Characterization of single chain urokinase-type plasminogen activator with a novel amino-acid substitution in the kringle structure.
Biochim Biophys Acta
; 1293(1): 83-9, 1996 Mar 07.
Article
em En
| MEDLINE
| ID: mdl-8652631
ABSTRACT
ECV304 is a cell line established by a spontaneous transformation of endothelial cells of a human umbilical vein. It was shown that ECV304 secretes single chain urokinase-type plasminogen activator (scu-PA). A subclone, ECV304 clone 15, was obtained by acclimatization of parental clone to serum-free medium followed by limiting dilution. The clone was found to produce approximately five times as much scu-PA (approximately 20 IU/10(6) cells per day) as the parental clone after a 40 days' culture. Though the biochemical characteristics of the purified scu-PA were indistinguishable from those of the native scu-PA, it had a lower affinity for fibrin clots under the employed conditions. Molecular cloning of a cDNA encoding the scu-PA has identified a novel substitution from C to T in the nucleotide sequence encoding the kringle structure. The substitution resulted in an alteration from Pro (CCG) to Leu (CTG) at amino-acid position 121, which may be directly or indirectly involved in the decrease in the apparent affinity.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Endotélio Vascular
/
Ativador de Plasminogênio Tipo Uroquinase
/
Kringles
Tipo de estudo:
Prognostic_studies
Limite:
Humans
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
1996
Tipo de documento:
Article
País de afiliação:
Japão