pancreatic cancer cells. Downregulation of FXYD3 by stable antisense transfection increased significantly the doubling time of T3M4 pancreatic cancer cells from 44 +/- 2 hr to 55 +/- 12 hr (p = 0.02). Nude mice transplanted with antisense transfected cells displayed a significant increase in tumor doubling time from 3.3 days +/- 1.0 to 4.3 days +/- 0.43 (p = 0.058). Anchorage-independent growth and sensitivity to 5-fluorouracil, gemcitabine and cisplatin as well as to MgCl2 were not dependent on the level of FXYD3 expression. In conclusion, overexpression of FXYD3 in pancreatic cancer may contribute to the proliferative activity of this malignancy. (c) 2005 Wiley-Liss, Inc
    Type of Publication: Journal article published
    PubMed ID: 16003754
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  • 9
    Keywords: CELLS ; tumor ; CELL ; Germany ; neoplasms ; imaging ; TOOL ; DISEASE ; DISEASES ; RESOLUTION ; SURGERY ; MECHANISM ; MARKER ; prognosis ; AUTOIMMUNE-DISEASE ; mechanisms ; T cell ; T cells ; T-CELL ; T-CELLS ; treatment ; MARKERS ; RESECTION ; LOCALIZATION ; HEAD ; ATROPHY ; FUTURE ; DIABETES-MELLITUS ; AUTOANTIBODIES ; autoimmune pancreatitis ; PRIMARY SCLEROSING CHOLANGITIS ; SJOGRENS-SYNDROME ; INFLAMMATORY-BOWEL-DISEASE ; FEATURES ; fibrosis ; INFILTRATION ; inflammatory bowel disease ; AUTOIMMUNE-DISEASES ; STENOSIS ; LEVEL ; pancreatic ; MASS ; autoimmune disease ; TOOLS ; DUCT ; serological ; Diabetes Mellitus ; surgical resection ; BOWEL ; EFFECTIVE STEROID-THERAPY ; ENTITY ; IgG4 ; pancreatic neoplasms ; pancreatic tumor ; PSEUDOTUMOROUS PANCREATITIS ; SERUM IGG4 ; steroids ; URSODEOXYCHOLIC ACID
    Abstract: The term autoimmune pancreatitis (AIP) describes a nonalcoholic, chronic lymphoplasmocytic pancreatitis. The lymphoplasmocytic infiltration is characterized by periductal localization of predominantly CD4-positive T cells, fibrosis, and acinar atrophy, frequently resulting in stenosis of the main pancreatic and distal common bile ducts. Imaging studies often reveal a diffuse narrowing of the pancreatic main duct and swelling of the pancreatic head wrongly suggesting the presence of a malignant tumor. Clinical signs include mild abdominal pain,jaundice, recurrent episodes of acute pancreatitis, and even new-onset diabetes mellitus. Additionally, AIP can be associated with other autoimmune diseases such as Sjogren's syndrome, primary sclerosing cholangitis, chronic inflammatory bowel diseases, and retroperitoneal fibrosis. Serological markers include autoantibodies and increased levels of gamma globulin and especially IgG4. Steroids seem to be effective in improving clinical symptoms as well as in the resolution of pancreatic and bile duct narrowing. This distinguishes AIP from other forms of pancreatitis and from pancreatic neoplasms. Further studies of the underlying pathophysiologic mechanisms, prognosis, and new diagnostic tools are needed to provide adequate and effective treatment in the future. In this article, we summarize the current knowledge about AIP and present 17 cases that underwent surgical resection at our institution from 2003 to 2004
    Type of Publication: Journal article published
    PubMed ID: 17007063
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  • 10
    Keywords: INHIBITOR ; Germany ; DISEASE ; RISK ; SITE ; GENE ; GENES ; PROTEIN ; ACTIVATION ; CLEAVAGE ; MUTATION ; genetics ; MUTATIONS ; Jun ; INDIVIDUALS ; heredity ; chronic pancreatitis ; RECOMBINANT ; pancreas ; VARIANT ; ENZYME ; pancreatic ; LOSSES ; odds ratio ; PROTECTS ; HEREDITARY PANCREATITIS ; HUMAN CATIONIC TRYPSINOGEN
    Abstract: Chronic pancreatitis is a common inflammatory disease of the pancreas. Mutations in the genes encoding cationic trypsinogen (PRSS1) 1 and the pancreatic secretory trypsin inhibitor (SPINK1) 2 are associated with chronic pancreatitis. Because increased proteolytic activity owing to mutated PRSS1 enhances the risk for chronic pancreatitis, mutations in the gene encoding anionic trypsinogen (PRSS2) may also predispose to disease. Here we analyzed PRSS2 in individuals with chronic pancreatitis and controls and found, to our surprise, that a variant of codon 191 (G191R) is overrepresented in control subjects: G191R was present in 220/6,459 (3.4%) controls but in only 32/2,466 (1.3%) affected individuals (odds ratio 0.37; P = 1.1 x 10(-8)). Upon activation by enterokinase or trypsin, purified recombinant G191R protein showed a complete loss of trypsin activity owing to the introduction of a new tryptic cleavage site that renders the enzyme hypersensitive to autocatalytic proteolysis. In conclusion, the G191R variant of PRSS2 mitigates intrapancreatic trypsin activity and thereby protects against chronic pancreatitis
    Type of Publication: Journal article published
    PubMed ID: 16699518
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