Search by BoMiProt ID - Bomi15


Primary Information

BoMiProt ID Bomi15
Protein Name Protein S100-A8
Organism Bos taurus
Uniprot IdP28782
Milk FractionWhey
Ref Sequence Id NP_001107197.1
Amino Acid Lenth 89
Molecular Weight 10460
Fasta Sequence https://www.uniprot.org/uniprot/P28782.fasta
Gene Name S100A8
Gene Id 616818
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondry Information

Presence in other biological fluids/tissue/cells S100A8 and S100A9 are small calcium-binding proteins that are highly expressed in neutrophil and monocyte cytosol, endothelial and epithelial cells; uterus, cervix
Protein Function s100 A8 and A9 are found at high levels in the extracellular milieu during inflammatory conditions; Extracellular S100A8, S100A9, and S100A8/A9 mediate regulatory and biological functions, including antiproliferative, antitumoral, antimicrobial, and antinociceptive activities and induce neutrophil adhesion to fibrinogen in vitro; vital role in regulating the interactions between the mammalian foetus and the uterus; important in regulating reproductive functions; showed specific patterns during the different stages of pregnancy; exert strong proinflammatory and chemotactic activities by promoting leukocyte recruitment; In murine macrophages, S100A8, but not S100A9, is induced by TLR agonists in an interleukin (IL)-10-dependent manner; some agonists require cAMP and/or PGE2 generation for full expression; In murine keratinocytes, S100A8 is induced by oxidative stress whereas S100A9 is not, confirming; S100A9 is a p38 MAPK target phosphorylated after phagocyte activation; S100A9 reduces microtubule polymerization and F-actin cross-linking by the S100A8/S100A9 complex; S100A8 and S100A9 form a heterocomplex. S100A8/S100A9 inhibits casein kinase I and II suggesting a role in myeloid cell differentiation
Biochemical Properties S100A8 and S100A9 form noncovalent homodimers and a heterodimer (S100A8/A9) in a calcium-dependent manner; low molecular weight S100 proteins; EF-hand Ca2+-binding proteins; form homodimers as well as heterodimers; heterodimers assemble in a Ca2+ and Zn2+-dependent manner into heterotetrameric and larger complexes; ability to self-assemble into highly heterogeneous amyloid complexes, encompassing both oligomeric species and highly stable fibrils able to grow and accumulate in the ageing prostate; the function and biochemical properties of s100 A8 and A9 are mostly simily and both of them work forming heterocomplex
Significance in milk involved in the innate immune defense against pathogens;
Linking IDs Bomi2720
Bibliography 1. Ryckman, C., Vandal, K., Rouleau, P., Talbot, M., & Tessier, P. A. (2003). Proinflammatory activities of S100: proteins S100A8, S100A9, and S100A8/A9 induce neutrophil chemotaxis and adhesion. Journal of Immunology (Baltimore, Md. : 1950), 170(6), 3233–3242. https://doi.org/10.4049/jimmunol.170.6.3233.
2. Addis, M. F., Pisanu, S., Marogna, G., Cubeddu, T., Pagnozzi, D., Cacciotto, C., … Uzzau, S. (2013). Production and release of antimicrobial and immune defense proteins by mammary epithelial cells following Streptococcus uberis infection of sheep. Infection and Immunity, 81(9), 3182–3197. https://doi.org/10.1128/IAI.00291-13.
3. Elgawish, R. A., Ogata, Y., Hidaka, T., Nii, T., Yoshimura, Y., & Isobe, N. (2018). Changes in plasma concentrations of S100A7 and S100A8 in dairy cows during pregnancy. Reproduction in Domestic Animals = Zuchthygiene, 53(4), 1013–1015. https://doi.org/10.1111/rda.13185