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The activities of MMP-9 and total gelatinase respond differently to substrate coating and cyclic mechanical stretching in fibroblasts and myoblasts
- Source :
- Cell Biology International. 34:587-591
- Publication Year :
- 2010
- Publisher :
- Wiley, 2010.
-
Abstract
- The current study was designed to investigate whether the activities of TGC (total gelatinase and collagenase) as well as MMP-9 (matrix metalloproteinase-9, gelatinase B) secreted by the cultured fibroblasts and myoblasts were influenced by the specific extracellular substrates and by cyclic mechanical strain. Fibroblasts (Rat 2) and myoblasts (C2C12) were cultured with either fibronectin, laminin or collagen type I for 24 h and applied with or without a biaxial deformation at 1 Hz using the Flexcell FX-4000 system. MMP-9 activity was increased in fibroblasts when the cells were in contact with fibronectin and laminin, while in myoblasts, enhanced activity of the secreted enzyme was only observed when collagen was present. TGC activity expressed from myoblasts was increased in cells growing on all three types of extracellular proteins in response to the mechanical stimulation, but in fibroblasts, such an increase was only observed in cells grown on the laminin coating. In summary, our data demonstrate that the activities of MMP-9 synthesized by fibroblasts tend to be regulated by the specific extracellular protein the cells are in contact with, whereas the gelatinolytic actions of proteases produced by myoblasts are more responsive to the mechanical deformation.
- Subjects :
- Matrix (biology)
Cell Line
Myoblasts
Mice
Laminin
medicine
Extracellular
Animals
Gelatinase
Collagenases
Fibroblast
biology
Chemistry
Cell Biology
General Medicine
Fibroblasts
Extracellular Matrix
Fibronectins
Rats
Cell biology
Fibronectin
medicine.anatomical_structure
Matrix Metalloproteinase 9
Biochemistry
Gelatinases
Collagenase
biology.protein
Stress, Mechanical
C2C12
medicine.drug
Subjects
Details
- ISSN :
- 10958355 and 10656995
- Volume :
- 34
- Database :
- OpenAIRE
- Journal :
- Cell Biology International
- Accession number :
- edsair.doi.dedup.....e1ff2d96f67f40cb81f71c66a356c5d0