Literature summary for 3.4.21.68 extracted from

Komoriya, K.; Kato, Y.; Hayashi, Y.; Ohsuye, K.; Nishigaki, R.; Sugiyama, Y.
Characterization of the hepatic disposition of lanoteplase, a rationally designed variant of tissue plasminogen activator in rodents (2007), Drug Metab. Dispos., 35, 469-475.

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Protein Variants

Protein Variants	Comment	Organism
additional information	a much lower uptake clearance is found in the liver for lanoteplase compared to wild-type t-PA. Rate constants for cell surface binding, internalization, and degradation of lanoteplase are also lower than those for t-PA in primary cultured rat hepatocytes. Results suggest that the improved stability of lanoteplase in vivo is due to the delay in the receptor-mediated endocytosis of lanoteplase. Uptake clearance in liver decreases with coadministration of lactoferrin, a ligand for low-density lipoprotein receptor-related protein (LRP) and the asialoglycoprotein receptors (ASGP) and in Irpap1-/- mice, which have a hereditary deficiency of lipoprotein receptor-related protein. Uptake clearance is not affected by mannose, whereas that of t-PA decreases with both ligands and in Irpap1(-/-) mice. Hepatic disposition of lanoteplase seems to be mediated by common specific receptors for t-PA, including LRP and the ASGP receptors	Rattus norvegicus
additional information	disposition profile of lanoteplase, a recombinant mutant of t-PA, in vivo and the kinetics of receptor-mediated endocytosis of this recombinant t-PA in vitro is examined to kinetically characterize the mechanism underlying its tissue distribution and elimination	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
liver	-	Rattus norvegicus	-

Synonyms

Synonyms	Comment	Organism
t-PA	-	Rattus norvegicus
Tissue plasminogen activator	-	Rattus norvegicus

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Release 2023.1 (January 2023)