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Osteopontin, a substrate for transglutaminase and factor XIII activity
C W Prince1, D Dickie, C L Krumdieck
1Department of Nutrition Sciences, University of Alabama, Birmingham 35294.
Biochemical and Biophysical Research Communications
|June 28, 1991
Summary
Osteopontin (OPN) acts as a substrate for transglutaminase enzymes, incorporating radiolabeled putrescine. This suggests OPN
Area of Science:
- Biochemistry
- Cell Biology
- Extracellular Matrix Research
Background:
- Osteopontin (OPN) is an extracellular matrix cell adhesion protein.
- The functional roles of OPN are diverse, including roles in bone homeostasis, tumorigenesis, and immune responses.
Purpose of the Study:
- To investigate whether Osteopontin (OPN) serves as a substrate for transglutaminase enzymes.
- To explore the implications of OPN's potential cross-linking by transglutaminases for its extracellular functions.
Main Methods:
- Incubation of Osteopontin (OPN) with a commercial preparation of guinea pig liver transglutaminase.
- Assay for the incorporation of radiolabeled putrescine into OPN.
- Preliminary investigation using plasma transglutaminase, Factor XIIIa.
Main Results:
- Osteopontin (OPN) was confirmed as a substrate for guinea pig liver transglutaminase, with radiolabeled putrescine incorporation.
- Preliminary data indicate that OPN is also a substrate for plasma transglutaminase, Factor XIIIa.
- The identified cross-linking capacity of OPN was demonstrated.
Conclusions:
- Osteopontin (OPN) can be modified by transglutaminases, suggesting a mechanism for its extracellular localization.
- This cross-linking may influence OPN's involvement in critical physiological and pathological processes.
- Further research is needed to identify in vivo protein substrates of OPN and fully elucidate its functional consequences.