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1988 ; 79
(1
): 82-90
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The molecular heterogeneity of nonspecific cross-reacting antigen synthesized by
tumor cells and granulocytes
#MMPMID3128509
Kuroki M
; Kuroki M
; Moore GE
; Ichiki S
; Matsuoka Y
Jpn J Cancer Res
1988[Jan]; 79
(1
): 82-90
PMID3128509
show ga
The molecular heterogeneity of nonspecific cross-reacting antigen (NCA) was
examined. Metabolically-labeled glycoproteins were precipitated from cell lysates
of human tumor cell lines and of normal peripheral granulocytes with antibodies
specific for NCA, and analyzed by SDS-PAGE. NCA components synthesized by three
tumor cell lines, QGP-1 (pancreas), HLC-1 (lung) and CAOV-2 (ovary) showed
slightly different migration patterns on SDS-PAGE, but the molecular weights of
their unglycosylated peptides synthesized in the presence of tunicamycin were all
found to be 35K. On the other hand, two molecular species of NCA were identified
in normal granulocytes: an 80K mature form derived from a 69K precursor peptide
and a 58K mature form from a 41K precursor peptide. Upon SDS-PAGE, the migration
pattern of the unglycosylated NCA peptides from tumor cells was affected by the
presence of 2-mercaptoethanol, while that of the peptides of granulocytes was
not. All the NCAs identified in this study possessed antigenic determinants
common to carcinoembryonic antigen as well as those unique to NCA. These results
suggest that the molecular heterogeneity of NCA observed thus far resulted from
diverse glycosylation of the three fundamental molecular forms of unglycosylated
peptides: one with a molecular weight of 35K produced by tumor cells and two with
molecular weights of 69K and 41K produced by granulocytes.