Effects of epidermal growth factor and transforming growth factor alpha on the function of wool follicles in culture

Bond, J. J.; Wynn, PC; Moore, George T.

doi:10.1007/s004030050066

Cited by 7 publications

(10 citation statements)

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“…In the present study, EGF treatment or overexpression of EGF accelerated the proliferation of the ORS cells. The mitogenic effect of EGF on the cultured ORS cells is consistent with previous studies [7,23]. In addition, EGF also promoted the migration of ORS cells.…”

Section: Egf Promotes Proliferation and Migration Of Ors Cellssupporting

confidence: 91%

“…These observations demonstrated a dynamic expression of EGFR during the initiation and cyclic growth of hair follicles, suggesting a spatiotemporal regulation of EGF signaling in follicle development and growth. Previous studies have shown that EGF can stimulate a mitogenic response in ORS cells in vitro and in vivo [6,7], yet the underlying mechanism remains elusive.…”

Section: Introductionmentioning

confidence: 99%

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Epidermal Growth Factor Promotes Proliferation and Migration of Follicular Outer Root Sheath Cells via Wnt/β-Catenin Signaling

Zhang

Nan²,

Wang³

et al. 2016

Cell Physiol Biochem

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Background/Aims: To investigate the effect and molecular mechanism of EGF on the growth and migration of hair follicle outer root sheath (ORS) cells. Methods: Intact anagen hair follicles were isolated from mink skin and cultured with EGF in vitro to measure ORS daily growth. Meanwhile, purified primary ORS cells were treated or transfected with EGF, and their proliferation and migration were assessed by MTT assay and transwell assay, respectively. The signaling pathway downstream of EGF was characterized by using the Wnt/β-catenin signaling inhibitor, XAV-939. Results: EGF of 2-20 ng/ml, not higher or lower, promoted the growth of follicular ORS in vitro. EGF treatment or overexpression promoted the proliferation and migration of ORS cells. Moreover, EGF stimulation induced nuclear translocation of β-catenin, and upregulated the expression of Wnt10b, β-catenin, EGF receptor and SOX9. Inhibition of Wnt/β-catenin signaling by XAV-939 significantly reduced the basal and EGF-enhanced proliferation and migration of ORS cells. In addition, a number of follicle-regulatory genes, such as Survivin, Msx2 and SGK3, were upregulated by EGF in the ORS cells, which was also inhibited by XAV-939. Conclusion: EGF promotes the proliferation and migration of ORS cells and modulates the expression of several follicle-regulatory genes via Wnt/β-catenin signaling.

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Section: Egf Promotes Proliferation and Migration Of Ors Cellssupporting

confidence: 91%

Section: Introductionmentioning

confidence: 99%

Epidermal Growth Factor Promotes Proliferation and Migration of Follicular Outer Root Sheath Cells via Wnt/β-Catenin Signaling

Zhang

Nan²,

Wang³

et al. 2016

Cell Physiol Biochem

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“…These results are consistent with those described by Philpott and Kealey (1994) in human hair follicles with the response resembling the anagen-catagen transition described in sheep follicles (Panaretto et al, 1984). Responses to EGF in sheep wool follicles have been reported by Bond et al (1996) and Ansari-Renani and Hynd (2004). The data presented thus indicate concentration-dependent effects on mohair follicles and confirm, and taking into account the activity of mouse-derived growth factor, an apparent conservation of biological activity of EGF across species.…”

Section: Collection and Preparation Of Hair Folliclessupporting

confidence: 92%

“…Similar methodology has been successfully applied to investigations of sheep wool follicles (AnsariRenani and Hynd, 2004;Bond et al, 1996). This current study reviews selected results from the application of this in vitro technique in our research programmes that studied the chemical regulation and nutrition of pelage secondary hair follicles from major fibre-bearing ruminant animal species.…”

Section: Introductionmentioning

confidence: 95%

In vitro methodology, hormonal and nutritional effects and fibre production in isolated ovine and caprine anagen hair follicles

Galbraith

2010

Animal

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Mammalian hair follicles are complex multicellular structures in the skin, which produce hair fibre under the influence of locally produced and systemic signalling systems. Investigation to determine mechanisms of regulation, follicular responses and the importance of nutritional supply have utilised a number of in vivo and in vitro approaches. Included in these are studies on isolated intact anagen secondary follicles singly or in groups with incubation in culture medium. These utilise techniques developed for investigation of follicles from human skin. Results from selected studies reviewed here demonstrate differences in capacity for hair growth and protein synthesis between secondary follicles from Angora and cashmere-bearing goats. Mohair follicles were shown to exhibit faster hair shaft elongation both in vivo and in vitro, to have greater DNA content per follicle and to deposit significantly more protein per follicle and per unit of DNA. Incubation of anagen mohair and cashmere follicles in the presence of melatonin or prolactin showed positive responses in hair shaft growth and protein synthesis to both signalling molecules. This result indicated directly acting effects on the follicle in addition to any indirect effects arising at a whole animal level in response to, for example, variation in photoperiod. Similarly, epidermal growth factor was shown to alter elongation and protein synthesis in mohair follicles and to produce, at higher concentration, club hair structures similar to effects observed in other species. The vitamin biotin was shown to be important in maintaining viability of isolated sheep secondary hair follicles where supplementation increased the proportion continuing to grow. Effects on growth and apparent protein synthesis suggested comparatively lesser effects on follicles, which remained viable. Histology on follicles indicated effects of biotin deficiency in reducing proliferation of basal keratinocytes. The final study, included in this review, demonstrated that supply of the essential sulphur-containing amino acid L-methionine was necessary to maintain the viability and growth of mohair follicles. L-cysteine was not required in the presence of L-methionine, although there was evidence of an optimisation when both amino acids were present in adequate concentrations. Consideration is given to the importance of transport mechanisms and capacity to utilise absorbed nutrients when considering optimising nutritional supply to individual follicles. These may then provide targets for attainment in applied nutrition of animals in vivo.Keywords: hair follicle, in vitro culture, cashmere, mohair, sheep wool ImplicationsHair fibres are products with value depending on quality and quantity produced. We require information to optimise breeding and husbandry of fibre-producing animals. This includes better understanding of the hair follicles in skin, which produce fibre. This report reviews results from in vitro studies on follicles removed from skin of sheep and goats. It describes how: (i) var...

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“…In order to investigate and understand the mechanisms involved in the control of keratin gene expression, in vitro experimental systems are required. Culture systems for intact wool 4 –6 and hair follicles have been successfully established 7 –9 . Although human and rat germinative/matrix cell culture systems have been reported, 10 –13 there have been no previous reports of wool follicle matrix cell culture.…”

mentioning

confidence: 99%

Wool follicle matrix cells: culture conditions and keratin expressionin vitro

Bates

Penno

Hynd

1999

British Journal of Dermatology

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Wool follicle matrix cell cultures were initiated as explants from Tukidale (carpet wool) sheep primary follicle bulbs after removal of the outer root sheath. Successful explantation required coculture on collagen with intact dermal papillae. Cells had a typical epidermal morphology (pavements of flattened. polyhedral cells). Extracellular matrix from dermal papillae, conditioned media, separation of dermal papilla from bulb matrices by tissue culture inserts and feeder layers were unable to support matrix cell explantation. Cultures could be maintained for up to 14 passages during which time the cells became larger with an increased cytoplasmic/nuclear ratio and irregular outline. Proliferation of matrix cells was greater on laminin than with either collagen type I or type IV. Proliferation was considerably reduced under serum-free conditions. This was most apparent at low calcium (0.09 mmol/L). By Northern hybridization matrix cells were found to express keratin K18 at all stages of culture. Keratin K 1.15 expression was evident by the tenth passage. The wool-specific keratin K2.10 was not detected. The data demonstrate that successful wool matrix cell culture is achievable. Keratin gene expression occurs in these cells and varies with the stage of culture.

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Effects of epidermal growth factor and transforming growth factor alpha on the function of wool follicles in culture

Cited by 7 publications

References 0 publications

Epidermal Growth Factor Promotes Proliferation and Migration of Follicular Outer Root Sheath Cells via Wnt/β-Catenin Signaling

Epidermal Growth Factor Promotes Proliferation and Migration of Follicular Outer Root Sheath Cells via Wnt/β-Catenin Signaling

In vitro methodology, hormonal and nutritional effects and fibre production in isolated ovine and caprine anagen hair follicles

Wool follicle matrix cells: culture conditions and keratin expressionin vitro

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