Investigation of luminal surface structures of rod photoreceptor outer segments by lectin cytochemistry combined with freeze-etching

Makoto Ishikawa, Akira Tonosaki, Tohru Abe, Shozo Sakuragi

Research output: Contribution to journalArticlepeer-review

Abstract

The luminal surface of the rod photoreceptor disk membrane was exposed by means of osmotic shock and labeled with ferritin-conjugated concanavalin A. The structural changes of the luminal surface were examined by a freeze-etching procedure with cryoprotectant (methanol). On replicas from freeze-etched membranes with concanavalin A labeling, 6- to 10-nm particles were codistributed with ferritin particles on the luminal surface of the disk membrane. By contrast, there were few ferritin particles or less numerous 6- to 10-nm particles on the corresponding surface without concanavalin A labeling. If 6- to 10-nm particles corresponded to the carbohydrate moiety of rhodopsin, concanavalin A binding might tend to preserve this carbohydrate moiety. These results suggest that the two-dimensional analysis of lectin-induced structural changes of the membrane surface glycoconjugates may become available by lectin cytochemistry combined with freeze-etching.

Original languageEnglish
Pages (from-to)267-272
Number of pages6
JournalOphthalmic Research
Volume31
Issue number4
DOIs
Publication statusPublished - 1999 Jul
Externally publishedYes

Keywords

  • Carbohydrate moiety
  • Concanavalin A
  • Disk membrane
  • Freeze-etching
  • Luminal surface
  • Rhodopsin
  • Rod photoreceptor cell

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems
  • Cellular and Molecular Neuroscience

Fingerprint

Dive into the research topics of 'Investigation of luminal surface structures of rod photoreceptor outer segments by lectin cytochemistry combined with freeze-etching'. Together they form a unique fingerprint.

Cite this