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Thrombospondin induces glomerular mesangial cell adhesion and migration
G Taraboletti1, M Morigi, M Figliuzzi
1Istituto di Ricerche Farmacologiche Mario Negri, Bergamo, Italy.
Summary
Thrombospondin (TSP) enhances mesangial cell adhesion and motility. This glycoprotein acts as a potential regulator for mesangial cell functions in both normal and pathological conditions.
Area of Science:
- Cell Biology
- Biochemistry
- Extracellular Matrix Research
Background:
- Extracellular matrix components influence mesangial cell functions like adhesion, motility, and proliferation.
- Mesangial cells secrete thrombospondin (TSP), a glycoprotein involved in development, healing, and tumorigenesis.
Purpose of the Study:
- To functionally and molecularly characterize thrombospondin (TSP) interactions with mesangial cells.
Main Methods:
- Mesangial cell adhesion to TSP-coated surfaces and chemotaxis were assessed.
- Heparin, monoclonal antibodies against TSP domains, and TSP fragments were used to identify active domains.
Main Results:
- TSP dose-dependently induced mesangial cell adhesion and chemotaxis.
- Adhesion was inhibited by anti-TSP antiserum and an anti-CD36 antibody with heparin.
- The carboxy-terminal end of TSP retained adhesive properties, while all fragments exhibited chemotactic activity.
Conclusions:
- TSP modulates mesangial cell adhesion and motility.
- TSP may function as an autocrine and paracrine regulator in normal and pathological mesangial cell processes.