Crosslinked fibrin derivatives and fibronectin in ascitic fluid from patients with ovarian cancer compared to ascitic fluid in liver cirrhosis

Hafter, R.; Klaubert, W.; Gollwitzer, Rotraut; Hugo, R. von; Graeff, H.

doi:10.1016/0049-3848(84)90312-8

Cited by 30 publications

(10 citation statements)

References 17 publications

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“…The comparison of plasma and ascitic fibronectin gradient and ratio, unlike the isolated measurement of each one, did not show any difference between groups, indicating that changes in plasma and ascitic fluid levels of fibronectin are related. These observations corroborate the findings of Hafter et al (23) that plasma fibronectin is the main factor determining the levels of this glycoprotein in ascitic fluid. The present data show that fibronectin concentrations may be used as a risk indicator for SBP in cirrhotic patients.…”

Section: Group Isupporting

confidence: 82%

Fibronectin in the ascitic fluid of cirrhotic patients: correlation with biochemical risk factors for the development of spontaneous bacterial peritonitis

Mesquita

Leite-Mor²,

Parise³

1997

Braz J Med Biol Res

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Cirrhotic patients (23 with alcoholic cirrhosis, 5 with posthepatitic cirrhosis and 2 with cryptogenic cirrhosis) with ascites and portal hypertension were studied and divided into two groups corresponding to high or low risk to develop spontaneous bacterial peritonitis (SBP) related to the concentration of total protein in the ascitic fluid (A-TP): group I (high risk): A-TP≤1.5 g/dl and group II (low risk): A-TP>1.5 g/dl. Fibronectin (FN), C3 and C4 concentrations were measured by radial immunodiffusion while total protein was measured by the biuret method. The mean values (group I vs group II) of C3 (12.59 ± 4.72 vs 24.53 ± 15.58 mg/dl), C4 (4.26 ± 3.87 vs 7.26 ± 4.14 mg/dl) and FN (50.47 ± 12.49 vs 75.89 ± 24.70 mg/dl) in the ascitic fluid were significantly lower (P<0.05) in the group considered to be at high risk for SBP. No significant difference was observed in the plasma/ascites fibronectin ratio (3.91 ± 1.21 vs 3.80 ± 1.26) or gradient (131.46 ± 64.01 vs 196.96 ± 57.38) between groups. Fibronectin in ascites was significantly correlated to C3 (r = 0.76), C4 (r = 0.58), total protein (r = 0.73) and plasma FN (r = 0.58) (P<0.05). The data suggest that the FN concentration in ascites is related to the opsonic capacity of this fluid, and that its concentration in the ascitic fluid may be a biochemical risk factor indicator for the development of spontaneous bacterial peritonitis.

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Section: Group Isupporting

confidence: 82%

Fibronectin in the ascitic fluid of cirrhotic patients: correlation with biochemical risk factors for the development of spontaneous bacterial peritonitis

Mesquita

Leite-Mor²,

Parise³

1997

Braz J Med Biol Res

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“…Although proteolytic activity correlates with invasion in many tumor-cell lines, few data characterizing the proteolytic profiles of ovarian epithelial carcinoma cells relative to normal ovarian epithelium are currently available. Initial observations of high fibrinolytic activity in ascitic fluid from ovarian carcinoma patients and of the ability of ovarian tumor cells to degrade extracellular matrices in vitro implicate both PAS and MMPs in the pathology of ovarian carcinoma (Hafter et al, 1984;Niedbala el al., 1987;Crickard et al, 1989). Furthermore, both 6-aminohexanoic acid (6-AHA) and tissue inhibitor of metalloproteinases (TIMP) inhibit invasion of ovarian cancer cells in vitro, further implicating both PAS and MMPs in the invasive process (Kanemoto et al, 1991).…”

Section: Secretion Of Extracellular Matrix-degrading Proteinases Is Imentioning

confidence: 99%

Secretion of extracellular matrix‐degrading proteinases is increased in epithelial ovarian carcinoma

Moser

Young

Rodriguez

et al. 1994

Intl Journal of Cancer

110

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The biochemical events associated with tumor invasion involve localized degradation of the basement membrane by tumor-associated proteinases. In this study, we have characterized the proteinase secretion profiles of 5 ovarian epithelial carcinoma cell lines (DOV 13, OVCA 420, OVCA 429, OVCA 432, OVCA 433) as well as normal ovarian epithelial cells. Immunocapture assays demonstrated that all 5 carcinoma cell lines produce both secreted and surface-associated plasminogen activator. Urinary-type plasminogen activator (u-PA) production was one order of magnitude greater than production of tissue-type plasminogen activator (t-PA). Furthermore, t-PA secretion by normal ovarian epithelial cells was not detectable, whereas u-PA production was 17- to 38-fold lower than in ovarian carcinoma cells. Western-blotting analysis demonstrated that u-PA was secreted as the single chain form (scu-PA) when cells were cultured in serum-free medium. Incubation of plasminogen with ovarian carcinoma cell-conditioned medium resulted in direct activation of the zymogen to plasmin. Furthermore, following incubation of cells with plasminogen, plasmin was eluted from the cell surface, indicating that ovarian carcinoma cells contain binding sites for plasminogen/plasmin which are accessible to surface-associated plasminogen activators. In addition to plasminogen activators, metalloproteinases were also produced by DOV 13, OVCA 429 and OVCA 433 cells. DOV 13 cells produce a 68-kDa metalloproteinase similar to matrix metalloproteinase 2 (MMP-2) whereas a 92-kDa enzyme similar to MMP-9 is secreted by OVCA 429 and 433. Together, ovarian carcinoma-associated plasminogen activators and metalloproteinases catalyze the hydrolysis of the major basement membrane protein components, type-IV collagen, type-IV gelatin, laminin and fibronectin. The enhanced proteolytic capability of ovarian carcinoma cells relative to normal ovarian epithelium suggests a biochemical mechanism by which invasion and spread of ovarian epithelial carcinoma may be mediated.

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“…Fibrin degradation products, resulting from proteolysis of the provisional stroma, are elevated in the sera of women with advanced ovarian cancer [90,91]. In addition, polypeptides resulting from degradation of both fibrin and collagen, as well as procollagen peptides indicative of new collagen biosynthesis, are prevalent in carcinomatous ascites, as well as sera from women with ovarian cancer [92–95].…”

Section: Actions Of Mmps In Ovarian Cancermentioning

confidence: 99%

EGF-Receptor Regulation of Matrix Metalloproteinases in Epithelial Ovarian Carcinoma

2009

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Ovarian carcinoma is most frequently detected when disease has already disseminated intraabdominally, resulting in a 5-year survival rate of less than 20% owing to complications of metastasis. Peritoneal ascites is often present, establishing a unique microenvironmental niche comprised of tumor and inflammatory cells, along with a wide range of bioactive soluble factors, several of which stimulate the EGF-receptor (EGFR). Elevated EGFR is associated with less favorable disease outcome in ovarian cancer, related in part to EGFR activation of signaling cascades that lead to enhanced matrix metalloproteinase expression and/or function. The available data suggest that modulating the expression or activity of the EGFR and/or matrix metalloproteinases offers opportunity for targeted intervention in patients with metastatic disease. KeywordsEGF-receptor; invasion; metastasis; MMP-9; MT1-MMP/MMP-14; ovarian carcinoma Epithelial ovarian carcinoma (EOC) is the leading cause of death from gynecologic malignancy, resulting in 15,520 deaths in the USA in 2008 [201]. When disease is confined to the ovary, 5-year survival is greater than 90%. Unfortunately, the majority of women with EOC are diagnosed with already disseminated intra-abdominal disease and have a low 5-year survival rate of less than 20%. Thus, while early detection is a pressing clinical problem, analysis of factors that promote metastatic dissemination can ultimately improve the survival of women with ovarian cancer. Ovarian tumor microenvironmentA dualistic model for ovarian tumorigenesis has been proposed that is characterized by specific genetic alterations and unique molecular signatures [1][2][3]. In this classification system, lowgrade carcinomas are often confined to the ovary, arise from a recognized precursor lesion, †Author (Figure 1) [9][10][11]. These shed tumor cells may also block peritoneal lymphatics [12], contributing to the accumulation of peritoneal ascites, which can further facilitate metastatic implantation. Single cells and MCAs adhere to peritoneal mesothelium, where upon adhesive interactions and localized proteolysis enable anchoring of proliferative secondary lesions [9,10]. An exception is found in atypical proliferative serous tumors or micropapillary proliferative serous tumors (grouped as 'borderline' or 'low malignant potential'), the prognosis of which requires evaluation of peritoneal implants that often accompany these tumors. While patients with 'noninvasive implants' have a 10-year survival of practically 100%, a 34% mortality within 7 years is observed for those patients with invasive implants [12].An unique microenvironmental niche is thereby established in the peritoneal cavity, comprised of tumor cells, inflammatory cells and a plethora of soluble factors secreted by -or in response to -tumor cells, including growth factors, inflammatory mediators, bioactive lipids and proteolytic enzymes [13][14][15][16][17][18][19][20]. In addition, products of matrix invasion or partially resolved fibrosis, as well as shed...

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Crosslinked fibrin derivatives and fibronectin in ascitic fluid from patients with ovarian cancer compared to ascitic fluid in liver cirrhosis

Cited by 30 publications

References 17 publications

Fibronectin in the ascitic fluid of cirrhotic patients: correlation with biochemical risk factors for the development of spontaneous bacterial peritonitis

Fibronectin in the ascitic fluid of cirrhotic patients: correlation with biochemical risk factors for the development of spontaneous bacterial peritonitis

Secretion of extracellular matrix‐degrading proteinases is increased in epithelial ovarian carcinoma

EGF-Receptor Regulation of Matrix Metalloproteinases in Epithelial Ovarian Carcinoma

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