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Arginine-specific ADP-ribosyltransferases in leukocytes
B A Saxty1, P Kefalas, M Yadollahi-Farsani
1Division of Medicine, Imperial College School of Medicine, London, United Kingdom.
Journal of Leukocyte Biology
|February 20, 1998
Summary
ADP-ribosyltransferases modify proteins in leukocytes, playing roles in immune responses and cell movement. Further research suggests involvement in surface integrin functions.
Area of Science:
- Biochemistry
- Immunology
- Cell Biology
Background:
- ADP-ribosyltransferases (ARTs) mediate protein posttranslational modification via ADP-ribose group addition.
- These enzymes are widely expressed in eukaryotic tissues, notably in leukocytes like neutrophils and lymphocytes.
- The DNA encoding arginine-specific ARTs has been cloned, revealing conserved structures, especially in NAD+ binding and catalytic domains.
Purpose of the Study:
- To review recent advances in the field of ADP-ribosyltransferases in leukocytes.
- To highlight the known functions and potential roles of these enzymes in cellular processes.
Main Methods:
- Review of existing literature on ADP-ribosyltransferases.
- Analysis of cloned DNA sequences for conserved domains.
- Identification of known protein substrates and implicated cellular functions.
Main Results:
- ADP-ribosyltransferases are often cell-surface-associated or released from the cell surface.
- The catalytic activity of ARTs has been linked to immune responses and leukocyte chemotaxis.
- Specific protein substrates for some ARTs have been identified.
Conclusions:
- ADP-ribosyltransferases are crucial enzymes involved in leukocyte function.
- Emerging evidence points to their significant role in immune responses and cell migration.
- Future research is expected to link ARTs to additional leukocyte functions, particularly those involving surface integrins.