Studies on the Role of the Plasma Protease Inhibitors on in Vitro C3 Activation and in Acute Pancreatitis

Balldin, G; Eddeland, Allan; Ohlsson, Kjell

doi:10.3109/00365528109182018

Cited by 44 publications

(12 citation statements)

References 13 publications

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“…Similarly, we also found a total degradation of C3 in the peritoneal exudates of many of these patients accompanied by degradation products in their plasma [3]. In addition, we have now also demonstrated a similar pattern for kininogen [17].…”

Section: Discussionsupporting

confidence: 53%

“…This protease-antiprotease imbalance has the potential to result in a dramatic local release of vasoactive substances [4]. Evidence of involvement of the complement system in experimental acute pancreatitis has been reported previously [16], and we have .also found this to be true in patients with severe acute pancreatitis [3]. The complement catabolism appears to take place mainly in the abdominal cavity.…”

Section: Introductionsupporting

confidence: 66%

“…Specific rabbit antisera against human al-antitrypsin, a2-macroglobulin, C3, orosomucoid, cationic trypsin [3], leukocyte elastase [20], PSTI [12], aprotinin [7], and pancreatic elastase [9] were the same as used in earlier studies. Rabbit antiserum to human high molecular and low molecular weight kininogen was obtained from Professor Hans Fritz, Munich (FRG).…”

Section: P-valuementioning

confidence: 99%

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The effect of peritoneal lavage and aprotinin in the treatment of severe acute pancreatitis

et al. 1983

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Fifty-five patients with severe acute pancreatitis were treated with peritoneal lavage at the Dept. of Surgery at Malmö General Hospital. In a randomized study 26 of the 55 patients received in addition 500,000 KIU aprotinin in the lavage fluid every 2 h. There were no significant differences between the aprotinin- and non-aprotinin-treated groups as to mortality and clinical results. The initial concentration of alpha 1-antitrypsin in plasma was mainly within normal range with increasing values during the treatment. No differences were seen between the two groups. The initial mean level of alpha 2-macroglobulin in plasma was slightly decreased, but 17 patients showed values below normal range. The alpha 2-macroglobulin level during the lavage showed a similar course in the two groups. alpha 1-Antitrypsin and alpha 2-macroglobulin in the lavage fluids showed signs of complexation but in plasma these inhibitors did not show any signs of complexation. On admission to the hospital the mean levels of C3 and kininogen in the plasma were slightly below normal. During the lavage treatment no differences were seen between the two groups. Degradation products of C3 and kininogen were seen in both serum and peritoneal fluids. The electrophoretic patterns of C3 and kininogen normalized in serum as well as in lavage fluids during the lavage treatment without any significant differences in the two groups. High levels of immunoreactive trypsin, pancreatic elastase, PSTI, and leukocyte elastase in serum were seen equally in both groups of patients.

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Section: Discussionsupporting

confidence: 53%

Section: Introductionsupporting

confidence: 66%

Section: P-valuementioning

confidence: 99%

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The effect of peritoneal lavage and aprotinin in the treatment of severe acute pancreatitis

et al. 1983

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“…The concentrations of the trypsin-2-␣ 1 -antitrypsin complex in serum reflects the severity of the pancreatitis (60,61). It is thought that activation of trypsinogen plays a pivotal role in development of pancreatitis by activating other pancreatic enzymes (61,62). It is conceivable that activation of proMMP-9 derived from inflammatory cells (8 -10) could also contribute to the tissue destruction seen in this disease.…”

Section: Discussionmentioning

confidence: 99%

Activation of Type IV Procollagenases by Human Tumor-associated Trypsin-2

Sorsa¹,

Salo²,

Koivunen³

et al. 1997

Journal of Biological Chemistry

179

170

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Increased production of proteinases, such as matrix metalloproteinases (MMPs), is a characteristic feature of malignant tumors. Some human cancers and cell lines derived from them also express trypsinogen, but the function of the extrapancreatic trypsin has remained unclear. In this study we cloned and sequenced trypsinogen-2 cDNA from human COLO 205 colon carcinoma cells and characterized the ability of the enzyme to activate latent human type IV procollagenases (proMMP-2 and proMMP-9). As shown by cloning and N-terminal amino acid sequencing, the amino acid sequence of tumor-associated trypsin-2 is identical to that of pancreatic trypsin-2. We found that both pancreatic trypsin-2 and tumor cell-derived trypsin-2 are efficient activators of proMMP-9 and are capable of activating proMMP-9 at a molar ratio of 1:1000, the lowest reported so far. Human trypsin-2 was a more efficient activator than widely used bovine trypsin and converted the 92-kDa proMMP-9 to a single 77-kDa product that was not fragmented further. The single peptide bond cleaved by trypsin-2 in proMMP-9 was Arg 87 -Phe 88 . The generation of the 77-kDa species coincided with the increase in specific activity of MMP-9. In contrast, trypsin-2 only partially activated proMMP-2. Trypsin-2 cleaved the Arg 99 -Lys 100 peptide bond of proMMP-2 generating 62-65-kDa MMP-2 species. Trypsin-2-induced proMMP-2 and -9 conversions were inhibited by tumor-associated trypsin inhibitor added either prior to or during activation indicating that proMMPs were not activated autocatalytically. Trypsin-2 also activated proMMPs associated with tissue inhibitor of matrix metalloproteinases, the complexes of which are thought to be the major MMP forms in vivo. The ability of human tumor cellderived trypsin-2 to activate latent MMPs suggests a role for trypsin-2 in initiating the proteinase cascade that mediates tumor invasion and metastasis formation.

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“…Trypsin plays a cen tral role in the pathophysiology of acute pan creatitis, and its ability to interfere with the cascade systems is known from in vitro and in vivo experiments in acute pancreatitis [9,10]. A correlation exists between clinical se verity of the disease and the degree of bio…”

mentioning

confidence: 99%

Pathobiochemistry and Early CT Findings in Acute Pancreatitis

Hjelmqvist

Wattsgård²,

Borgström³

et al. 1989

Digestion

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Extrapancreatic findings at computed tomography (CT), performed within 24 h in 42 consecutive episodes of acute pancreatitis, were classified according to a scoring system (EP score) and were correlated to Ranson’s prognostic signs, to duration of hospital stay, biochemical changes in plasma and pancreatic ischaemia found at CT with contrast enhancement. Increasing EP score was found to be related to increasing number of positive Ranson’s signs, longer hospital stay and pancreatic ischaemia. Plasma levels of immunoreactive cationic trypsin and amylase were not proportional to EP score, α₁-protease inhibitor, antichymotrypsin but not immunoreactive pancreatic secretory trypsin inhibitor increased proportionally to EP score. No changes related to EP score were seen in α₂-macroglobulin levels. Serum levels of trypsin-α₁-protease inhibitor complex were maximal after 3 days and most pronounced in cases with high EP scores. Plasma levels of factor X, α₂-antiplasmin and C1-esterase inhibitor were found to be inversely proportional to EP score.

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Studies on the Role of the Plasma Protease Inhibitors on in Vitro C3 Activation and in Acute Pancreatitis

Cited by 44 publications

References 13 publications

The effect of peritoneal lavage and aprotinin in the treatment of severe acute pancreatitis

The effect of peritoneal lavage and aprotinin in the treatment of severe acute pancreatitis

Activation of Type IV Procollagenases by Human Tumor-associated Trypsin-2

Pathobiochemistry and Early CT Findings in Acute Pancreatitis

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