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Regulation of thioredoxin reductase by calcium in Hermansky-Pudlak syndrome.

Abstract
Cell cultures of keratinocytes, established from four Hermansky-Pudlak syndrome (HPS) homozygotes yielded low membrane-associated thioredoxin reductase activities compared with normal healthy adult controls. This low activity has been shown to be caused by a special sensitivity of the enzyme to calcium. 45Calcium has been used to compare the kinetics for the transport and bioaccumulation of this regulatory cation in keratinocyte cultures of a kindred with HPS (i.e., one HPS homozygote, one HPS obligate heterozygote, one normal family member, and healthy adult controls). The results show that both HPS-homozygous and -heterozygous cells bind more extracellular calcium than noncarriers of this genetic defect, and HPS homozygous cells appear to have a defective calcium transport system.
AuthorsK U Schallreuter, M R Pittelkow
JournalArchives of dermatological research (Arch Dermatol Res) Vol. 281 Issue 1 Pg. 40-4 ( 1989) ISSN: 0340-3696 [Print] GERMANY, WEST
PMID2730141 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)
Chemical References
  • NADH, NADPH Oxidoreductases
  • Thioredoxin-Disulfide Reductase
  • Calcium
Topics
  • Absorption
  • Adult
  • Albinism
  • Biological Transport
  • Blood Platelet Disorders
  • Calcium (analysis, pharmacokinetics)
  • Female
  • Humans
  • In Vitro Techniques
  • Male
  • NADH, NADPH Oxidoreductases (metabolism)
  • Skin Diseases (metabolism)
  • Syndrome
  • Thioredoxin-Disulfide Reductase (metabolism)

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