Identification and immunological characterization of a novel 40-kDa protein linked to CD98 antigen

Citation
Y. Matsumoto et al., Identification and immunological characterization of a novel 40-kDa protein linked to CD98 antigen, CELL STRUCT, 24(4), 1999, pp. 217-226
Citations number
29
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Cell & Developmental Biology
Journal title
CELL STRUCTURE AND FUNCTION
ISSN journal
0386-7196 → ACNP
Volume
24
Issue
4
Year of publication
1999
Pages
217 - 226
Database
ISI
SICI code
0386-7196(199908)24:4<217:IAICOA>2.0.ZU;2-1
Abstract
Monoclonal antibodies (mAbs) were obtained from hybridoma clones establishe d by cell fusion between mouse myeloma cells and spleen cells from a mouse immunized against an affinity-purified 40kDa component of rat 125-kDa glyco protein (GP125). Two mAbs designated as 3F2 and 6B4 detected a 40-kDa and a 125-kDa band under reducing and nonreducing conditions, respectively, in e xtracts prepared from rat, mouse and human tumor cells. Association of the 40-kDa protein with CD98 was revealed by sandwich-type enzyme-linked immuno sorbent assay. The two mAbs were strongly reactive with various tumor cells and activated lymphocytes, but were only weakly reactive with resting lymp hocytes. Confocal microscopy indicated colocalization of CD98 and the 40-kD a protein defined with 3F2 and 6B4 at the cell surface and perinuclear regi ons. On immunohistochemical analysis of frozen sections of rat tongue, the anti-rat CD98 mAb B3 selectively stained the basal layer and 3F2 stained th e upper epithelial part in addition to the basal layer, indicating the exis tence of CD98-unlinked 40-kDa protein.