TGFβ affects collagen cross-linking independent of chondrocyte phenotype but strongly depending on physical environment

Jazyk: angličtina
Rok vydání: 2008
Předmět:
Technology
Gelation
Cross linking
Collagen type 2
Primary cells
Smooth muscle actin (SMA)
Collagen type 1
Transcription factor Sox9
Cultures (Traditional)
Animal tissue
Painting
Physical environments
Collagen cross-linking
Photoacoustic effect
Alginate gel (AG)
Alginic acid
Cell proliferation
Priority journal
Gene expression regulation
Cobalt compounds
Cultured
SOX9 Transcription Factor
Cobalt
Extracellular matrix
Immunohistochemistry
Mechanical stressing
Tissue culture
Body fluids
Phenotype
Cross-Linking Reagents
Tissue culture plastic (TCP)
Fibroblast
Muscle
Collagen
Smooth
Animal cell
Alpha smooth muscle actin
Cells
Collagen deposition
Matrix algebra
Cell population
Cartilage tissue engineering
Article
Collagen Type I
Shape memory effect
Transforming growth factor beta2
Matrix formation
Chondrocytes
Smooth muscle
Upregulation
Genetics
Animals
Electron energy levels
Tissue engineering
Colloids
Transforming Growth Factor (TGF)
Biology
Collagen Type II
Actin
Tissue
Shape memory alloy (SMA) fibers
Animal
Alginate
Cross linking reagent
DNA
Fibroblasts
Chondrocyte
Nonhuman
Cell populations
Actins
Monolayer cultures
Drug effect
Metabolism
Cartilage cell
Calf (bovine)
Transforming growth factor beta
Cattle
Cell culture
Cytology
Controlled study
Popis: Transforming growth factor beta (TGFβ) is often used in cartilage tissue engineering to increase matrix formation by cells with various phenotypes. However, adverse effects of TGFβ, such as extensive cross-linking in cultured fibroblasts, have also been reported. Our goal was to study effects of TGFβ on collagen cross-linking and evaluating the role of cellular phenotype and physical environment. We therefore used four different cell populations in two very different physical environments: primary and expanded chondrocytes and fibroblasts embedded in alginate gel and attached to tissue culture plastic. Matrix production, collagen cross-linking, and α-smooth muscle actin (αSMA) were analyzed during 4 weeks with or without 2.5 ng/mL TGFβ2. TGFβ2 did not affect collagen deposition by primary cells. In expanded cells, TGFβ2 increased collagen deposition. Chondrocytes and fibroblasts in monolayer produced more collagen cross-links with TGFβ2. In alginate, primary and expanded cells displayed an unexpected decrease in collagen cross-linking with TGFβ2. αSMA was not present in alginate cultures and barely upregulated by TGFβ2. Organized αSMA fibers were present in all monolayer cultures and became more pronounced with TGFβ2. This study demonstrates that the physical environment determined by the substrate used co-determines the response of cells to TGFβ. The presence of mechanical stress, determined with αSMA-staining, is probably responsible for the increase in collagen cross-linking upon addition of TGFβ. © Copyright 2008, Mary Ann Liebert, Inc.
Databáze: OpenAIRE