Transforming Growth Factor-β1 Modulates Myofibroblastic Phenotype of Rat Palatal Fibroblastsin Vitro

Yokozeki, Masahiko; Moriyama, Keiji; Shimokawa, Hitoyata; Kuroda, Takayuki

doi:10.1006/excr.1997.3473

Cited by 56 publications

(39 citation statements)

References 48 publications

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“…5C), indicating that 0.6 pg/ml was sufficient to cause the observed changes. These effective doses are similar to those reported for both vertebrate and invertebrate cells (38,44,60).…”

Section: Vol 71 2003 Mammalian Tgf-␤1 Modulates Mosquito Immunity 3005supporting

confidence: 87%

Mammalian Transforming Growth Factor β1 Activated after Ingestion byAnopheles stephensiModulates Mosquito Immunity

et al. 2003

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During the process of bloodfeeding by Anopheles stephensi, mammalian latent transforming growth factor ␤1 (TGF-␤1) is ingested and activated rapidly in the mosquito midgut. Activation may involve heme and nitric oxide (NO), agents released in the midgut during blood digestion and catalysis of L-arginine oxidation by A. stephensi NO synthase (AsNOS). Active TGF-␤1 persists in the mosquito midgut to extended times postingestion and is recognized by mosquito cells as a cytokine. In a manner analogous to the regulation of vertebrate inducible NO synthase and malaria parasite (Plasmodium) infection in mammals by TGF-␤1, TGF-␤1 regulates AsNOS expression and Plasmodium development in A. stephensi. Together, these observations indicate that, through conserved immunological cross talk, mammalian and mosquito immune systems interface with each other to influence the cycle of Plasmodium development.

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“…5C), indicating that 0.6 pg/ml was sufficient to cause the observed changes. These effective doses are similar to those reported for both vertebrate and invertebrate cells (38,44,60).…”

Section: Vol 71 2003 Mammalian Tgf-␤1 Modulates Mosquito Immunity 3005supporting

confidence: 87%

Mammalian Transforming Growth Factor β1 Activated after Ingestion byAnopheles stephensiModulates Mosquito Immunity

et al. 2003

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“…Overexpression of Barx2 in C3H10T1/2 cells increased SM-␣-actin expression and promoted cell spreading and formation of stress fibers. These morphological changes are consistent with differentiation of SMCs or myofibroblasts, cells that have contractile properties like smooth muscle, but retain characteristics of fibroblasts (33,55,56). Because the SM-␣-actin gene also contains a CArG box that binds to SRF (41), it is possible that induction of SM-␣-actin after overexpression of Barx2 is mediated by a complex of Barx2 and SRF.…”

Section: Discussionmentioning

confidence: 63%

The Homeodomain Protein Barx2 Promotes Myogenic Differentiation and Is Regulated by Myogenic Regulatory Factors

Meech

Makarenkova

Edelman

et al. 2003

Journal of Biological Chemistry

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“…Because TGF-β1 stimulation has been reported to induce α-SMA expression in fibroblasts as differentiation into myofibroblasts for 1 to 4 days, [19][20][21] we cultured the cells for 0 to 168 h (7 days) with TGF-β1 treatment to examine the effect of TGF-β1 on mRNA expression of α(IV) chains in TIG-1-20 cells at various time points. We confirmed that the mRNA expression of α1(IV) and α2(IV) chains was upregulated in TIG-1-20 cells up to 96 h (4days; Supplementary Figure 2).…”

Section: Deposition Of Type I Iii and Iv Collagens And α Chains Of mentioning

confidence: 99%

Role of α1 and α2 chains of type IV collagen in early fibrotic lesions of idiopathic interstitial pneumonias and migration of lung fibroblasts

Urushiyama

Terasaki

Nagasaka

et al. 2015

Laboratory Investigation

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Early fibrotic lesions are thought to be the initial findings of fibrogenesis in idiopathic interstitial pneumonias, but little is known about their properties. Type IV collagen comprises six gene products, α1-α6, and although it is known as a major basement membrane component, its abnormal deposition is seen in fibrotic lesions of certain organs. We studied the expression of type I and III collagen and all α chains of type IV collagen in lung specimens from patients with usual interstitial pneumonia (UIP) or organizing pneumonia (OP) via immunohistochemistry. With cultured lung fibroblasts, we analyzed the expression and function of all α chains of type IV collagen via immunohistochemistry, western blotting, realtime quantitative PCR, and a Boyden chamber migration assay after the knockdown of α1 and α2 chains. Although we observed type I and III collagens in early fibrotic lesions of both UIP and OP, we found type IV collagen, especially α1 and α2 chains, in early fibrotic lesions of UIP but not OP. Fibroblasts enhanced the expression of α1 and α2 chains of type IV collagen after transforming growth factor-β1 stimulation. Small interfering RNA against α1 and α2 chains increased fibroblast migration, with upregulated phosphorylation of focal adhesion kinase (FAK), and adding medium containing fibroblast-produced α1 and α2 chains reduced the increased levels of fibroblast migration and phosphorylation of FAK. Fibroblasts in OP were positive for phosphorylated FAK but fibroblasts in UIP were not. These results suggest that fibroblasts in UIP with type IV collagen deposition, especially α1 and α2 chains, have less ability to migrate from early fibrotic lesions than fibroblasts in OP without type IV collagen deposition. Thus, type IV collagen deposition in early fibrotic lesions of UIP may be implicated in refractory pathophysiology including migration of lesion fibroblasts via a FAK pathway.

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Transforming Growth Factor-β1 Modulates Myofibroblastic Phenotype of Rat Palatal Fibroblastsin Vitro

Cited by 56 publications

References 48 publications

Mammalian Transforming Growth Factor β1 Activated after Ingestion byAnopheles stephensiModulates Mosquito Immunity

Mammalian Transforming Growth Factor β1 Activated after Ingestion byAnopheles stephensiModulates Mosquito Immunity

The Homeodomain Protein Barx2 Promotes Myogenic Differentiation and Is Regulated by Myogenic Regulatory Factors

Role of α1 and α2 chains of type IV collagen in early fibrotic lesions of idiopathic interstitial pneumonias and migration of lung fibroblasts

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