Abstract:
:Transforming growth factor-beta1 is known for its effect on the production of extracellular matrix in tendons. Elevated levels of transforming growth factor-beta1 have been reported in tendon adhesion and tendinosis, which suggests that transforming growth factor-beta1 plays an important role in matrix disturbances. Tendon adhesion involves excessive collagen deposition, whereas tendinosis is associated with increased proteoglycan deposition. It seems that other factors also may affect matrix deposition and modulate the effects of transforming growth factor-beta1. We assessed whether matrix anchorage to Type I collagen or fibronectin could change the gene expression of matrix proteins in tendon fibroblasts, and studied whether the effects of transforming growth factor-beta1 were altered by matrix anchorage. Human patellar tendon fibroblast cultures were prepared in different cell anchorages, and the cellular responses to transforming growth factor-beta1 were measured as gene expression of procollagen Type I, Type III, decorin, and biglycan by real-time reverse transcriptase-polymerase chain reaction. Fibronectin anchorage significantly increased the messenger ribonucleic acid level of decorin, and the messenger ribonucleic acid level of procollagen Type I was decreased by matrix anchorage to either fibronectin or Type I collagen. Transforming growth factor-beta1 increased the messenger ribonucleic acid level of procollagen Type I in Type I collagen-coated plates, but it suppressed the messenger ribonucleic acid level of decorin in fibronectin-coated plates. These findings suggest that interaction of matrix anchorage and transforming growth factor-beta1 is an important determinant of matrix deposition in healing tendons and the development of matrix disturbances in tendons.
journal_name
Clin Orthop Relat Resjournal_title
Clinical orthopaedics and related researchauthors
Fu SC,Wong YP,Cheuk YC,Lee KM,Chan KMdoi
10.1097/01.blo.0000145887.48534.6fsubject
Has Abstractpub_date
2005-02-01 00:00:00pages
226-32issue
431eissn
0009-921Xissn
1528-1132pii
00003086-200502000-00034pub_type
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