Abstract
The sera from three C8α-γ deficient patients previously reported to have a selective C8α-γ defect were analyzed by SDS-PAGE and Western blot using two polyclonal antisera to C8α-γ and a monoclonal antibody to C8α. All three sera exhibited C8α-γ bands that dissociated into α and γ chains under reducing conditions. Quantitation of the α-γ subunit in these sera by a sensitive ELISA revealed an amount ~1% of that found in normal human serum. A similar assay performed with a specific antiserum to C8β showed unexpectedly low levels of C8β in these sera, which were confirmed by hemolytic titration of C8β. The remarkable differences between C8α-γ and C8β in the C8α-γ deficient sera was that in spite of their comparable immunochemical levels, C8β still exhibited functional activity whereas C8α-γ was totally inactive. That the residual C8α-γ was inactive was also proved by its inability to show lytic bands in an overlay system after SDS-PAGE and subsequent removal of SDS. The implications of these findings for a novel concept of C8 deficiency are discussed.
| Original language | English |
|---|---|
| Pages (from-to) | 884-888 |
| Number of pages | 5 |
| Journal | Journal of Clinical Investigation |
| Volume | 86 |
| Issue number | 3 |
| Publication status | Published - 1990 |
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Keywords
- C8
- C8 subunits
- combined deficiency
- complement
- inherited defect
ASJC Scopus subject areas
- Medicine(all)
Cite this
Two distinct abnormalities in patients with C8α-γ deficiency. Low level of C8β chain and presence of dysfunctional C8α-γ subunit. / Tedesco, F.; Roncelli, L.; Petersen, B. H.; Agnello, V.; Sodetz, J. M.
In: Journal of Clinical Investigation, Vol. 86, No. 3, 1990, p. 884-888.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Two distinct abnormalities in patients with C8α-γ deficiency. Low level of C8β chain and presence of dysfunctional C8α-γ subunit
AU - Tedesco, F.
AU - Roncelli, L.
AU - Petersen, B. H.
AU - Agnello, V.
AU - Sodetz, J. M.
PY - 1990
Y1 - 1990
N2 - The sera from three C8α-γ deficient patients previously reported to have a selective C8α-γ defect were analyzed by SDS-PAGE and Western blot using two polyclonal antisera to C8α-γ and a monoclonal antibody to C8α. All three sera exhibited C8α-γ bands that dissociated into α and γ chains under reducing conditions. Quantitation of the α-γ subunit in these sera by a sensitive ELISA revealed an amount ~1% of that found in normal human serum. A similar assay performed with a specific antiserum to C8β showed unexpectedly low levels of C8β in these sera, which were confirmed by hemolytic titration of C8β. The remarkable differences between C8α-γ and C8β in the C8α-γ deficient sera was that in spite of their comparable immunochemical levels, C8β still exhibited functional activity whereas C8α-γ was totally inactive. That the residual C8α-γ was inactive was also proved by its inability to show lytic bands in an overlay system after SDS-PAGE and subsequent removal of SDS. The implications of these findings for a novel concept of C8 deficiency are discussed.
AB - The sera from three C8α-γ deficient patients previously reported to have a selective C8α-γ defect were analyzed by SDS-PAGE and Western blot using two polyclonal antisera to C8α-γ and a monoclonal antibody to C8α. All three sera exhibited C8α-γ bands that dissociated into α and γ chains under reducing conditions. Quantitation of the α-γ subunit in these sera by a sensitive ELISA revealed an amount ~1% of that found in normal human serum. A similar assay performed with a specific antiserum to C8β showed unexpectedly low levels of C8β in these sera, which were confirmed by hemolytic titration of C8β. The remarkable differences between C8α-γ and C8β in the C8α-γ deficient sera was that in spite of their comparable immunochemical levels, C8β still exhibited functional activity whereas C8α-γ was totally inactive. That the residual C8α-γ was inactive was also proved by its inability to show lytic bands in an overlay system after SDS-PAGE and subsequent removal of SDS. The implications of these findings for a novel concept of C8 deficiency are discussed.
KW - C8
KW - C8 subunits
KW - combined deficiency
KW - complement
KW - inherited defect
UR - http://www.scopus.com/inward/record.url?scp=0025184271&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0025184271&partnerID=8YFLogxK
M3 - Article
C2 - 2394837
AN - SCOPUS:0025184271
VL - 86
SP - 884
EP - 888
JO - Journal of Clinical Investigation
JF - Journal of Clinical Investigation
SN - 0021-9738
IS - 3
ER -