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THBS2  -  thrombospondin 2

Bos taurus

Synonyms: TMEM200A, TSP-2
 
 
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Disease relevance of THBS2

  • No significant differences in TSP1 and TSP2 expressions were found between control adrenals and nonfunctional adenomas [1].
 

High impact information on THBS2

 

Biological context of THBS2

  • We report here the nucleotide sequence of a 386 bp RT-PCR fragment specific for CISP [3].
  • This protein was recently purified in our laboratory, and its N-terminal amino-acid sequence revealed a significant similarity with thrombospondin-2 (TSP2) [3].
  • Using glycosylation inhibitors, we could determine that CISP is synthesized as a 175-kDa core protein, is then matured into a 190-kDa high-mannose form and secreted as a 195-kDa mature protein [2].
  • Recombinant mouse TSP2 inhibited BAE cell proliferation in response to LPA in a dose range similar to that of TSP1 [4].
  • The overall distribution of TSP2 in the glomerulosa and fasciculata zones of the adrenal cortex, and its absence from the reticularis zone, argue in favor of a role in the protection of adrenocortical cells against apoptosis [5].
 

Anatomical context of THBS2

 

Associations of THBS2 with chemical compounds

 

Analytical, diagnostic and therapeutic context of THBS2

  • We report here the purification of CISP to apparent homogeneity with an overall yield of 43% using a combination of heparin-agarose and Mono-Q chromatographies [7].
  • The protein levels of TSP1 and CISP/TSP2 varied accordingly with their respective mRNA levels, as shown by immunoprecipitation and immunofluorescence experiments [3].
  • The trimeric structure of CISP could be observed by rotary shadowing/electron microscopy, where CISP appeared to be composed of three equally electron-dense nodules and of a fourth nodule formed by the close association of three smaller fragments [2].

References

  1. Thrombospondin expression in aldosterone-producing adenomas. Hatakeyama, H., Nishizawa, M., Nakagawa, A., Nakano, S., Kigoshi, T., Miyamori, I., Uchida, K. Hypertens. Res. (2002) [Pubmed]
  2. The molecular structure of corticotropin-induced secreted protein, a novel member of the thrombospondin family. Pellerin, S., Lafeuillade, B., Wade, R.H., Savona, C., Chambaz, E.M., Feige, J.J. J. Biol. Chem. (1993) [Pubmed]
  3. Opposite regulation of thrombospondin-1 and corticotropin-induced secreted protein/thrombospondin-2 expression by adrenocorticotropic hormone in adrenocortical cells. Lafeuillade, B., Pellerin, S., Keramidas, M., Danik, M., Chambaz, E.M., Feige, J.J. J. Cell. Physiol. (1996) [Pubmed]
  4. Endothelial cell mitogenesis induced by LPA: inhibition by thrombospondin-1 and thrombospondin-2. Panetti, T.S., Chen, H., Misenheimer, T.M., Getzler, S.B., Mosher, D.F. J. Lab. Clin. Med. (1997) [Pubmed]
  5. Hormonally regulated components of the adrenocortical cell environment and the control of adrenal cortex homeostasis. Feige, J.J., Keramidas, M., Chambaz, E.M. Horm. Metab. Res. (1998) [Pubmed]
  6. Bovine thrombospondin-2: complete complementary deoxyribonucleic acid sequence and immunolocalization in the external zones of the adrenal cortex. Danik, M., Chinn, A.M., Lafeuillade, B., Keramidas, M., Aguesse-Germon, S., Penhoat, A., Chen, H., Mosher, D.F., Chambaz, E.M., Feige, J.J. Endocrinology (1999) [Pubmed]
  7. Corticotropin-induced secreted protein, an ACTH-induced protein secreted by adrenocortical cells, is structurally related to thrombospondins. Pellerin, S., Lafeuillade, B., Scherrer, N., Gagnon, J., Shi, D.L., Chambaz, E.M., Feige, J.J. J. Biol. Chem. (1993) [Pubmed]
 
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