Search by BoMiProt ID - Bomi12


Primary Information

BoMiProt ID Bomi12
Protein Name Transforming growth factor beta-2
Organism Bos taurus
Uniprot IdP21214
Milk FractionWhey
Ref Sequence Id NP_001106723.1
Amino Acid Lenth 414
Molecular Weight 47692
Fasta Sequence https://www.uniprot.org/uniprot/P21214.fasta
Gene Name TGFB2
Gene Id 534069
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondry Information

Protein Function maintenance of metabolic homeostasis in the bone tissue; leading role in the fracture healing process; induces chondrogenesis and osteogenesis; potent inhibitor of intestinal epithelial cell proliferation
Biochemical Properties A dimer; a compact, globular conformation; single interchain disulfide bridge, suggesting that hydrophobic interactions between the two chains are of major importance in stabilizing the dimer; TßRIII shows affinity to all three TGFß forms and the highest to TGFß2; low pH activates TGFß2; TGF-8 directly induces an H-chain class switch which results in the expression of secretory IgA in lipopolysaccharide-stimulated B-cell cultures
Significance in milk have inhibitory effects on [3H]thymidine uptake by concanavalin-A-stimulated thymocytes; found in milk MFG and has immunosuppressive effects; important roles in the regulation of growth and differentiation processes in the foetus, neonate and adult and leads us to speculate on the function of these molecules in milk; regulate growth and differentiation of the intestinal epithelia from the lumenal surface of the neonatal gut in the early days following birth
Additional Comments TGFß2 RNAand TGFß3 RNA levels are the highest on the 7th day of the fracture
Bibliography 1. Daopin, S., Piez, K. A., Ogawa, Y., & Davies, D. R. (1992). Crystal structure of transforming growth factor-beta 2: an unusual fold for the superfamily. Science (New York, N.Y.), 257(5068), 369–373. https://doi.org/10.1126/science.1631557.
2. Joyce, M. E., Roberts, A. B., Sporn, M. B., & Bolander, M. E. (1990). Transforming growth factor-beta and the initiation of chondrogenesis and osteogenesis in the rat femur. The Journal of Cell Biology, 110(6), 2195–2207. https://doi.org/10.1083/jcb.110.6.2195.
3. Cho, T.-J., Gerstenfeld, L. C., & Einhorn, T. A. (2002). Differential temporal expression of members of the transforming growth factor beta superfamily during murine fracture healing. Journal of Bone and Mineral Research : The Official Journal of the American Society for Bone and Mineral Research, 17(3), 513–520. https://doi.org/10.1359/jbmr.2002.17.3.513.
4. Cox, D. A., & Bürk, R. R. (1991). Isolation and characterisation of milk growth factor, a transforming-growth-factor-beta 2-related polypeptide, from bovine milk. European Journal of Biochemistry, 197(2), 353–358. https://doi.org/10.1111/j.1432-1033.1991.tb15918.x.
5. Javelaud, D., & Mauviel, A. (2004). Mammalian transforming growth factor-betas: Smad signaling and physio-pathological roles. The International Journal of Biochemistry & Cell Biology, 36(7), 1161–1165. https://doi.org/10.1016/S1357-2725(03)00255-3