Wherefore art thou, YY1

Research output: Contribution to journalComment/debate

Abstract

In this issue, Taguchi et al. demonstrate that the transcription factor Yin Yang-1 (YY1) regulates proliferation in three-dimensional cultures of the HaCaT human keratinocyte cell line. HaCaT keratinocytes overexpressing YY1 form artificial epidermal constructs that are thicker than those produced from vector-transfected cells. RNA interference-mediated YY1 knockdown decreases the thickness of YY1-overexpressing constructs, indicating that YY1 mediates the thickening. In primary keratinocytes, overexpressed YY1 also inhibits differentiation marker expression induced by calcium, supporting the idea that YY1 is important in regulating epidermal structure and function.

Original languageEnglish (US)
Pages (from-to)11-12
Number of pages2
JournalJournal of Investigative Dermatology
Volume131
Issue number1
DOIs
StatePublished - Jan 1 2011

Fingerprint

Yin-Yang
Art
Keratinocytes
Differentiation Antigens
Cell culture
Transcription Factors
Cells
RNA
Calcium
RNA Interference
Cell Line

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Dermatology
  • Cell Biology

Cite this

Wherefore art thou, YY1. / Bollag, Wendy B; Bollag, Roni Jacob.

In: Journal of Investigative Dermatology, Vol. 131, No. 1, 01.01.2011, p. 11-12.

Research output: Contribution to journalComment/debate

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AB - In this issue, Taguchi et al. demonstrate that the transcription factor Yin Yang-1 (YY1) regulates proliferation in three-dimensional cultures of the HaCaT human keratinocyte cell line. HaCaT keratinocytes overexpressing YY1 form artificial epidermal constructs that are thicker than those produced from vector-transfected cells. RNA interference-mediated YY1 knockdown decreases the thickness of YY1-overexpressing constructs, indicating that YY1 mediates the thickening. In primary keratinocytes, overexpressed YY1 also inhibits differentiation marker expression induced by calcium, supporting the idea that YY1 is important in regulating epidermal structure and function.

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