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Published on: January 7, 2019
Latent MMP-9 is bound to TIMP-1 before secretion
Martin Roderfeld1, Jürgen Graf, Bernd Giese
1Department of Medicine II, Gastroenterology, University Hospital Giessen & Marburg GmbH, Justus Liebig University Giessen, D-35392, Giessen, Germany.
Biological Chemistry
|November 3, 2007
Summary
Matrix metalloproteinase-9 (MMP-9) and tissue inhibitor of metalloproteinases-1 (TIMP-1) form complexes within the Golgi apparatus. This intracellular complex formation of proMMP-9 and TIMP-1 may impact biochemical processes.
Area of Science:
- Biochemistry
- Cell Biology
- Molecular Biology
Background:
- Matrix metalloproteinase-9 (MMP-9) and tissue inhibitor of metalloproteinases-1 (TIMP-1) regulate extracellular matrix (ECM) remodeling.
- MMP-9 and TIMP-1 form complexes, influencing physiological and pathological processes.
- Previous studies observed intracellular co-localization, but the origin of complex formation was unclear.
Purpose of the Study:
- To investigate the subcellular origin of proMMP-9 and TIMP-1 complex formation.
- To determine where the latent enzyme and its inhibitor first associate within the cell.
Main Methods:
- Utilized fluorescence resonance energy transfer (FRET) in co-transfected human hepatoma cells.
- Fused MMP-9 and TIMP-1 to cyan (CFP) and yellow (YFP) fluorescent proteins.
- Analyzed intracellular distribution using confocal laser scanning microscopy.
Main Results:
- Demonstrated FRET between MMP-9-CFP and TIMP-1-YFP, indicating intracellular complex formation.
- Verified complex formation within the Golgi apparatus.
- Showed that the proMMP-9-TIMP-1 complex is present in the Golgi.
Conclusions:
- The proMMP-9-TIMP-1 complex forms intracellularly, specifically within the Golgi apparatus.
- This finding has potential implications for intracellular and extracellular biochemical processes involving proMMP-9.
- Further research is needed to determine the functional relevance and magnitude of this observation.
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