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.

• Authors: K U Schallreuter, M R Pittelkow
• Journal: Archives of dermatological research (Arch Dermatol Res) Vol. 281 Issue 1 Pg. 40-4 ( 1989) ISSN: 0340-3696 [Print] Germany
• PMID: 2730141 (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)