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Gene Review

SYCP2  -  synaptonemal complex protein 2

Homo sapiens

Synonyms: SCP-2, SCP2, Synaptonemal complex lateral element protein, Synaptonemal complex protein 2, hsSCP2
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Disease relevance of SYCP2


High impact information on SYCP2

  • The patients with gallstones also had significantly increased cytosolic total and free cholesterol levels (P < 0.001), which correlated strongly with increased cytosolic levels of SCP2/nsLTP (r = 0.80, P < 0.001 and r = 0.81, P < 0.001, respectively) [6].
  • The expressed cDNA in COS-7 cells yields a 15.3-kDa polypeptide and increased amounts of a 13.2-kDa polypeptide, both reacting with a specific rabbit antiserum to rat liver SCP2 [7].
  • The 1.3-kilobase (kb) cDNA contains an open reading frame which encompasses a 143-amino acid sequence which is 89% identical to the rat SCP2 amino acid sequence [7].
  • Southern blot analysis suggests either that there are multiple copies of the SCP2 gene in the human genome or that the SCP2 gene is very large [7].
  • Coexpression of the SCP2 cDNA with expression vectors for cholesterol side-chain cleavage enzyme and adrenodoxin resulted in a 2.5-fold enhancement of progestin synthesis over that obtained with expression of the steroidogenic enzyme system alone [7].

Biological context of SYCP2


Anatomical context of SYCP2

  • These results suggest that in normal fibroblasts the major fraction of newly synthesized cholesterol is transported to the plasma membrane by a SCP-2-dependent mechanism [3].
  • In contrast, sterol carrier protein-2 (SCP-2) was only 2.2-fold more effective in mediating sterol transfer from steroidogenic cell mitochondria [12].
  • After SCP-2 antisense oligonucleotides treatment of normal fibroblasts, the rapid transport was reduced by 81% with a simultaneous increase of the slower one [3].
  • The effect of sterol carrier protein-2 (SCP-2) on dolichol biosynthesis by rat liver microsomes was investigated. cis-Prenyltransferase activity was stimulated 7-fold in the presence of 5 micrograms of purified SCP-2/mg of microsomal protein, which was similar to the increase obtained by adding detergent [13].
  • Incubation with cytosol pretreated with anti-SCP-2 showed no stimulatory effect and led to the accumulation of shorter polyisoprenoids [13].

Associations of SYCP2 with chemical compounds

  • Cholesterol transfer was rapid, cytoskeleton-independent, and Golgi-independent in normal cells, but it was slower, cytoskeleton-dependent, and Golgi-dependent in SCP-2-deficient cells [3].
  • Interestingly, the orientation of the fatty acid is opposite to the observed orientation for Triton X-100 in the SCP-2-like domain from the peroxisomal multifunctional enzyme (Haapalainen, A. M., van Aalten, D. M., Merilainen, G., Jalonen, J. E., Pirila, P., Wierenga, R. K., Hiltunen, J. K., and Glumoff, T. (2001) J. Mol. Biol. 313, 1127-1138) [2].
  • The clones were equally sensitive to tert-butyl hydroperoxide, suggesting that the 7alpha-OOH effect was SCP-2-specific [1].
  • We report here the three-dimensional structure of the complex of SCP-2 from Aedes aegypti with a C16 fatty acid to 1.35-A resolution [2].
  • SCP-2 had no appreciable effect on polyprenol alpha-saturase, dolichol kinase, dolichyl phosphate phosphatase, or acyl-CoA:dolichol acyltransferase [13].

Analytical, diagnostic and therapeutic context of SYCP2

  • Circular dichroism also showed that these chemical-shift changes, upon oleic acid binding, did not alter the secondary structure of SCP-2 [10].
  • Differential polarized phase fluorometry revealed decreased SCP-2 tryptophan rotational correlation time upon cholesterol binding [14].
  • We used protein modelling and site-directed mutagenesis to investigate why the BODIPY-PC transfer mediated by E. lagascae SCP-2 is not sensitive to sterols, whereas the transfer mediated by A. thaliana SCP-2 shows sterol sensitivity [15].
  • In contrast, the level of sterol carrier protein 2 (SCP2), a Leydig cell-specific protein, was affected by hypophysectomy much less than the other parameters measured [16].
  • By immunoblotting, peroxisome-deficient cells were confirmed to contain either no detectable SCP2 or far less SCP2 than corresponding normal cells [17].


  1. Intracellular dissemination of peroxidative stress. Internalization, transport, and lethal targeting of a cholesterol hydroperoxide species by sterol carrier protein-2-overexpressing hepatoma cells. Kriska, T., Levchenko, V.V., Korytowski, W., Atshaves, B.P., Schroeder, F., Girotti, A.W. J. Biol. Chem. (2006) [Pubmed]
  2. The structural determination of an insect sterol carrier protein-2 with a ligand-bound C16 fatty acid at 1.35-A resolution. Dyer, D.H., Lovell, S., Thoden, J.B., Holden, H.M., Rayment, I., Lan, Q. J. Biol. Chem. (2003) [Pubmed]
  3. Sterol carrier protein-2 is involved in cholesterol transfer from the endoplasmic reticulum to the plasma membrane in human fibroblasts. Puglielli, L., Rigotti, A., Greco, A.V., Santos, M.J., Nervi, F. J. Biol. Chem. (1995) [Pubmed]
  4. Refsum's disease: a peroxisomal disorder affecting phytanic acid alpha-oxidation. Wierzbicki, A.S., Lloyd, M.D., Schofield, C.J., Feher, M.D., Gibberd, F.B. J. Neurochem. (2002) [Pubmed]
  5. Probing the ligand binding sites of fatty acid and sterol carrier proteins: effects of ethanol. Schroeder, F., Myers-Payne, S.C., Billheimer, J.T., Wood, W.G. Biochemistry (1995) [Pubmed]
  6. Hepatic cholesterol metabolism in patients with cholesterol gallstones: enhanced intracellular transport of cholesterol. Ito, T., Kawata, S., Imai, Y., Kakimoto, H., Trzaskos, J.M., Matsuzawa, Y. Gastroenterology (1996) [Pubmed]
  7. Cloning and expression of a cDNA encoding human sterol carrier protein 2. Yamamoto, R., Kallen, C.B., Babalola, G.O., Rennert, H., Billheimer, J.T., Strauss, J.F. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  8. Identification of differentially expressed genes in HPV-positive and HPV-negative oropharyngeal squamous cell carcinomas. Martinez, I., Wang, J., Hobson, K.F., Ferris, R.L., Khan, S.A. Eur. J. Cancer (2007) [Pubmed]
  9. A meiotic chromosomal core consisting of cohesin complex proteins recruits DNA recombination proteins and promotes synapsis in the absence of an axial element in mammalian meiotic cells. Pelttari, J., Hoja, M.R., Yuan, L., Liu, J.G., Brundell, E., Moens, P., Santucci-Darmanin, S., Jessberger, R., Barbero, J.L., Heyting, C., Höög, C. Mol. Cell. Biol. (2001) [Pubmed]
  10. Sterol carrier protein-2: structure reveals function. Stolowich, N.J., Petrescu, A.D., Huang, H., Martin, G.G., Scott, A.I., Schroeder, F. Cell. Mol. Life Sci. (2002) [Pubmed]
  11. Fusion and fission, the evolution of sterol carrier protein-2. Edqvist, J., Blomqvist, K. J. Mol. Evol. (2006) [Pubmed]
  12. Steroidogenic acute regulatory protein binds cholesterol and modulates mitochondrial membrane sterol domain dynamics. Petrescu, A.D., Gallegos, A.M., Okamura, Y., Strauss, J.F., Schroeder, F. J. Biol. Chem. (2001) [Pubmed]
  13. Involvement of sterol carrier protein-2 in dolichol biosynthesis. Ericsson, J., Scallen, T.J., Chojnacki, T., Dallner, G. J. Biol. Chem. (1991) [Pubmed]
  14. Cholesterol interaction with recombinant human sterol carrier protein-2. Colles, S.M., Woodford, J.K., Moncecchi, D., Myers-Payne, S.C., McLean, L.R., Billheimer, J.T., Schroeder, F. Lipids (1995) [Pubmed]
  15. Characterization of SCP-2 from Euphorbia lagascae reveals that a single Leu/Met exchange enhances sterol transfer activity. Viitanen, L., Nylund, M., Eklund, D.M., Alm, C., Eriksson, A.K., Tuuf, J., Salminen, T.A., Mattjus, P., Edqvist, J. FEBS J. (2006) [Pubmed]
  16. Effects of hypophysectomy and human chorionic gonadotrophin on Leydig cell function in mature rats. Stocco, D.M., Teerds, K.J., van Noort, M., Rommerts, F.F. J. Endocrinol. (1990) [Pubmed]
  17. Lack of requirement for sterol carrier protein-2 in the intracellular trafficking of lysosomal cholesterol. Johnson, W.J., Reinhart, M.P. J. Lipid Res. (1994) [Pubmed]
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