Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0031154 (peritonitis)
 15,372 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Peritoneal fluids from patients with diffuse peritonitis secondary to perforation of the appendix contained large quantities of collagenase and elastase. The enzymes, which existed in the form of complexes with plasma protease inhibitors, probably had been released from the granulocytes. The two enzymes had linked almost half of the alpha 1-antitrypsin and four fifths of the alpha 2-macroglobulin in the fluid. Evidence that regional defense against protease had failed was obtained by finding the C3 component of complement completely converted. Toxic peptides probably had been released. Recognition of plasma protease inhibitors as an important part of the regional defense against protease also suggested use for therapy. We lavaged the peritoneum postoperatively with fluid that did not contain plasma inhibitors but with volumes large enough to eliminate the accumulation of enzymes for the granulocyte.
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PMID:Collagenase and elastase released during peritonitis are complexed by plasma protease inhibitors. 17 59

Human granulocytes release 25-30% of the granular neutral proteases, collagenase and elastase, to the exterior of the cell during phagocytosis of yeast cells or immune complexes. Similar amounts of myeloperoxidase and lactoferrin are released. Crossed immunoelectrophoresis demonstrated that collagenase and elastase released extracellularly formed complexes with serum alpha1-antitrypsin. The presence of alpha1-antitrypsin complexes with granulocyte collagenase and elastase were also demonstrated in inflammatory processes, e.g. in the peritoneal exudate of acute peritonitis. The reactivity of neutrophil proteases with natural plasma protease inhibitors must be considered in assessing the role of these proteases as the etiologic agent of tissue damage and degradation during the inflammatory process.
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PMID:The extracellular release of granulocyte collagenase and elastase during phagocytosis and inflammatory processes. 19 89

The concentration and functional state of alpha 1-proteinase inhibitor (alpha 1-PI) may modulate the expression of peritoneal phlogosis by affecting the activity of proteases and synthesis of autacoids. alpha 1-PI is detectable in peritoneal effluents of peritonitis-free patients. alpha 1-PI purified from peritoneal fluid of these patients was biologically active both in terms of inhibition of elastase activity and of synthesis of platelet activating factor (PAF). The biological activity of alpha 1-PI could therefore explain the absence of detectable amounts of PAF in peritonitis free patients despite the presence of intraperitoneal concentrations of tumor necrosis factor-alpha (TNF alpha) that would be sufficient per se to induce the synthesis of PAF. In patients with acute infectious peritonitis, the concentration of immunoreactive alpha 1-PI was significantly increased in respect ot stable patients. However, alpha 1-PI purified from patients with acute peritonitis was functionally inactive both on proteolytic activity on elastase and on TNF alpha-induced PAF synthesis by purified human PMN. The loss of alpha 1-PI activity correlated with the number of peritoneal leukocytes and was probably dependent on oxidative inactivation. Indeed, treatment with reducing agent restored the inhibitory function of alpha 1-PI. The inactivation of alpha 1-PI in patients with peritonitis was associated with the presence of PAF in peritoneal dialysates. These results suggest that alpha 1-PI prevents the proteolytic action and cell activation leading to PAF synthesis in peritonitis free patients. However, inactivation of its function by oxidants generated during the inflammatory process may lead to proteolytic injury and unrestrained synthesis of inflammatory mediators during peritonitis.
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PMID:Role of alpha 1-proteinase inhibitor in restraining peritoneal inflammation in CAPD patients. 140 51

A specific enzyme-linked immunoassay (ELISA) has been developed for the determination of neutrophil proteinase 4 (NP4) in human plasma/serum and tissue fluids. Comparison of the sequence for the first 20 N-terminal amino acids of NP4, neutrophil elastase and cathepsin G shows that NP4 is distinct from the other two proteases. However, all three show considerable homology. Neither elastase nor cathepsin G show any immunoreactivity when tested in the present ELISA. Normal human plasma contains about 38 micrograms/l of NP4, identified as alpha 1-proteinase inhibitor complexes. This represents about 50% of the total amount of NP4 released in plasma. The remaining 50% is bound by alpha 2-macroglobulin. Blood coagulation leads to a rapid release of NP4 from the leukocytes. Peritonitis is accompanied by a pronounced release of NP4, as shown by a three-to 10-fold increase of NP4 plasma levels and by the NP4 level in peritoneal exudates, which reaches about 40 mg/l in severe cases.
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PMID:Release of immunoreactive human neutrophil proteinase 4, normally and in peritonitis. 170 22

Peritonitis exudate reveals strong proteolytic activity which is paralleled by deficient opsonic capacity and high concentrations of lysosomal proteinases (elastase and cathepsin B). Lysosomal serine and cysteine proteinases (elastase, cathepsins B, L) were shown to degrade immunoglobulin G(IgG) and seem to be at least partially responsible for the observed proteolytic inactivation of IgG in peritonitis exudates. Intraabdominal serum application seems to restore opsonic activity by substitution of opsonins and proteinase inhibitors.
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PMID:Proteolysis of defensive proteins in peritonitis exudate: pathobiochemical aspects and therapeutical approach. 180 4

In patients with diffuse purulent peritonitis, the total pool of an acid-soluble blood plasma fraction (ABPF) considerably increases as compared to that in normals (donors). The present paper is concerned with the role of proteolytic activity and lysis of bacterial cells and cells of different human tissues in the formation of the ABPF in patients with peritonitis. For this purpose the normals' blood and its separate components were treated with various enzymes (trypsin, pronase, chemotrypsin, papain, elastase, alpha-amylase) to measure the ABPF. The pattern of changes detectable on such a treatment was compared with the tendency of changes seen in patients with peritonitis. Measurements were also made of acid-soluble fractions in suspensions of bacterial cells and cells of the pancreas, liver and heart muscle tissue of man. It has been found that on proteolysis of plasma proteins and membrane proteins of blood cells there form products contained by the ABPF. Such products formed in the greatest amount as a result of treatment with pronase. Products of the lysis of bacterial cells may be also contained by the ABPF of peritonitis patients. The possibility of detecting proteolytic degradation and cellular disintegration according to the spectral characteristics of separate fractions of the ABPF is discussed.
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PMID:[The possible pathways for the formation of a pool of an acid-soluble blood plasma fraction in patients with diffuse suppurative peritonitis]. 218 99

Despite a high concentration of serum proteins and intact phagocytes peritonitis exudates contain a large number of viable, pathogenic bacteria. The reason for this biological paradox is unknown. Our investigations reveal a pronounced defect in humoral opsonization of foreign particles in peritonitis exudate. We evaluated a modified chemiluminescence system allowing the determination of opsonic activity in serum and exudate. In serum we found a close correlation between opsonic activity and immunologically measurable levels of C3-complement and IgG. In purulent peritonitis exudates, however, the actual opsonizing activity was much less than expected according to the opsonin concentrations. We found a pronounced difference between immunologically determined opsonin levels and impaired opsonic function. Employing crossed immunoelectrophoresis massive C3-splitting into smaller fragments could be demonstrated in peritonitis exudates. In these exudates we found very high concentrations of granulocyte proteolytic (elastase) and oxidative (myeloperoxidase) enzymes which may lead to a functional destruction of opsonins followed by impaired opsonization in peritonitis exudate. The great number of bacteria and foreign particles in addition can cause a pronounced physiological consumption of complement components. The almost complete breakdown of intact C3-complement in intraabdominal exudate explains the deficient host defence in patients with severe peritonitis.
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PMID:[Insufficiency of intra-abdominal immunity to infection in purulent peritonitis--sequela of disordered foreign body opsonization]. 254 Mar 81

The inflammatory response which is similar in all forms of peritonitis was recorded by determining the levels of parameters shown to represent the activation state of plasmatic and cellular systems as well as the inhibitory capacity of the plasma. In a selected series of patients with different underlying diseases, blood sampling was started at the time of admission when the clinical finding of an acute abdomen led to emergency laparotomy. Depending upon the duration of the illness and the severity of the peritonitis, a significant increase in fibrinopeptide A and of C3a could be detected within a few hours, which was followed by an increase in the elastase alpha-1-proteinase inhibitor complex. Differences due to variable cause could not be found. There was a striking correlation between the preoperative values of these three parameters and the postoperative course of the patients. Additionally, there was a significant enhancement of an endothelial proliferation-inhibiting capacity in the serums of the lethal group, whereas endotoxin could only be detected in trace amounts in four patients with intraabdominal infection in the preoperative period.
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PMID:Monitoring of the inflammatory response in early peritonitis. 278 51

The blood plasma granulocyte elastase activity and the urine acid-fast inhibitor level have been measured in 23 healthy puerperae and in 65 puerperae with various pyo-septic complications in the postpartum period. These parameters have been found stable in healthy puerperae and shifted in those with pyo-septic complications: elastase activity increased parallel with the reduction of the acid-fast inhibitor level. The most manifest shifts in the enzymatic inhibitor balance have been observed in the puerperae with peritonitis. These data indicate the pathogenetic role of the enzymatic inhibitor imbalance in the development of pyo-septic complications postpartum.
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PMID:[Enzyme-inhibitory imbalance in suppurative-infective diseases in puerperants]. 281 53

In 27 patients with severe diffuse purulent or fecal peritonitis planned relaparotomies with peritoneal lavage or continuous dorsoventral lavage with open abdomen were performed after surgical treatment of the primary infection. During the course of the lavage treatment serum endotoxin was measured daily. The endotoxin-induced liberation of lysosomal proteases was studied by determining the elastase from polymorphonuclear leucocytes. 16 surviving patients showed decreasing endotoxin levels and decreasing elastase concentrations during the course of abdominal lavages. Planned peritoneal lavage and continuous dorso-ventral lavage seem to have the same potency in eliminating endotoxin from the infected peritoneal cavity. In letal courses endotoxinemia either persisted at high levels or even progressed inspite of lavage treatment.
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PMID:[Serum endotoxin level in the course of open peritonitis treatment]. 391 Mar 74


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