Controlled release of a protein kinase inhibitor UCN-01 from liposomes influenced by the particle size

Yamauchi, Masahiro; Kusano, Hiroko; Saito, Etsuko; Abe, Masayuki; Tsutsumi, Kyoko; Uosaki, Yoichi; Nakakura, Masashi; Kato, Yasuki; Aoki, Noboru

doi:10.1016/j.ijpharm.2007.08.021

Cited by 2 publications

(1 citation statement)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In contrast, canine AGP has lower affinity for UCN-01 and therefore has little effect on the pharmacodynamics of UCN-01 and rat AGP exhibited only weak and nonspecific binding to UCN-01 (Fuse et al, 1998(Fuse et al, , 1999. Interestingly, encapsulation of UCN-01 in liposomes has been proposed to reduce the impact of AGP on UCN-01 pharmacodynamics (Yamauchi et al, 2005(Yamauchi et al, , 2008.…”

Section: Xenobiotics-bindingmentioning

confidence: 99%

Into the Labyrinth of the Lipocalin α1-Acid Glycoprotein

Ruiz

2021

Front. Physiol.

View full text Add to dashboard Cite

α1-acid glycoprotein (AGP), also known as Orosomucoid (ORM), belongs to the Lipocalin protein family and it is well-known for being a positive acute-phase protein. AGP is mostly found in plasma, with the liver as main contributor, but it is also expressed in other tissues such as the brain or the adipose tissue. Despite the vast literature on AGP, the physiological functions of the protein remain to be elucidated. A large number of activities mostly related to protection and immune system modulation have been described. Recently created AGP-knockout models have suggested novel physiological roles of AGP, including regulation of metabolism. AGP has an outstanding ability to efficiently bind endogenous and exogenous small molecules that together with the complex and variable glycosylation patterns, determine AGP functions. This review summarizes and discusses the recent findings on AGP structure (including glycans), ligand-binding ability, regulation, and physiological functions of AGP. Moreover, this review explores possible molecular and functional connections between AGP and other members of the Lipocalin protein family.

show abstract

Section: Xenobiotics-bindingmentioning

confidence: 99%