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Glycopeptide of P0 protein inhibits homophilic cell adhesion Competition assay with transformants and peptides
Author(s) -
Yazaki Takahito,
Miura Masayuki,
Asou Hiroaki,
Kitamura Kunio,
Toya Shigeo,
Uyemura Keiichi
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80713-q
Subject(s) - glycopeptide , chemistry , peptide , cell adhesion , transfection , adhesion , cell , microbiology and biotechnology , glycoprotein , biochemistry , biology , organic chemistry , gene , antibiotics
Expression of major myelin glycoprotein P0 by PO cDNA transfection into C6 glioma cells promoted homophilic cell adhesion of the cells. After the dissociated cells were incubated for various times, the number of particles at each time point was measured. The total number of particles decreased to 24% in 60 min for transformant (C6P0) cells, in contrast to only 68% for control (C6P0′) cells. To confirm the homophilic mechanism of adhesion, mixed‐cell aggregation experiments were performed. Among the four synthetic peptides corresponding to a part of the P0 sequence used, only peptide 3 (residues 90–96), which contained a carbohydrate attaching site, caused considerable inhibition of cell aggregation (approximately 50%). In addition, the glycopeptide (residues 91–95) obtained from bovine P0 markedly inhibited cell aggregation (by approximately 85%).