Cell-mediated contraction of collagen lattices in serum-free medium: Effect of serum and nonserum factors

Anderson, Steven N.; Ruben, Zadok; Fuller, G. C.

doi:10.1007/bf02624156

Cited by 27 publications

(18 citation statements)

References 23 publications

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“…DEs were cast with 400 ml of respective cellular and acellular DE solution per well and left to polymerize at 37 1C for 1 h. Following collagen polymerization, 1.0 ml of DMEM supplemented with 10% FBS was added to each DE. Maximal contraction of this model system is achieved with 10% FBS [32,35,36]. At this stage, TGF-b1 was added directly to the medium at 10 ng/ml (final concentration).…”

Section: Dermal Equivalent Fabricationmentioning

confidence: 99%

The effect of the amelogenin fraction of enamel matrix proteins on fibroblast-mediated collagen matrix reorganization

et al. 2006

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Section: Dermal Equivalent Fabricationmentioning

confidence: 99%

The effect of the amelogenin fraction of enamel matrix proteins on fibroblast-mediated collagen matrix reorganization

et al. 2006

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“…PDGF-BB promotes the synthesis of the a2 integrin subunit, 1 increases the expression of stress fibers, 14 and stimulates collagen gel contraction by fibroblasts. 3,11,30,32 TGF-b1 can mediate gel contraction by increasing a2b1, decreasing a3b1, and halting the expression of a1b1 in some cell lines, 53 as well as increasing the expression of actin and stress fibers in fibroblasts. 15 TGF-b1 has also been shown to stimulate collagen gel contraction by fibroblasts.…”

Section: Introductionmentioning

confidence: 99%

Collagen Gel Anisotropy Measured by 2-D Laser Trap Microrheometry

Parekh

Velegol

2007

Ann Biomed Eng

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Collagen gels can serve as biomaterials ideal for tissue equivalents, especially if they are remodeled to have fibril anisotropy mimicking native tissue. Type I collagen gel remodeling was studied microscopically to investigate the changes caused by fibroblasts in collagen gel structures, with and without the growth factors PDGF-BB and TGF-beta1. A bidirectional laser trap microrheometry technique was developed that revealed a high degree of local heterogeneity and anisotropy in the structure of the collagen gels during active fibroblast contraction. The use of the growth factors increased not only the gel anisotropy, but the heterogeneity as well, indicating further changes in the collagen fibril orientations. This work shows the ability to influence the remodeling capabilities of fibroblasts by using growth factors in order to begin to elucidate the changes in the local mechanical environment of contracting collagen gels. We present this experimental technique as a method for probing changes in the fibroblast-driven anisotropy of collagen gels as a basis for understanding microstructural tissue organization important in the development of collagen-based tissue equivalents.

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“…The contraction of collagen lattices is enhanced by various physiological mediators, such as transforming growth factor‐β, 5 platelet‐derived growth factor, 6,7 endothelin, 8 or insulin. 9 …”

Section: Introductionmentioning

confidence: 99%

Mast cells enhance contraction of three‐dimensional collagen lattices by fibroblasts by cell–cell interaction: role of stem cell factor/c‐kit

Yamamoto¹,

Hartmann²,

Eckes³

et al. 2000

Immunology

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SUMMARYReorganization of the extracellular matrix is important in many biological and pathophysiological processes, including tissue remodelling, wound healing, or cancer metastasis. The ability of cultured ®broblasts to reorganize and contract three-dimensional type I collagen gels is regarded as an in vitro model for this process. In tissue ®brosis, complex interactions among ®broblasts, in¯ammatory cells and the extracellular matrix are taking place. Mast cells have often been discussed to play a role in several ®brotic conditions including scleroderma, scar formation, or wound healing. In this study, we examined the effects of mast cells on contraction of collagen lattices. The results demonstrate that co-culture of dermal ®broblasts with a human mast cell line (HMC-1) signi®cantly enhanced contraction of the three-dimensional collagen lattices, whereas mast cells alone failed to contract the gel. Addition of culture supernatants of mast cells did not enhance the speed of gel contraction, indicating the importance of cell±cell contact. Morphological analysis showed that mast cells were incorporated into the lattices. Histological examination also demonstrated that within the lattices, mast cells were localized in close contact to, or attached to, ®broblasts. As ®broblasts and mast cells are known to attach via stem cell factor (SCF)/c-kit interaction when co-cultured in monolayers, we also examined the effect of antibodies against SCF and c-kit in this system. Addition of both antibodies inhibited gel contraction up to 70%. In contrast, antibodies against interleukin-4 (IL-4) and IL-4 receptor did not affect gel contraction. These results indicate that mast cells enhance ®broblast-mediated contraction of collagen lattices via direct cell±cell contact, mediated in part by SCF/c-kit interactions.

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Cell-mediated contraction of collagen lattices in serum-free medium: Effect of serum and nonserum factors

Cited by 27 publications

References 23 publications

The effect of the amelogenin fraction of enamel matrix proteins on fibroblast-mediated collagen matrix reorganization

The effect of the amelogenin fraction of enamel matrix proteins on fibroblast-mediated collagen matrix reorganization

Collagen Gel Anisotropy Measured by 2-D Laser Trap Microrheometry

Mast cells enhance contraction of three‐dimensional collagen lattices by fibroblasts by cell–cell interaction: role of stem cell factor/c‐kit

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