ArticleThe Journal of membrane biology2007
Interactions of recombinant mouse erythrocyte transglutaminase with membrane skeletal proteins.
Article in The Journal of membrane biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 10 citations in OpenAlex.
- Transglutaminase-mediated remodeling of the human erythrocyte membrane skeleton: relevance for erythrocyte diseases with shortened cell lifespan.Advances in enzymology and related areas of molecular biology · 2011Review
- Erythrocyte tropomodulin isoforms with and without the N-terminal actin-binding domain.The Journal of biological chemistry · 2010Article
- Modulation of erythrocyte acetylcholinesterase activity and its association with G protein-band 3 interactions.The Journal of membrane biology · 2009Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transglutaminases (TGs) are a family of enzymes that catalyze the formation of covalent gamma-glutamyl-epsilon-lysine crosslinks between glutamine (Q) acyl-donors and lysine (K) acyl-acceptors. Here, we report the cDNA cloning of a TG from mouse reticulocytes, its 4.6-kb message size and high-yield synthesis of recombinant TG in yeast cultures. Its activity was assayed by crosslinking the amine of monodansylcadaverine (DC) onto casein and inside-out vesicles of erythrocytes. The latter contain TG substrates including the anion ion exchanger (AE1) or band 3, and the crosslinking activity was the highest at physiological [GTP] and [ATP] of erythrocytes. To study individually how TG interacts with band 3 and what role P4.2, a pseudo-TG that is normally associated with band 3, may play in their interaction, recombinant cytoplasmic domain of band 3 (cdb3) and P4.2 were also cloned by polymerase chain reaction from mouse reticulocytes, expressed and affinity-purified from Escherichia coli. Enzyme-linked immunosorbent assay and Western blot analysis revealed that increasing [CaCl(2)] enhanced TG-mediated crosslinking of DC to cdb3 but decreased TG binding to cdb3. P4.2 inhibited the TG-mediated crosslinking of cdb3 but stabilized the binding of TG to cdb3 in the presence of calcium. This in vitro study suggests a relationship among TG, cdb3 and P4.2 in erythrocyte membrane during calcium influx.
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