Note. The novel sequence data published here have been submitted to the GenBank and are available under the accession number U75686.
Identification and Structure of Activated-Platelet Protein-1, a Protein with RNA-Binding Domain Motifs that is Expressed by Activated Platelets
Article first published online: 16 JUL 2004
European Journal of Biochemistry
Volume 243, Issue 1-2, pages 209–218, January 1997
How to Cite
Houng, A. K., Maggini, L., Clement, C. Y. and Reed, G. L. (1997), Identification and Structure of Activated-Platelet Protein-1, a Protein with RNA-Binding Domain Motifs that is Expressed by Activated Platelets. European Journal of Biochemistry, 243: 209–218. doi: 10.1111/j.1432-1033.1997.0209a.x
- Issue published online: 16 JUL 2004
- Article first published online: 16 JUL 2004
- (Received 24 July/23 October 1996) – EJB 96 1110/1
Beyond their critical role in thrombosis, platelets perform important functions in vascular remodeling, inflammation, and wound repair. Many of these functions are executed by molecules expressed by activated platelets. A novel molecule, activated-platelet protein-1 (APP-1), was identified by a monoclonal antibody against activated rabbit platelets. When platelets were stimulated by thrombin, A23187 or ADP, APP-I was expressed on the platelet surface. APP-1 was also detected in whole cell lysates of platelets, but not on the external surfaces of resting platelets. With maximal activation by thrombin, 15900±2800 molecules APP-1 were expressed/platelet. A 2.3-kb cDNA fragment containing a partial coding sequence for APP-1 was isolated from a rabbit bone marrow library by expression cloning with the anti-APP-l monoclonal antibody. When expressed as a recombinant fusion protein in bacteria, APP-1 bound specifically to poly(A)-Sepharose. The full-length cDNA coding for human APP-1, obtained by DNA hybridization techniques, showed 98.7% amino acid sequence identity with the rabbit protein. Northern analysis with human APP-1 identified a 3.7-kb mRNA transcript in megakaryocytic lines that express transcripts for platelet proteins. Human APP-1 has four ribonucleotide binding domains with ribonucleoprotein 1 and 2 motifs. By virtue of its ribonucleotide binding domains, APP-1 is structurally related to polyadenylate-binding protein, which regulates translation initiation and polyadenylate shortening, and to nucleolysin, a specific effector molecule found in the granules of cytotoxic T lymphocytes.
polyadenylate binding protein
- 1Gordon, J. L. (ed.) (1976) Platelets in biology and pathology, pp. 1–378, North Holland Publishing, New York .
- 81994) Platelet secretion and energy metabolism, in Hemostasis and thrombosis: basic principles and clinical practice, 3rd edn (Colman, R. W., Hirsch, J., Marder, V. J. & Salzman, E. W., eds) pp. 525–545, Lippincott, Philadelphia .(
- 261989) Moleculur cloring, a laboratory manual, 2nd edn, Cold Spring Harbor Laboratory Press, Cold Spring Harbor NY ., & (
- 521992) Nuclear magnetic resonance studies of amine and nucleotide storage mechanisms in platelet dense granules. in Tlie plutelet urnirze storage grutzule (Meyers, K. M. & Barnes, C. D., eds), pp. 51–71, CRC Press, Ann Arbor MI .& (