A protease-hypersensitive deletion derivative of human tissue-type plasminogen activator.
Gene
; 73(2): 439-47, 1988 Dec 20.
Article
em En
| MEDLINE
| ID: mdl-3149609
ABSTRACT
We have constructed amplified Chinese hamster ovary cell lines constitutively synthesizing human tissue-type plasminogen activator (t-PA) or a derivative in which the domains homologous to epidermal growth factor and kringle 1 have been removed [delta(G + K1)]. The properties of the secreted proteins were investigated when synthesized in the presence or absence of the serine protease inhibitor aprotinin in the medium. t-PA in the culture supernatants was either single-chain or two-chain protein. The protease activity of both forms was stimulated by fibrin. The biochemical properties of delta(G + K1) were significantly different when harvested from cells grown under different culturing conditions. Protease activity of delta(G + K1) was stimulated ten- to 20-fold by fibrin when harvested from medium with aprotinin, but was stimulated only two- to three-fold when aprotinin was absent from the serum. Characterization of the secreted proteins revealed that the heavy-chain equivalent of delta(G + K1) is degraded when serine protease inhibitor is absent in the culture medium. These results indicate that the functional and biochemical properties of restructured versions of t-PA may depend on the presence of protease(s) in the culture supernatants.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Transfecção
/
Deleção Cromossômica
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Ativador de Plasminogênio Tecidual
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Genes
Limite:
Animals
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Humans
Idioma:
En
Ano de publicação:
1988
Tipo de documento:
Article