Protein–Protein Interactions: Inhibition of Mammalian Carbonic Anhydrases I–XV by the Murine Inhibitor of Carbonic Anhydrase and Other Members of the Transferrin Family

The murine inhibitor of carbonic anhydrase (mICA), a member of the transferrin (TF) superfamily of proteins, together with human holo- and apoTF and lactoferrin (LF) were assessed as inhibitors of all catalytically active mammalian (h = human, m = murine) CA isoforms, from CA I to CA XV. mICA was a...

Full description

Saved in:
Bibliographic Details
Published in:Journal of medicinal chemistry 2012-06, Vol.55 (11), p.5529-5535
Main Authors: Durdagi, Serdar, Vullo, Daniela, Pan, Peiwen, Kähkönen, Niklas, Määttä, Juha A, Hytönen, Vesa P, Scozzafava, Andrea, Parkkila, Seppo, Supuran, Claudiu T
Format: Article
Language:English
Subjects:
Animals
Apoproteins - metabolism
Biological Assay
Biosensing Techniques
Calorimetry, Differential Scanning
Carbonic Anhydrases - metabolism
Humans
Isoenzymes - antagonists & inhibitors
Isoenzymes - metabolism
Mice
Protein Binding
Protein Denaturation
Protein Interaction Mapping
Transferrins - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The murine inhibitor of carbonic anhydrase (mICA), a member of the transferrin (TF) superfamily of proteins, together with human holo- and apoTF and lactoferrin (LF) were assessed as inhibitors of all catalytically active mammalian (h = human, m = murine) CA isoforms, from CA I to CA XV. mICA was a low nanomolar to subnanomolar inhibitor of hCAs I, II, III, VA, VB, VII and mCAs XV (K I of 0.7–44.0 nM) and inhibited the remaining isoforms with K I of 185.5–469 nM. hTF, apoTF, and hLF were inhibitors of most of these CAs but with reduced efficiency compared to mICA (K I of 18.9–453.8 nM). Biacore surface plasmon resonance and differential scanning calorimetry experiments were also used for obtaining more insights into the interaction between these proteins, which may be useful for drug design of protein-based CA inhibitors.
ISSN:0022-2623
1520-4804
DOI:10.1021/jm3004587