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Biosynthesis, post-translation modification, and functional characterization of Drm/Gremlin
1Intramural Research Support Program, SAIC Frederick, NCI-Frederick Cancer Research and Development Center, Frederick, Maryland 21702-1201, USA.
The Journal of Biological Chemistry
|March 18, 2000
Summary
Down-regulated by mos (Drm)/Gremlin protein exists in secreted and cell-associated forms, affecting cell signaling. Both forms antagonize bone morphogenetic protein signaling, suggesting a role in development and transformation.
Area of Science:
- Molecular Biology
- Developmental Biology
- Cell Biology
Background:
- Down-regulated by mos (Drm)/Gremlin is a conserved protein implicated in development and cell transformation.
- Its precise role and molecular processing require further investigation.
Purpose of the Study:
- To investigate the biosynthesis and processing of Drm/Gremlin.
- To determine the functional properties of different Drm/Gremlin forms.
Main Methods:
- Metabolic labeling of cells expressing Drm/Gremlin.
- SDS-polyacrylamide gel electrophoresis for protein analysis.
- Confocal immunofluorescent microscopy.
- Binding assays with bone morphogenetic protein-4.
Main Results:
- Drm/Gremlin is synthesized and processed into glycosylated and nonglycosylated forms.
- Both forms are secreted and cell-associated, with distinct half-lives.
- Drm/Gremlin localizes to the endoplasmic reticulum, Golgi, and cell surface.
- Both forms antagonize bone morphogenetic protein signaling and bind BMP-4.
Conclusions:
- Drm/Gremlin exists in multiple forms with distinct localization and stability.
- These forms interfere with bone morphogenetic protein signaling, potentially at the cell surface.
- Drm/Gremlin likely plays a role in tissue development and cell transformation.