Work

Residue Gln-30 of human erythrocyte anion transporter is a prime site for reaction with intrinsic transglutaminase.

Year: 1994

Type: article

Abstract: Elevating the intracellular concentration of Ca2+ ions in human erythrocytes leads to the formation of membrane-associated polymers, composed of skeletal and cytoplasmic proteins. The anion transporter band 3 serves as a membrane anchor for this N epsilon-(gamma-glutamyl)lysine cross-linked polymer. The reaction is catalyzed by an intrinsic transglutaminase, and it can be observed in broken cells merely by the addition of Ca2+. Certain primary amines, such as dansylcadaverine, inhibit the process by virtue of competition against the epsilon-lysyl or donor functionalities of the protein substrates. Dansylcadaverine itself becomes incorporated into the enzyme-specific gamma-glutaminyl or acceptor residues, blocking these from participating in the formation of protein-to-protein cross-links. This labeling procedure, coupled with an anti-dansyl antibody affinity procedure to isolate dansyl-labeled compounds, was employed to identify Gln-30 as the preferred transglutaminase-reactive acceptor site in the band 3 protein.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(17)31731-3

Authors: S.N. Murthy, J. Wilson, Y. Zhang, L. Lorand

Institution: Northwestern University

Language: English

Topic: Blood properties and coagulation

Subfield: Pulmonary and Respiratory Medicine

Field: Medicine

Domain: Health Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

Funders: National Institutes of Health, National Heart, Lung, and Blood Institute