Differential glycosylation and proteolytical processing of LeechCAM in central and peripheral leech neurons.
LeechCAM is a recently described member of the Ig-superfamily which has five Ig-domains, two FNIII-domains, a transmembrane domain, and a cytoplasmic domain. Phylogenetic analysis indicated that LeechCAM is the leech homolog of apCAM, FasII, and vertebrate NCAM. Using a leechCAM-specific monoclonal antibody we show by immunoblot analysis and by Triton X-114 phase separation experiments that in addition to existing in a transmembrane version LeechCAM is likely to be proteolytically cleaved into a secreted form without the transmembrane domain and the intracellular tail. Furthermore, by immunoprecipitation we demonstrate that LeechCAM is glycosylated with the Laz2-369 glycoepitope, an epitope that has been specifically implicated in regulation of axonal outgrowth and synapse formation.
Jie
C
C
Department of Zoology and Genetics, 3156 Molecular Biology Building, Iowa State University, Ames, IA, USA.
Zipser
B
B
Jellies
J
J
Johansen
K M
KM
Johansen
J
J
D000818:Animals; D015815:Cell Adhesion Molecules / Q000737:chemistry / Q000378:metabolism*; D010450:Endopeptidases; D053222:Fas Ligand Protein; D006031:Glycosylation; D007865:Leeches / Q000196:embryology / Q000378:metabolism*; D008562:Membrane Glycoproteins / Q000378:metabolism; D009474:Neurons / Q000378:metabolism; D017830:Octoxynol; D010802:Phylogeny; D011092:Polyethylene Glycols; D011233:Precipitin Tests; D020033:Protein Isoforms / Q000378:metabolism
D015815:Cell Adhesion Molecules; D053222:Fas Ligand Protein; D008562:Membrane Glycoproteins; D020033:Protein Isoforms; D011092:Polyethylene Glycols; D017830:Octoxynol; C010615:Nonidet P-40; D010450:Endopeptidases