TY - JOUR
T1 - Effects of Anti-Thrombospondin Monoclonal Antibodies on the Agglutination of Erythrocytes and Fixed, Activated Platelets by Purified Thrombospondin
AU - Dixit, Vishva M.
AU - Haverstick, Doris M.
AU - O'Rourke, Karen M.
AU - Hennessy, Sally W.
AU - Grant, Gregory A.
AU - Santoro, Samuel A.
AU - Frazier, William A.
PY - 1985/7/1
Y1 - 1985/7/1
N2 - A monoclonal antibody (Mab) has been raised against native thrombospondin (TSP), the endogenous lectin of human platelets, that inhibits the hemagglutination of trypsinized, glutaraldehyde-fixed human erythrocytes by purified TSP. This Mab, designated A2.5, also inhibits the agglutination of fixed, activated platelets by TSP. Mab A2.5 immunoprecipitates a 25-kilodalton (kDa) peptide from chymotryptic digests of TSP that is not disulfide bonded to any other region of the TSP molecule. This fragment represents the previously characterized heparin binding domain of TSP [Dixit, V. M., Grant, G. A., Santoro, S. A., & Frazier, W. A. (1984) J. Biol. Chem. 259, 10100-10105]. In agreement with this assignment, heparin inhibits the binding of Mab A2.5 to TSP. Another Mab, designated C6.7, also blocks TSP-mediated hemagglutination, yet has no effect on the agglutination of fixed, activated platelets by TSP. This Mab has been shown to inhibit the thrombin-stimulated aggregation of live platelets and to immunoprecipitate an 18-kDa fragment from chymotryptic digests, which is distinct from the heparin binding domain [Dixit, V. M., Haverstick, D. M., O'Rourke, K. M., Hennessy, S. W., Grant, G. A., Santoro, S. A., & Frazier, W. A. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 3472-3476].
AB - A monoclonal antibody (Mab) has been raised against native thrombospondin (TSP), the endogenous lectin of human platelets, that inhibits the hemagglutination of trypsinized, glutaraldehyde-fixed human erythrocytes by purified TSP. This Mab, designated A2.5, also inhibits the agglutination of fixed, activated platelets by TSP. Mab A2.5 immunoprecipitates a 25-kilodalton (kDa) peptide from chymotryptic digests of TSP that is not disulfide bonded to any other region of the TSP molecule. This fragment represents the previously characterized heparin binding domain of TSP [Dixit, V. M., Grant, G. A., Santoro, S. A., & Frazier, W. A. (1984) J. Biol. Chem. 259, 10100-10105]. In agreement with this assignment, heparin inhibits the binding of Mab A2.5 to TSP. Another Mab, designated C6.7, also blocks TSP-mediated hemagglutination, yet has no effect on the agglutination of fixed, activated platelets by TSP. This Mab has been shown to inhibit the thrombin-stimulated aggregation of live platelets and to immunoprecipitate an 18-kDa fragment from chymotryptic digests, which is distinct from the heparin binding domain [Dixit, V. M., Haverstick, D. M., O'Rourke, K. M., Hennessy, S. W., Grant, G. A., Santoro, S. A., & Frazier, W. A. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 3472-3476].
UR - http://www.scopus.com/inward/record.url?scp=0022415767&partnerID=8YFLogxK
U2 - 10.1021/bi00337a003
DO - 10.1021/bi00337a003
M3 - Article
C2 - 4052397
AN - SCOPUS:0022415767
VL - 24
SP - 4270
EP - 4275
JO - Biochemistry
JF - Biochemistry
SN - 0006-2960
IS - 16
ER -