TY - JOUR
T1 - Differential glycosylation and proteolytical processing of LeechCAM in central and peripheral leech neurons
AU - Jie, Chunfa
AU - Zipser, Birgit
AU - Jellies, John
AU - Johansen, Kristen M.
AU - Johansen, Jørgen
N1 - Funding Information:
We wish to thank Anna Yeung for expert technical assistance as well as Dr. Paul Kapke at the Iowa State University Hybridoma Facility for help with maintaining the monoclonal antibody lines. This work was supported by NIH Grant NS 28857 (J.Jo.) and by NSF grant 9724064 (J.Je.).
PY - 1999/11/11
Y1 - 1999/11/11
N2 - 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.
AB - 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.
KW - (Leech)
KW - Differential glycosylation
KW - LeechCAM
KW - Neuron
KW - Proteolytic processing
UR - http://www.scopus.com/inward/record.url?scp=0032751438&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032751438&partnerID=8YFLogxK
U2 - 10.1016/S0167-4889(99)00118-4
DO - 10.1016/S0167-4889(99)00118-4
M3 - Article
C2 - 10559469
AN - SCOPUS:0032751438
SN - 0167-4889
VL - 1452
SP - 161
EP - 171
JO - Biochimica et Biophysica Acta - Molecular Cell Research
JF - Biochimica et Biophysica Acta - Molecular Cell Research
IS - 2
ER -