Literature DB >> 1314568

Minoxidil specifically decreases the expression of lysine hydroxylase in cultured human skin fibroblasts.

T Hautala1, J Heikkinen, K I Kivirikko, R Myllylä.   

Abstract

The levels of lysine hydroxylase protein and the levels of the mRNAs for lysine hydroxylase and the alpha- and beta-subunits of proline 4-hydroxylase were measured in cultured human skin fibroblasts treated with 1 mM-minoxidil. The data demonstrate that minoxidil decreases the amount of lysine hydroxylase protein, this being due to a decrease in the level of lysine hydroxylase mRNA. The effect of minoxidil appears to be highly specific, as no changes were observed in the amounts of mRNAs for the alpha- and beta-subunits of proline 4-hydroxylase.

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Year:  1992        PMID: 1314568      PMCID: PMC1130991          DOI: 10.1042/bj2830051

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  22 in total

1.  Molecular biology of prolyl 4-hydroxylase.

Authors:  K I Kivirikko; T Helaakoski; K Tasanen; K Vuori; R Myllylä; T Parkkonen; T Pihlajaniemi
Journal:  Ann N Y Acad Sci       Date:  1990       Impact factor: 5.691

2.  Prolyl 4-hydroxylase: molecular cloning and the primary structure of the alpha subunit from chicken embryo.

Authors:  J A Bassuk; W W Kao; P Herzer; N L Kedersha; J Seyer; J A DeMartino; B L Daugherty; G E Mark; R A Berg
Journal:  Proc Natl Acad Sci U S A       Date:  1989-10       Impact factor: 11.205

3.  Post-translational processing of procollagens.

Authors:  K I Kivirikko; R Myllylä
Journal:  Ann N Y Acad Sci       Date:  1985       Impact factor: 5.691

4.  Increases in mRNA concentrations of the alpha and beta subunits of prolyl 4-hydroxylase accompany increased gene expression of type IV collagen during differentiation of mouse F9 cells.

Authors:  T Helaakoski; L Pajunen; K I Kivirikko; T Pihlajaniemi
Journal:  J Biol Chem       Date:  1990-07-15       Impact factor: 5.157

Review 5.  Protein hydroxylation: prolyl 4-hydroxylase, an enzyme with four cosubstrates and a multifunctional subunit.

Authors:  K I Kivirikko; R Myllylä; T Pihlajaniemi
Journal:  FASEB J       Date:  1989-03       Impact factor: 5.191

6.  Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex.

Authors:  J R Wetterau; K A Combs; S N Spinner; B J Joiner
Journal:  J Biol Chem       Date:  1990-06-15       Impact factor: 5.157

7.  Polyclonal and monoclonal antibodies to human lysyl hydroxylase and studies on the molecular heterogeneity of the enzyme.

Authors:  R Myllylä; L Pajunen; K I Kivirikko
Journal:  Biochem J       Date:  1988-07-15       Impact factor: 3.857

8.  Molecular cloning of a multifunctional chicken protein acting as the prolyl 4-hydroxylase beta-subunit, protein disulphide-isomerase and a cellular thyroid-hormone-binding protein. Comparison of cDNA-deduced amino acid sequences with those in other species.

Authors:  T Parkkonen; K I Kivirikko; T Pihlajaniemi
Journal:  Biochem J       Date:  1988-12-15       Impact factor: 3.857

9.  Human lysyl hydroxylase: purification to homogeneity, partial characterization and comparison of catalytic properties with those of a mutant enzyme from Ehlers-Danlos syndrome type VI fibroblasts.

Authors:  T M Turpeenniemi-Hujanen; U Puistola; K I Kivirikko
Journal:  Coll Relat Res       Date:  1981-07

10.  Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene.

Authors:  T Pihlajaniemi; T Helaakoski; K Tasanen; R Myllylä; M L Huhtala; J Koivu; K I Kivirikko
Journal:  EMBO J       Date:  1987-03       Impact factor: 11.598

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  2 in total

1.  [Androgenetic alopecia].

Authors:  R Hoffman
Journal:  Hautarzt       Date:  2004-01       Impact factor: 0.751

2.  Effects of minoxidil gel on burn wound healing in rats.

Authors:  Payam Khazaeli; Mohammad Karamouzian; Shohreh Rohani; Behnam Sadeghirad; Nima Ghalekhani
Journal:  Iran J Pharm Res       Date:  2014       Impact factor: 1.696

  2 in total

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