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Spon2  -  spondin 2, extracellular matrix protein

Mus musculus

Synonyms: 2310045I24Rik, AI504350, M-spondin, Mindin, Mspondin, ...
 
 
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Disease relevance of Spon2

 

High impact information on Spon2

  • Moreover, mindin binds directly to bacteria and their components and functions as an opsonin for macrophage phagocytosis of bacteria [3].
  • Mindin(-/-) mice displayed defective CD4(+) T-cell priming and impaired humoral immune responses to T-dependent antigens [4].
  • DCs lacking beta(1) integrin had reduced adhesion to mindin matrix, decreased expression of Rac1/2 and impaired priming capacity [4].
  • The adhesion of neutrophils to mindin is blocked by anti-integrin alpha4, anti-integrin alpha(M), and anti-integrin beta2 antibodies [5].
  • Mindin/RG-1 protein expression is maintained in >80% of prostate cancers metastatic to bone or lymph nodes as well as in locally recurrent tumors in androgen-unresponsive patients [1].
 

Anatomical context of Spon2

  • In response to LPS at low concentrations, or to 5,6-MeXAA at all concentrations, tumouricidal activity from macrophages from Spon-2-bearing C3H/HeJ mice was severely depressed compared with activity from their C3H/HeN counterparts [2].
  • Macrophages from Spon-2 tumour bearing mice behaved like "primed" thioglycollate-elicited macrophages and produced a tumouricidal response to 5,6-MeXXA which was significantly higher than that obtained from resident peritoneal macrophages from non-tumour bearing mice [2].
 

Associations of Spon2 with chemical compounds

  • Similarly in C3H/HeN mice, cortisone pre-treatment prevented FAA-induced necrosis of Spon-2 and partially prevented necrosis induction in mammary M-16/C tumours [6].
 

Analytical, diagnostic and therapeutic context of Spon2

  • A fully human antibody, 19G9, was generated against mindin/RG-1 protein and was shown to accumulate at high abundance in LNCaP tumor xenografts [1].

References

  1. Identification of a novel prostate tumor target, mindin/RG-1, for antibody-based radiotherapy of prostate cancer. Parry, R., Schneider, D., Hudson, D., Parkes, D., Xuan, J.A., Newton, A., Toy, P., Lin, R., Harkins, R., Alicke, B., Biroc, S., Kretschmer, P.J., Halks-Miller, M., Klocker, H., Zhu, Y., Larsen, B., Cobb, R.R., Bringmann, P., Roth, G., Lewis, J.S., Dinter, H., Parry, G. Cancer Res. (2005) [Pubmed]
  2. Effect of tumour growth on the macrophage response to the antitumour agent 5,6-dimethylxanthenone-4-acetic acid. Ching, L.M., Joseph, W.R., Baguley, B.C. Anticancer Res. (1993) [Pubmed]
  3. The extracellular matrix protein mindin is a pattern-recognition molecule for microbial pathogens. He, Y.W., Li, H., Zhang, J., Hsu, C.L., Lin, E., Zhang, N., Guo, J., Forbush, K.A., Bevan, M.J. Nat. Immunol. (2004) [Pubmed]
  4. Efficient dendritic cell priming of T lymphocytes depends on the extracellular matrix protein mindin. Li, H., Oliver, T., Jia, W., He, Y.W. EMBO J. (2006) [Pubmed]
  5. The extracellular matrix protein mindin serves as an integrin ligand and is critical for inflammatory cell recruitment. Jia, W., Li, H., He, Y.W. Blood (2005) [Pubmed]
  6. Inhibition of antitumor effects of flavone acetic acid by cortisone. Ching, L.M., Joseph, W.R., Baguley, B.C. Anticancer Res. (1993) [Pubmed]
 
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