Loading…
Identification of the rat Heymann nephritis autoantigen (GP330) as a receptor site for plasminogen
Previous results have demonstrated the binding of a 76- and 80-kDa serum protein to the Heymann nephritis autoantigen, gp330. This 76-kDa serum protein was purified by column chromatography and preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis. A rabbit polyclonal antibody for th...
Saved in:
Published in: | The Journal of biological chemistry 1991-06, Vol.266 (17), p.10825-10829 |
---|---|
Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Summary: | Previous results have demonstrated the binding of a 76- and 80-kDa serum protein to the Heymann nephritis autoantigen, gp330.
This 76-kDa serum protein was purified by column chromatography and preparative sodium dodecyl sulfate-polyacrylamide gel
electrophoresis. A rabbit polyclonal antibody for the serum protein was produced and used to screen a rat liver cDNA expression
library. Sequence analysis of an isolated clone identified the serum protein as plasminogen. Plasminogen was isolated from
rat serum by standard techniques, and the binding of plasminogen to gp330 was confirmed by Western analysis. Enzyme-linked
immunosorbent assay results demonstrated a time-dependent, saturable, and specifically inhibitable binding of plasminogen
to gp330. There was no significant difference in the binding of the two carbohydrate forms of plasminogen to gp330. Plasminogen
binding to gp330 could be completely inhibited by the addition of exogenous gp330. This binding could also be partially inhibited
by benzamidine but only slightly by the lysine analogue, epsilon-aminocaproic acid. However, even a combination of these two
inhibitors could not completely block the binding of plasminogen to gp330 indicating that gp330 may be binding to plasminogen
through some other unknown interactions. These results demonstrate that gp330 is a receptor site for plasminogen. |
---|---|
ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/s0021-9258(18)99093-9 |