Studies of Streptococcal Fibrinolysis. I. The Dissimilarity of Serum Protease and Trypsin as Indicated by the Separate Specificities of Their Kinases, Fibrinolysin and Enterokinase 1

Kaplan, Melvin H.

doi:10.1172/jci101713

Cited by 38 publications

(8 citation statements)

References 19 publications

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“…Initially, the inactive form of this proteolytic enzyme was named serum tryptogen (Ferguson, 1943) and several reports had considered that serum tryptogen and trypsin might be identical. It was subsequently demonstrated that serum tryptogen and trypsin were not identical based on separate specificities of their activators, fibrinolysin and enterokinase, respectively, as well antibody neutralization studies that distinguished these enzymes (Kaplan, 1946). The terms that emphasize the plasma source of serum tryptogen proteolytic activity were subsequently adopted, plasmin and plasminogen (Christensen, 1945).…”

Section: The Plasminogen Activation Systemmentioning

confidence: 99%

New Insights into the Role of Plg-RKT in Macrophage Recruitment

Miles

Lighvani

Baik

et al. 2014

International Review of Cell and Molecular Biology

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Plasminogen is the zymogen of plasmin, the major enzyme that degrades fibrin clots. In addition to its binding and activation on fibrin clots, plasminogen also specifically interacts with cell surfaces where it is more efficiently activated by plasminogen activators, compared with the reaction in solution. This results in association of the broad spectrum proteolytic activity of plasmin with cell surfaces that functions to promote cell migration. Here we review emerging data establishing a role for plasminogen, plasminogen receptors and the newly discovered plasminogen receptor, Plg-RKT, in macrophage recruitment in the inflammatory response and we address mechanisms by which the interplay between plasminogen and its receptors regulates inflammation.

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Section: The Plasminogen Activation Systemmentioning

confidence: 99%

New Insights into the Role of Plg-RKT in Macrophage Recruitment

Miles

Lighvani

Baik

et al. 2014

International Review of Cell and Molecular Biology

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confidence: 99%

“…Schmitz (2, 3, 4) claimed that he isolated both trypsin and a specific trypsin-inhibitor from plasma. However, more recent work indicates that the protease is not identical with trypsin, although it is quite similar in many respects (5,6).It has long been known that proteolytic activity appears in blood following treatment with chloroform, acetone, or certain other denaturing agents. Tagnon and others (7,8,9) used this technic to activate blood protease and described many of its properties.…”

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confidence: 99%

Effect of Blood Protease and Trypsin Inhibitor on the Clotting Mechanism 1

Glazko¹

1947

J. Clin. Invest.

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The influence of proteolytic enzymes on blood coagulation has attracted considerable attention in recent years because of the possibility of their involvement in the normal clotting process. Eagle and Harris (1) showed that certain proteolytic enzymes such as trypsin could activate prothrombin; while other enzymes such as papain could clot fibrinogen directly. Schmitz (2, 3, 4) claimed that he isolated both trypsin and a specific trypsin-inhibitor from plasma. However, more recent work indicates that the protease is not identical with trypsin, although it is quite similar in many respects (5,6).It has long been known that proteolytic activity appears in blood following treatment with chloroform, acetone, or certain other denaturing agents. Tagnon and others (7,8,9) used this technic to activate blood protease and described many of its properties. Holmberg (10) and Christensen (11) independently demonstrated that streptokinase,2 which is itself devoid of proteolytic activity, could activate the protease in blood and thus produce digestion. Christensen also showed that the blood protease activated by streptokinase was identical with chloroform-activated serum protease (6). The inactive enzyme is located principally in globulin fraction III-2, along with considerable amounts of prothrombin (12, 13). Active protease is present in globulin fraction III-3, which is actually a sub-fraction of III-2. Fraction III-3 was used in the present experiments as a convenient source of blood protease.A definite coagulation-inhibiting effect of crystalline pancreatic trypsin-inhibitor was demon-1 This work was supported in part by grants from the Life Insurance Medical Research Fund and the University Center in Georgia.2 Following the suggestion of Christensen (11), it was decided to adopt the term "streptokinase" for use throughout this paper. The earlier designation "streptococcal fibrinolysin" was based on the erroneous assumption that the fibrinolytic enzyme itself was produced in the bacterial culture. strated by Ferguson (14), supporting his thesis that a protease is involved in the activation of prothrombin (15). Similar results were obtained by Grob (16), who also found that serum anti-protease prepared by the method of Schmitz (4) delayed coagulation. Tagnon and Soulier (17) showed that trypsin-inhibitor isolated from soy bean flour could also inhibit coagulation. Their work has been confirmed and extended by the observations described in this paper. METHODS AND MATERIALSMost of the experiments described here involve changes in thrombin concentration which can be measured indirectly by means of the clotting time (18). In all cases, solutions were maintained at 380 C., and the pH was kept in the range of 7.2 to 7.6 as measured with a glass electrode. A small amount of phenyl mercuric borate was added to the reagents to prevent bacterial growth. Tests for thrombic activity were carried out by pipetting 0.5 ml. of thrombin into 1 ml. of fibrinogen solution, using 10 mm. X 75 mm. serological tubes. Clot formation was timed fr...

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“…preplasmin1 (plasminogen) [27,28]. The preplasmin-plasmin system resembles the pretrypsin-trypsin system, but dissimilarities in the two enzyme systems have been clearly established [28,29]. Plasma kallikrein is also present in plasma as an inactive precursor called prekallikrein1 (kallikreinogen) [18].…”

Section: Interrelationship Of Human Plasma Kallikrein and Plasmin In mentioning

confidence: 99%