Trypsin Release, Kinin Production, and Shock

Katz, William E.

doi:10.1001/archsurg.1964.01320020086014

Cited by 55 publications

(6 citation statements)

References 15 publications

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“…However, the role of these peptides in the pathogenesis of hemorrhagic shock is not clear (6)(7)(8)(9). Previous studies have shown that a myocardial depressant factor (MDF) present in the plasma of This investigation was supported by U. S. Public Health Service Crant HE-09924 from the National Heart Institute and by a grant from the American Heart Association.…”

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confidence: 99%

Relationship of Plasma Peptides to the Myocardial Depressant Factor in Hemorrhagic Shock in Cats

Lefer

Martin

1970

Circulation Research

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The pathophysiological relationships of a myocardial depressant factor (MDF) present in the plasma of cats in hemorrhagic shock were studied. Aprotinin (Trasylol), an inhibitor of a variety of proteases including kallikrein and trypsin, prolonged survival of cats in postoligemic shock as well as prevented the appearance of MDF in the plasma. Trasylol did not alter the arterial blood pressure, venous pressure, or heart rate of these cats in shock, nor did it protect by exerting a positive inotropic effect. Trasylol was ineffective in preventing or reversing the negative inotropic effects of MDF in isolated cat papillary muscles. Column chromatography of plasma from control cats, from untreated shocked cats and from cats treated with Trasylol before shock showed six peptide peaks, designated A, B, C, D, E, and F in decreasing order of molecular weights. Peptides corresponding to peaks A, B, E, and F exhibited insignificant myocardial depressant activity. The peptide corresponding to peak C was present in control plasma and accounted for some of the small negative inotropic effect of control plasma. The peptide corresponding to peak D had a marked myocardial depressant effect which could account for all the activity of shock plasma. The molecular weight of this peptide was estimated to be 800 to 1000. This peptide is not bradykinin, but appears to be produced by a protease present in shock.ADDITIONAL KEY WORDS kallikrein papillary muscle Trasylol postoligemic shock bradykinin column chromatography toxic factor membrane ultrafiltration eledoisin proteases• Several investigators have reported that there is a substantial increase in the concentration of circulating peptides (1-4) or in proteolytic enzymes (2,5) in the plasma of animals in hemorrhagic shock. However, the role of these peptides in the pathogenesis of hemorrhagic shock is not clear (6)(7)(8)(9). Previous studies have shown that a myocardial depressant factor (MDF) present in the plasma of This investigation was supported by U. S. Public Health Service Crant HE-09924 from the National Heart Institute and by a grant from the American Heart Association. Dr. Lefer is an Established Investigator of the American Heart Association. Mr. Martin is a U. S. Public Health Service research trainee of the National Heart Institute (Crant HE-05661).Received August 16, 1969. Accepted for publication November 9, 1969. cats in postoligemic shock is a peptide having a molecular weight between 500 and 1000 (10). MDF accumulates in the plasma as postoligemic shock progresses, and exerts a depressant effect upon isolated heart muscle (11), upon systemic blood pressure in the intact cat (10), and upon the reticuloendothelial system (12). The purposes of this study were: (a) to determine whether MDF production could be inhibited by a protease inhibitor, and (b) to isolate MDF and determine some aspects of its chemical nature. Methods SHOCK PROCEDUREAdult cats of both sexes weighing between 2.4 and 3.1 kg were used for the shock experiments. All cats were isolated for ...

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Relationship of Plasma Peptides to the Myocardial Depressant Factor in Hemorrhagic Shock in Cats

Lefer

Martin

1970

Circulation Research

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“…These compounds produce hypotension, increase capillary perm eability and produce pain by an irritation of nerve fibres [11]. In acute pancreatitis the level of vasoactive substances in the blood serum rises, the increase being parallel with th at of amylase activity [14,21]. Their level is directly related to the severity of the disease.…”

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confidence: 99%

Therapeutic Effect of the Prolonged Thoracic Duct Lymph Fistula in Patients with Acute Pancreatitis

Brzek¹,

Bartoš²

1969

Digestion

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In 10 patients with acute pancreatitis and in 10 patients with cholelithiasis the thoracic duct was a cannulated and a prolonged external drainage of the lymph was performed. Initial lymph flow per min, total volume of the lymph diverted, and the levels of lymph and blood serum amylase were measured. In patients with acute pancreatitis, the initial lymph flow, lymph and blood serum amylase were found to be significantly higher than those in cholelithiasis. In patients with acute pancreatitis, lymph amylase was significantly higher than blood amylase. Early in the course of acute pancreatitis, there was a considerable increase in lymph flow followed subsequently by a reduction. The prolonged external drainage of the thoracic duct resulted in a rapid improvement of the clinical picture. It is concluded that [1] the thoracic duct lymph is an important pathway for the rise in blood serum enzymes in acute pancreatitis, and [2] by the external drainage of the thoracic duct a considerable amount of toxic substances originating in the necrotic tissues may be removed from the organism.

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“…For example, free trypsin [35] like kallikrein [9] can hydrolyze bradykininogen to yield the hypotensive polypeptide bradykinin and it has not yet been demonstrated that a2M is able to prevent this action. However the results of Katz et al [22] are suggestive in this respect: a peritoneal fluid (dog) able to hydrolyze TAME, was also capable of liberating hypotensive polypeptides from plasma.…”

Section: The Presence Of Trypsin Is Generally Associated With High Ammentioning

confidence: 95%

Detection and Determination of α(2)-Macroglobulin Trypsin Activity in Pleural Fluids and Ascites

Bieth¹,

Métais²,

Warter³

1971

Enzyme

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Pancreatic effusions are able to hydro- lyze BAPNA, a specific substrate of trypsin. Gel filtration on Sephadex G-200 indicates that this activity is due to α(2)-macroglobulin-bound trypsin. The presence of α(2)M-trypsin complexes is further substantiated by the behaviour of the tryptic activity toward inhibitors of increasing molecular weights. Tryptic activity was found not only in pancreatic effusions but also in a small number of non pancreatic ascitic fluids. No correlation exists between this activity and the α(2)M or amylase content. These results, as well as the absence of chymotryptic activity are discussed in view of the known binding properties of α(2)-macroglobulin.

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Trypsin Release, Kinin Production, and Shock

Cited by 55 publications

References 15 publications

Relationship of Plasma Peptides to the Myocardial Depressant Factor in Hemorrhagic Shock in Cats

Relationship of Plasma Peptides to the Myocardial Depressant Factor in Hemorrhagic Shock in Cats

Therapeutic Effect of the Prolonged Thoracic Duct Lymph Fistula in Patients with Acute Pancreatitis

Detection and Determination of α(2)-Macroglobulin Trypsin Activity in Pleural Fluids and Ascites

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