التفاصيل البيبلوغرافية
| العنوان: |
Human single-chain urokinase is activated by the omptins PgtE ofSalmonella entericaand Pla ofYersinia pestisdespite mutations of active site residues |
| المؤلفون: |
Marjo Suomalainen, Carmen Buchrieser, Hanna M. Järvinen, Johanna Haiko, Tiira Johansson, Nisse Kalkkinen, Liisa Laakkonen, Timo K. Korhonen, Katri M. Juuti |
| المصدر: |
Molecular Microbiology. 89:507-517 |
| بيانات النشر: |
Wiley, 2013. |
| سنة النشر: |
2013 |
| مصطلحات موضوعية: |
0303 health sciences, Protease, biology, medicine.diagnostic_test, 030306 microbiology, Plasmin, Omptin, Proteolysis, medicine.medical_treatment, biology.organism_classification, Microbiology, OmpT, 03 medical and health sciences, Shigella flexneri, Yersinia pestis, medicine, Yersinia pseudotuberculosis, Molecular Biology, 030304 developmental biology, medicine.drug |
| الوصف: |
Fibrinolysis is important in cell migration and tightly regulated by specific inhibitors and activators; of the latter, urokinase (uPA) associates with enhancement of cell migration. Active uPA is formed through cleavage of the single-chain uPA (scuPA). The Salmonella enterica strain 14028R cleaved human scuPA at the peptide bond Lys158-Ile159, the site cleaved also by the physiological activator human plasmin. The cleavage led to activation of scuPA, while no cleavage or activation were detected with the mutant strain 14028R lacking the omptin protease PgtE. Complementation and expression studies confirmed the role of PgtE in scuPA activation. Similar cleavage and activation of scuPA were detected with recombinant Escherichia coli expressing the omptin genes pla from Yersinia pestis, ompT and ompP from E. coli, sopA from Shigella flexneri, and leo from Legionella pneumophila. For these omptins the activation of scuPA is the only shared function so far detected. Only poor cleavage and activation of scuPA were seen with YcoA of Y. pestis and YcoB of Yersinia pseudotuberculosis that are considered to be proteolytically inactive omptin variants. Point mutations of active site residues in Pla and PgtE had different effects on the proteolysis of plasminogen and of scuPA, indicating versatility in omptin proteolysis. © 2013 John Wiley & Sons Ltd. |
| تدمد: |
0950-382X |
| URL الوصول: |
https://explore.openaire.eu/search/publication?articleId=doi_________::94c6adaa3bd84b5938b7c4a0384f2c9a
https://doi.org/10.1111/mmi.12293 |
| حقوق: |
OPEN |
| رقم الأكسشن: |
edsair.doi...........94c6adaa3bd84b5938b7c4a0384f2c9a |
| قاعدة البيانات: |
OpenAIRE |
