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Interactions in vit...
Interactions in vitro and in vivo between porcine tissue kallikrein and porcine plasma proteinase inhibitors
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- Bläckberg, Mats (författare)
- Lund University,Lunds universitet,Kliniska Vetenskaper, Helsingborg,Sektion II,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Clinical Sciences, Helsingborg,Section II,Department of Clinical Sciences, Lund,Faculty of Medicine,Skåne University Hospital
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- Ohlsson, Kjell (författare)
- Skåne University Hospital
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(creator_code:org_t)
- 2009-07-08
- 1994
- Engelska.
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Ingår i: Scandinavian Journal of Clinical & Laboratory Investigation. - : Informa UK Limited. - 1502-7686 .- 0036-5513. ; 54:8, s. 643-651
- Relaterad länk:
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http://dx.doi.org/10...
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https://lup.lub.lu.s...
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https://doi.org/10.3...
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Abstract
Ämnesord
Stäng
- The elimination of radio-iodinated porcine tissue kallikrein, after intravenous injection in the pig, showed a rapid initial clearance from plasma (T1/2 approximately 10min), followed by a phase of slower elimination (T1/2 approximately 100min). Gel filtration of plasma samples showed complexes with alpha1-alpha2-macroglobulin (A1a2-M) and alpha1-proteinase inhibitor (A1PI), which decreased with time. The urinary excretion of undegraded tissue kallikrein was about 1.8%. Gel filtration of urine showed a minor peak representing free tissue kallikrein and a major peak representing degradation products. On average, 8.3% was found in the liver and 1.3% in the kidneys post mortem, indicating that these are the primary organs for the elimination of tissue kallikrein.The in vivo findings were supported by in vitro experiments. A1a2-M were found to be the major inhibitors of tissue kallikrein, when a mixture of the enzyme and porcine plasma was analysed by gel filtration, Immunoelectrophoresis, crossed Immunoelectrophoresis and autoradiography. A1PI was only a minor inhibitor of tissue kallikrein. Both the A1a2-M and A1-PI complex formation was found to be time-dependent and slow; unbound glandular kallikrein was still detected after 12h, even when there was a molar surplus of A1-M and A1PI. The complexes with A1a2-M and the unbound tissue kallikrein were found to be enzymatically active against low-molecular-weight chromogenic substrate. The total tissue kallikrein-inhibiting capacity of plasma seemed to be exceeded at a concentration of 800 KU/1 when analysed using the rat uterus bioassay.A1a2-M appears to be the major inhibitor of tissue kallikrein in plasma and the complexes are removed mainly by the reticulo-endothelial system, such as that in the liver.
Ämnesord
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Fysiologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Physiology (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine (hsv//eng)
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