Secreted Phosphoprotein 2 Proteins (SPP2)

Mouse (Murine) Secreted Phosphoprotein 2 (SPP2) interaction partners

1. proteolytic processing of spp24 affects the interaction of this protein with BMP-2 and this affects the function of the protein

Human Secreted Phosphoprotein 2 (SPP2) interaction partners

1. Spp24 can inhibit the growth of prostate cancer and its bone metastasis induced by BMP2; spp24 may have great potential to be a therapeutic agent in clinical situations

2. the two mutations of SPP2 have dominant negative effects and cellular accumulation of Spp-24 might be particularly toxic to photoreceptors and/or retinal pigment epithelium. SPP2 has a new role in retinal degeneration.

3. Report describes a C-terminal fragment within SPP24 that is distinct from the cystatin domain and which independently binds to BMP-2 and TGF-beta. This fragment inhibited BMP-2 activity in an ectopic bone forming assay.

4. Spp24, or proteolytic products of Spp24, bind cytokines of the TGF-beta superfamily and also activate intracellular signaling pathways [review]

5. Spp24 truncation products have effects on osteoblastic differentiation mediated by kinase pathways that are independent of exogenous BMP/TGF-beta cytokines.

6. Results describe the localization of the human secreted phosphoprotein 24 gene, its structure and the start of transcription in liver.

7. spp24 contains at least 2 single nucleotide polymorphisms. Given its mechanism of action and sequence variability, SPP24 may be an interesting candidate for future studies of the genetic regulation of bone mass.

Cow (Bovine) Secreted Phosphoprotein 2 (SPP2) interaction partners

1. We report here for the first time the direct isolation of Spp24 covalently bound to alpha2-macroglobulins as a core complex (Spp24-alpha2M) from bovine calf serum.

2. The beta-pleated sheets of recombinant spp24 play a greater role in bone morphogenetic protein (BMP)-2 binding than does the alpha-helical turn.

3. levels of spp24 in bone may be regulated, in part, by calcium-dependent proteolysis mediated by osteoblastic cells