Absence of binding of pancreatic and urinary kallikreins to α 2-macroglobulin

Vahtera, Elina; Hamberg, Ulla

doi:10.1042/bj1570521

Cited by 19 publications

(14 citation statements)

References 15 publications

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“…This usually results in a dose-response curve that is nonparallel to the standard curve, which these authors also re ported [21]. The low recovery of active tissue kallikrein when added to plasma and perito neal fluid in this study, and previously also reported in the rat and human [22,23], indi cates that such complex formation takes place, even though it has been reported that porcine tissue kallikrein does not bind to alpha-macroglobulins [24], However, the larg er recovery of active tissue kallikrein from normal peritoneal fluid compared with plas ma supports the theory of alpha-macroglobulin complexes masking the immunoreactivity, as the level of alpha-macroglobulins in normal porcine peritoneal fluid is only about 10% of that in plasma [11,13]. Furthermore the a Fig.…”

Section: Discussionmentioning

confidence: 45%

Studies on the Release of Tissue Kallikrein in Experimental Pancreatitis in the Pig

Bläckberg

Ohlsson

1994

Eur Surg Res

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The activation of the kallikrein-kinin system is thought to be one of the pathophysiological factors in acute pancreatitis. A radioimmunoassay for porcine, pancreatic tissue kallikrein was developed and used to measure levels in normal plasma and peritoneal fluid and in experimental, bile-induced (group and bile trypsin-induced (group B) acute pancreatitis in the pig. Normal porcine plasma and peritoneal fluid contained about 2.17 ± 0.11 and 1.91 ± 0.19 µg/l (SEM) tissue kallikrein, respectively. In experimental, acute pancreatitis there was a rapid rise in the plasma level of tissue kallikrein, followed by a slow increase to a final value of about 150% of the normal plasma level in both groups. In the peritoneal exudate a large increase (200-fold in group A and 2,000-fold in group in tissue kallikrein was seen, with a maximum within about 1/3 of the survival time, followed by a slow decrease until death in group B. In group A a smaller second peak was seen at about 2/3 of the survival time. Gelfiltration of peritoneal exudates showed complexes with alpha₁-, alpha₂-macroglobulin (α₁α₂-M), and alphai-proteinase inhibitor (α₁-PI) and a large portion of free tissue kallikrein. The complexes with α₁α₂-M and the free tissue kallikrein were found to be enzymatically active when tested on chromogenic tripeptide substrate. The presence of large amounts of free and active tissue kallikrein in the peritoneal exudate leads us to the conclusion that tissue kallikrein may be a major cause of local release of kinins in acute pancreatitis.

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Section: Discussionmentioning

confidence: 45%

Studies on the Release of Tissue Kallikrein in Experimental Pancreatitis in the Pig

Bläckberg

Ohlsson

1994

Eur Surg Res

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“…As confirmed in previous reports (Sumi et al, 1978;Takasugi et al, 1980) and in the present study almost all of the pancreatic kallikrein, which was released from the pancreas into blood, also combined with lIz-macroglobulin in plasma from patients. Conversely, Vahtera & Hamberg (1976) reported that pancreatic or urinary kallikrein could not combine with lIz-macroglobulin. If the findings of Vahtera & Hamberg (1976) are correct, how should we interpret the phenomenon of pancreatic kallikrein being combined with lIzmacroglobulin observed in the present study?…”

Section: Discussionmentioning

confidence: 96%

“…Conversely, Vahtera & Hamberg (1976) reported that pancreatic or urinary kallikrein could not combine with lIz-macroglobulin. If the findings of Vahtera & Hamberg (1976) are correct, how should we interpret the phenomenon of pancreatic kallikrein being combined with lIzmacroglobulin observed in the present study? Vahtera & Hamberg (1976) also reported that, if pancreatic or urinary kallikrein could combine with lIz-macroglobulin, the complex-formation might be due to contamination with another proteinase in the kallikrein preparation.…”

Section: Discussionmentioning

confidence: 96%

Purification and Characterization of Kallikrein from Plasma of Patients with Acute Pancreatitis

1981

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1. A kallikrein-like enzyme in plasma of patients with acute pancreatitis was further purified by successive hydroxyapatite/cellulose and Sepharose-4B column chromatography. 2. By these procedures 0.26 mg of purified enzyme with a specific activity of 215 S-2266 chromozyme units/mg of protein was obtained from 10 ml of original plasma. 3. The purified material was homogeneous as ascertained by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and had an apparent molecular weight of 31 000 as measured by gel filtration on Sephadex G-200. 4. It was confirmed immunologically that this enzyme was pancreatic kallikrein, which is distinct from plasma kallikrein, and that it could combine with alpha 2-macroglobulin only in the presence of trypsin.

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“…The protein complex contained 13.4 gg trypsin indicating that an equimolar complex was formed. This was further sustained by the recovery of trypsin in the complex [3,24].…”

Section: Trypsin Binding Activity Of Synovial Ohmmentioning

confidence: 87%

“…As seen in Table 5 the bradykinin releasing effect of trypsin is blocked by complex formation with cr2M. In earlier studies we have shown the absence of binding of pancreatic and urinary kallikreins to a2M [24]. Another possibility to prevent proteinase binding would be the blocking of binding sites in E,UTION VOLUME (m0 .…”

Section: Synovial Kininogen and Bradyldnin Releasementioning

confidence: 89%

Functionally active α2-macroglobulin and kinin release in synovial fluids of rheumatoid arthritis

1978

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The function of a2M (a2-macroglobulin) as a proteinase inhibitor in synovial fluid of rheumatoid arthritis was investigated. Low esterase activity was found in the 19S sieve fraction of Sephadex G-200 gel filtered synovial fluid samples, comparable with that obtained with normal human plasma. The molar binding ratio of uzM isolated from the synovial fluid and trypsin was estimated according to earlier established methods. The formation of an equimolar complex indicated that the synovial u2M was functionally intact.Esterase activities were measured on uN-tosyI-Larginine [3H]methyl ester. Synovial fluid samples were all found to contain proteinase enzyme which did not bind to the synovlal ohM nor to the added functionally intact, immunologically pure a2M prepared from normal human plasma.Albumin, uL-acid glycoprotein, a2HS-glyeoprotein , u2M and kininogen in synoviai fluids were determined by single radial immunodiffuslon. Only the ct2M contents were clearly lower than in normal human serum per ml.The higher than 1 ratio between the immunoreactive kininogen determined with monospeeific anti-human kininogen serum and the pharmacologically active klninogen indicated that klnin release had occurred possibly in the synovial membrane. Protelnase enzymes present in the synovial fluids and unbound to ohM caused further depletion of the active klnin Segment in synovlal kininogen. A model of the regulation by u2M of the synovlal klninogen-klnin system is given.

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Absence of binding of pancreatic and urinary kallikreins to α 2-macroglobulin

Cited by 19 publications

References 15 publications

Studies on the Release of Tissue Kallikrein in Experimental Pancreatitis in the Pig

Studies on the Release of Tissue Kallikrein in Experimental Pancreatitis in the Pig

Purification and Characterization of Kallikrein from Plasma of Patients with Acute Pancreatitis

Functionally active α2-macroglobulin and kinin release in synovial fluids of rheumatoid arthritis

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