Interactions in vitro and in vivo between porcine tissue kallikrein and porcine plasma proteinase inhibitors
(1994) In Scandinavian Journal of Clinical & Laboratory Investigation 54(8). p.643-651- Abstract
- 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... (More)
- 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. (Less)
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- author
- Bläckberg, Mats LU and Ohlsson, Kjell
- organization
- publishing date
- 1994
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Scandinavian Journal of Clinical & Laboratory Investigation
- volume
- 54
- issue
- 8
- pages
- 643 - 651
- publisher
- Informa Healthcare
- external identifiers
-
- scopus:0027948355
- ISSN
- 1502-7686
- DOI
- 10.3109/00365519409087545
- language
- English
- LU publication?
- yes
- id
- 6df3bd7e-6347-4d6a-91f3-38a82727a234
- date added to LUP
- 2020-04-14 13:10:57
- date last changed
- 2023-04-13 04:03:27
@article{6df3bd7e-6347-4d6a-91f3-38a82727a234,
abstract = {{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.<br/>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.<br/>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.}},
author = {{Bläckberg, Mats and Ohlsson, Kjell}},
issn = {{1502-7686}},
language = {{eng}},
number = {{8}},
pages = {{643--651}},
publisher = {{Informa Healthcare}},
series = {{Scandinavian Journal of Clinical & Laboratory Investigation}},
title = {{Interactions in vitro and in vivo between porcine tissue kallikrein and porcine plasma proteinase inhibitors}},
url = {{http://dx.doi.org/10.3109/00365519409087545}},
doi = {{10.3109/00365519409087545}},
volume = {{54}},
year = {{1994}},
}