Localisation of alpha(2,3) and alpha(2,6) linked terminal sialic acid groups in human trabecular meshwork.
Sialic acid specific lectins were used to localise isomers of sialyl glycosides in human trabecular meshwork (TM) at the ultrastructural level. A lectin immunogold method demonstrated that sialic groups were concentrated on the endothelial surface of Schlemm's canal (SC) and in the adjacent juxta-canalicular tissue (JCT). One sialyl glycoside, alpha(2,6) linked N-acetyl neuraminic acid, was present mainly on the luminal aspect of the SC endothelium and in the cytoplasm of the JCT cells. Another, alpha(2,3) linked N-acetyl neuraminic acid, was localised predominantly to the extracellular fibrillar material of the JCT. The existence of a topographical segregation of these two sialyl glycosides within the TM supports the view that highly charged anionic molecules may be of significance in regulating aqueous outflow.
Chapman
S A
SA
Department of Pathological Sciences, University of Manchester.
Bonshek
R E
RE
Stoddart
R W
RW
Mackenzie
K R
KR
McLeod
D
D
D000328:Adult; D000368:Aged; D000369:Aged, 80 and over; D001710:Biotin; D006801:Humans; D037102:Lectins; D008875:Middle Aged; D010835:Phytohemagglutinins; D037121:Plant Lectins; D054788:Ribosome Inactivating Proteins; D012794:Sialic Acids / Q000032:analysis*; D014129:Trabecular Meshwork / Q000737:chemistry*
D037102:Lectins; C042962:Limax flavus agglutinin; D010835:Phytohemagglutinins; D037121:Plant Lectins; C050600:Sambucus nigra lectins; D012794:Sialic Acids; C100156:leukoagglutinins, plants; D001710:Biotin; D054788:Ribosome Inactivating Proteins