Nitric oxide produced by iNOS is associated with collagen synthesis in keloid scar formation

Hsu, Yi‐Chiang; Hsiao, Michael; Wang, Leng-Fang; Chien, Yie W.; Lee, William R.

doi:10.1016/j.niox.2006.01.006

Cited by 45 publications

(33 citation statements)

References 37 publications

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“…Collagen synthesis is important for wound healing, and its deposition in the extracellular matrix (ECM) of the wound is regulated by NO (Hsu et al 2006). However, the precise role of NO in the regulation of collagen synthesis is unclear, and the mechanisms whereby healing is enhanced are undetermined.…”

Section: Introductionmentioning

confidence: 99%

Organization of collagen bundles during tendon healing in rats treated with L-NAME

et al. 2009

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The Achilles tendon can support high tension forces and may experience lesions. The damaged tissue does not regenerate completely, with the organization and mechanical properties of the repaired tendon being inferior to those of a healthy tendon. Nitric oxide (NO) plays an important role in wound repair. We have examined the structural reorganization and repair in Achilles tendon after injury in rats treated with the NO synthase inhibitor L-NAME. The right Achilles tendon of male Wistar rats was partially transected. One group of rats was treated with L-NAME (~300 mg/kg per day, given in drinking water) for 4 days prior to tendon sectioning and throughout the post-operative period. Control rats received water without L-NAME. The tendons were excised at 7, 14, and 21 days post-injury and used to quantify hydroxyproline and for mechanical tests. Tendons were also processed for histomorphological analysis by polarized light microscopy, which showed that the collagen fibers were disorganized by day 7 in non-treated and L-NAME-treated rats. In non-treated rats, the organization of the extracellular matrix was more homogeneous by days 14 and 21 compared with day 7, although this homogeneity was less than that in normal tendon. In contrast, in injured tendons from L-NAME-treated rats, the collagen fibers were still disorganized on day 21. Tendons from treated rats had more hydroxyproline but lower mechanical properties compared with those from non-treated rats. Thus, NO modulates tendon healing, with a reduction in NO biosynthesis delaying reorganization of the extracellular matrix, especially collagen.

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Section: Introductionmentioning

confidence: 99%

Organization of collagen bundles during tendon healing in rats treated with L-NAME

et al. 2009

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“…There are enormous evidences that NO is an important factor in collagen metabolism [48][49][50] and remodelling phase of wound healing [51]. Moreover, exposure of keloid fibroblast to NO increased collagen expression [52]. The primary source of NO in healing wounds is iNOS activity [53], however in our study we show that ecNOS could be contributing to NO production in keloid.…”

Section: No Upregulation and Its Role In Excess Collagen Deposition Imentioning

confidence: 47%

Co-upregulation of Transforming Growth Factor Beta-1 and Nitric Oxide Synthase in Keloid by comparison to normal human skin-A possible role for TGFβ1 and NOS in pathogenesis of keloid

El-Aleem¹,

Abdelwahab²,

Osman³

2017

J Cytol Histol

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Keloid disease is a benign but progressive form of abnormal wound healing associated with skin fibrosis and can cause a major functional disability and morbidity. TGF beta (TGFβ) and Nitric Oxide (NO) are active biomarkers known to regulate phases of wound healing and have been implicated in pathogenesis of fibrotic disease. There are three isoforms of TGFβ (1, 2 and 3) TGFβ1 and 3 have a crucial role in fibrosis, with TGFβ1 profibrotic and TGFβ3 antifibrotic. NO is produced by Nitric Oxide Synthase (NOS) which exist in three isoforms, inducible NOS (iNOS), endothelial NOS (ecNOS) and neuronal NOS (nNOS). TGFβ isoforms and NO were found to be associated with fibrotic disorders affecting the skin. We hypothesis that the interaction between TGFβ and NO in keloid could promote the excessive collagen deposition associated with this disorder.Using immunohistochemistry, we investigated the profile of TGFβ isoforms (TGFβ1, 3) and NOS isoforms (iNOS and ecNOS) in keloid tissues and normal human skin. The cellular distribution of all the isoforms were studied and the protein levels were assessed by using H-Scoring and Image J Scoring systems.

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“…propria of the small intestine (Chakravortty, Kumar, 1997) and in the re-epithelialization of normal skin as part of the healing processes (Stallmeyer et al, 1999;Hsu et al, 2006). Witte and coworkers (2000) revealed that although the NO donor used in the study presented a cytostatic effect on fibroblasts, the administration of low concentrations of NO donor in rat dermal fibroblast cultures enhanced collagen synthesis.…”

Section: Discussionmentioning

confidence: 98%

The in vivo effect of L-arginine on skin elasticity in mice

Souza

Oliveira

Andrade

et al. 2017

Braz. J. Pharm. Sci.

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The human skin aging process is a complex mechanism that can be induced both by intrinsic and extrinsic factors. Observations include a decrease in the biosynthetic and proliferative capacity of cells, increased expression of matrix metalloproteinases, reduction in collagen type I expression, and the progressive disappearance of elastic tissue in the papillary dermis. L-arginine, the substrate of nitric oxide synthesis, is involved in angiogenesis and cell proliferation, as well as an indirect precursor of collagen synthesis via the proline pathway. The aim of this study was to examine the tensile strength, histology, and immunohistochemistry of female and male mice skin receiving different concentrations of topically applied L-arginine, in order to evaluate the possibility of using L-arginine as an active cosmetic ingredient in antiaging products. The results suggest that the application of L-arginine improves the mechanical resistance of skin from older female mice (20 weeks old) and promotes the formation of a larger amount of collagen and elastic fibers in the skin when applied at a concentration of 15%.

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Nitric oxide produced by iNOS is associated with collagen synthesis in keloid scar formation

Cited by 45 publications

References 37 publications

Organization of collagen bundles during tendon healing in rats treated with L-NAME

Organization of collagen bundles during tendon healing in rats treated with L-NAME

Co-upregulation of Transforming Growth Factor Beta-1 and Nitric Oxide Synthase in Keloid by comparison to normal human skin-A possible role for TGFβ1 and NOS in pathogenesis of keloid

The in vivo effect of L-arginine on skin elasticity in mice

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