Claims
- 1. An isolated receptor protein reactive with advanced glycosylation end products, characterized as follows:
- (a) it has a molecular mass from 30 to 50 kD;
- (b) it is reactive with AGE-BSA, AGE-RNAse, AGE-collagen I and AGE-BSA reduced with NaBH.sub.4 and has a binding affinity of 2.0.+-.0.4.times.10.sup.-6 M.sup.-1 (kD=500 nM);
- (c) it is non-reactive with BSA, collagen I, RNAse or chemically synthesized FFI-BSA; and
- (d) it is present on mesangial cell membranes prior to purification.
- 2. A plurality of isolated receptor proteins reactive with advanced glycosylation endproducts, characterized as follows:
- (a) at least one of said proteins has a molecular mass from 30 to 50 kD;
- (b) the plurality of proteins is derived from mammalian mesangial cells;
- (c) the proteins are reactive with AGE-BSA, AGE-RNAse, AGE-collagen I and AGE-BSA reduced with NaBH.sub.4, having a binding affinity of 2.0.+-.0.4.times.10.sup.-6 M.sup.-1 (kD=500 nM);
- (d) the proteins are non-reactive with BSA, collagen I, RNAse or chemically synthesized FFI-BSA; and
- (e) the proteins are present on mesangial cell membranes prior to purification in an amount sufficient to bind about 3.0.+-.0.25.times.10.sup.5 AGE-modified protein molecules per mesangial cell.
- 3. The protein of claim 1 or the receptor proteins of claim 2 labeled with a detectable label.
- 4. An isolated receptor protein reactive with advanced glycosylation end products in accordance with claim 1 having a molecular mass of about 50 kD.
- 5. An isolated receptor protein reactive with advanced glycosylation end products in accordance with claim 1 having a molecular mass of about 40 kD.
- 6. An isolated receptor protein reactive with advanced glycosylation end products in accordance with claim 1 having a molecular mass of about30-35 kD.
CROSS-REFERENCE TO RELATED APPLICATIONS
The present Application is a continuation-in-part of application Ser. No. 453,958, filed Dec. 20, 1989, which is in turn, a Division of application Ser. No. 091,534, filed Sep. 3, 1987, now U.S. Pat. No. 4,900,747, issued Feb. 13, 1990, which is in turn, a continuation-in-part of application Ser. No. 907,747, filed Sep. 12, 1986, now abandoned; all of the above preceding applications by Helen Vlassara, Michael Brownlee and Anthony Cerami, said Ser. No. 907,747, in turn, a continuation-in-part of application Ser. No. 798,032, filed Nov. 14, 1985, by Anthony Cerami, Peter Ulrich and Michael Brownlee, now U.S. Pat. No. 4,758,583, which is, in turn, a continuation-in-part of application Ser. No. 590,820, now U.S. Pat. No. 4,665,192, filed Mar. 19, 1984 by Anthony Cerami alone.
Government Interests
This invention was made with partial assistance from grant Nos. AG 8245 and DK 19655 from the National Institutes of Health. The government may have certain rights in this invention.
Non-Patent Literature Citations (5)
Entry |
Skolnik, E. et al., J. Exp. Med 174:931/939 (Oct., 1991). |
Vlassara, H. et al., Science (Washington, D.C. 240:1546). |
Esposito, C. et al., J. Exp. Med 170:1387 (1989). |
Schlondorf, D. J. Fed. AM. Soc. Exp. Biol. 1:272 (1987). |
Lovett, D. H. et al., Kidney Int. 30/246 (1986). |
Divisions (1)
|
Number |
Date |
Country |
Parent |
91534 |
Sep 1987 |
|
Continuation in Parts (4)
|
Number |
Date |
Country |
Parent |
453958 |
Dec 1989 |
|
Parent |
907747 |
Sep 1986 |
|
Parent |
798032 |
Nov 1985 |
|
Parent |
590820 |
Mar 1984 |
|