[Study of the Mechanisms of Maintaining the Transparency of the Lens and Treatment of Its Related Diseases for Making Anti-cataract and/or Anti-presbyopia Drugs]

Yakugaku Zasshi. 2020;140(9):1095-1099. doi: 10.1248/yakushi.20-00120.
[Article in Japanese]

Abstract

The lens of the eye is an avascular and anuclear tissue that serves to focus objects on the retina. Cataract is opacity within the clear lens that changes the transparency and refractive index of the lens causing significant visual impairments. These impairments can severely restrict the ability to carry out daily activities. Cataracts is common among elderly person occurring in more than 80% of patients aged 80 or older. Notably, we have recently identified key compounds that are effective against cataract formation. Presbyopia is also an ocular disease that typically develops in people over the age of 45 while affecting almost 100% of people over the age of 65. Recent research suggests that age-related changes in hydrostatic pressure of the lens controlled by Na/K ATPase contribute to the development of presbyopia. In the lens, Na/K ATPase has been shown to be regulated by transient receptor potential cation channels, vanilloid 1 (TRPV1) and 4, thus suggesting the potential role of TRPV1 and TRPV4 in the development of presbyopia. This review article summarizes data obtained from our laboratory with my colleagues highlighting the critical role of aquaporin 0 (AQP0) in maintaining a healthy lens redox environment, key molecules that delay the onset of cataract in vivo, as well as potential mechanisms of lens hydrostatic pressure control that may be associated with presbyopia.

Keywords: cataract; lens; presbyopia.

Publication types

  • Review

MeSH terms

  • Aquaporins / physiology*
  • Cataract / drug therapy*
  • Cataract / etiology*
  • Drug Development*
  • Eye Proteins / physiology*
  • Hydrostatic Pressure
  • Lens, Crystalline / metabolism
  • Oxidation-Reduction
  • Presbyopia / etiology
  • Sodium-Potassium-Exchanging ATPase / metabolism
  • Sodium-Potassium-Exchanging ATPase / physiology
  • TRPV Cation Channels / physiology

Substances

  • Aquaporins
  • Eye Proteins
  • TRPV Cation Channels
  • TRPV1 protein, human
  • TRPV4 protein, human
  • aquaporin 0
  • Sodium-Potassium-Exchanging ATPase