Protease Inhibitors in Plasma

Laurell, C.‐B.; Jeppsson, J.-O.

doi:10.1016/b978-0-12-568401-9.50012-8

Cited by 108 publications

(50 citation statements)

References 128 publications

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“…Its inhibitory potential is greatly enhanced by heparin as determined by in vitro studies (8,13,14). a1PI is homologous to ATIII in its sequence and reaction mechanism (15) and is responsible for >90% of the trypsin inhibitory capacity of human plasma (16). Like ATIII, it is capable of inhibiting thrombin and Factor X. in vitro (6,17,18).…”

Section: Introductionmentioning

confidence: 99%

Regulation of factor Xa in vitro in human and mouse plasma and in vivo in mouse. Role of the endothelium and plasma proteinase inhibitors.

Fuchs¹,

Pizzo²

1983

J. Clin. Invest.

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A B S T R A C T The regulation of human Factor Xa was studied in vitro in human and mouse plasma, and in vivo in mouse. In human plasma, '251-Factor Xa bound to a1-proteinase inhibitor, antithrombin III, and a2-macroglobulin in a ratio of 4.9:1.9:1 as determined by gel electrophoresis and by adsorption to IgG-(antiproteinase inhibitor)-Sepharose beads. The distribution of Factor Xa in mouse plasma was similar. The clearance of Factor Xa in mice was rapid (50% clearance in 3 min) and biphasic. a1-Proteinase inhibitor-trypsin, even at a 2,000-fold molar excess, failed to inhibit the clearance of Factor Xa, while a2-macroglobulin-trypsin inhibited only the later phase of clearance. The plasma clearance of diisopropylphosphoryl-Factor Xa was more rapid than native Factor X. (50% clearance in 2.5 min), and the clearance was blocked by diisopropylphosphoryl-thrombin. Electrophoresis experiments confirmed that by 2 min after injection into the murine circulation, 90% of the bound Factor Xa was on a2-macroglobulin, in marked contrast to the in vitro results. Organ distribution studies at 3 and 15 min with 125I_ Factor X. demonstrated that the majority of radioactivity was in the liver, with significant radioactivity also present in lung and kidney. Autopsies performed 30 s after injection of 125I-Factor Xa also demonstrated significant binding to the aorta and vena cava. These studies indicate that Factor Xa binds to specific thrombin-binding sites on endothelial cells, and that this binding alters its proteinase inhibitor specificity. Factor Xa binds to a2-macroglobulin in vivo, whereas the predominant in vitro inhibitor of Factor X. is a,-proteinase inhibitor.

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Section: Introductionmentioning

confidence: 99%

Regulation of factor Xa in vitro in human and mouse plasma and in vivo in mouse. Role of the endothelium and plasma proteinase inhibitors.

Fuchs¹,

Pizzo²

1983

J. Clin. Invest.

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“…Alphai-antitrypsin (alphasprotease inhibitor) and alpha2-macroglobutin accounted for more than 90 % of the total protease inhibiting capacity of plasma 10 . It has been shown that plasma alphai-antitrypsin level increases in patients with ARF particularly after multiple traumatic injuries.…”

Section: Discussionmentioning

confidence: 99%

Proteolytic Activity in Patients with Hypercatabolic Renal Failure

Hörl

Schäfer

Scheidhauer

et al. 1984

Advances in Experimental Medicine and Biology

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“…at least from a Pi M Z subject. Assuming the same relation between the a]-AT concentration and the Pi-type in a fetus as in a newborn, a Pi ZZ fetus would have about 10% of the normal fetal plasma alAT concentration, that is, about 0.1 g/liter, and a Pi M Z fetus would have 70%, that is, about 0.5 g/liter (12). The electrofocusing of this sample showed that the density of the major Pi M bands was greater than that in pure amniotic fluid.…”

Section: Case Imentioning

confidence: 99%