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Gene Review

SLN  -  sarcolipin

Homo sapiens

Synonyms: MGC12301, MGC125854, MGC125855, Sarcolipin
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Disease relevance of SLN


Psychiatry related information on SLN

  • If SLN positive patients decline the standard recommendation of CAD or entry into clinical trials evaluating the significance of CAD then the BCN could help in decision making [6].

High impact information on SLN

  • These phenotypic changes were associated with up-regulation of sarco(endo)plasmic reticulum calcium ATPase (SERCA) 2a expression as well as decreased Na(+)/Ca(2+) exchanger, beta-myosin heavy chain, and sarcolipin (SLN) expression [1].
  • These homologous proteins differ at their N and C termini: the C-terminal Met-Leu-Leu in PLN is replaced by Arg-Ser-Tyr-Gln-Tyr in SLN [7].
  • Modeling showed that the SLN/SERCA1a complex closely resembles the PLN/SERCA1a complex, but with the luminal end of SLN extending to the loop connecting M1 and M2, where Tyr-29 and Tyr-31 interact with aromatic residues in SERCA1a [8].
  • The Ca(2+)-ATPase is implicated in thermogenesis in some types of muscle; this could involve processes of slippage and leak modulated by interaction between the Ca(2+)-ATPase and sarcolipin [9].
  • There was a major up-regulation of proteins interacting with calcium, namely S100 calcium-binding proteins and sarcolipin, a sarcoplasmic calcium regulator [10].

Chemical compound and disease context of SLN


Biological context of SLN

  • SLN and PLN genes resemble each other in having two small exons, with their entire coding sequences lying in exon 2 and a large intron separating the two segments [12].
  • Genomic DNA and cDNA encoding human sarcolipin (SLN) were isolated and characterized and the SLN gene was mapped to chromosome 11q22-q23 [12].
  • Sarcolipin (SLN), a 31 amino acid integral membrane protein, regulates SERCA1a and SERCA2a, two isoforms of the sarco(endo)plasmic Ca-ATPase, by lowering their apparent Ca(2+) affinity and thereby enabling muscle relaxation [13].
  • NF-SLN cDNA (SLN tagged N-terminally with a FLAG epitope) was introduced into rat soleus muscle in one hindlimb by plasmid injection and electrotransfer [14].
  • Even at a 50:1 molar ratio of SLN/ATPase, SLN had no significant effect on the rate of ATP hydrolysis by the ATPase or on the Ca(2+)-dependence of ATP hydrolysis [15].

Anatomical context of SLN


Associations of SLN with chemical compounds

  • Elevated Ca(2+) dissociates both PLN and NF-SLN from their complexes with both SERCA1a and SERCA2a, but NF-SLN induced resistance to Ca(2+) dissociation of the PLN.SERCA complex [17].
  • Analytical ultracentrifugation experiments revealed that SLN oligomerizes in the presence of the nonionic detergents octylpolyoxyethylene and octyl glucoside in a concentration-dependent manner [18].
  • 2D solution NMR experiments were performed on SLN solubilized in sodium dodecyl sulfate (SDS) micelles [19].
  • Systemic administration of L-696,418 significantly decreased loss of PG from cartilage and prevented the highly localized tissue degradation and the resultant changes in electromechanical behavior caused by intraarticular SLN injection [20].
  • Inoculation of SLN, but not SHN, attenuated the nerve damage caused by PDX and protected foot sensory amplitude, H-wave amplitude, and behavioral measures of proprioceptive function [21].

Regulatory relationships of SLN


Other interactions of SLN

  • PLN mutations had more dramatic effects on SERCA1a coimmunoprecipitation than SLN mutations, suggesting that PLN dominates in the primary interaction with SERCA1a [8].
  • Addition of the FLAG epitope to the highly conserved C terminus decreased the apparent affinity of SERCA1 for Ca2+ relative to native SLN and decreased Vmax significantly [16].
  • Here is reviewed the assessed or suggested regulatory role of a family of small plasma/SR associated membrane proteins including gamma-subunit, phospholemman, Mat 8, KCNE (type 1, 2 and 3), RAMP (type 1, 2 and 3), sarcolipin and phospholamban, mainly found in muscular and vascular tissues [23].
  • RESULTS: Relative expression levels of sarcolipin mRNA were significantly lower in MVD/AF (0.60 +/- 0.11) than in either MVD/NSR (1.28 +/- 0.17, P < 0.01) or controls (1.10 +/- 0.10, P < 0.05) [4].
  • To characterize the effects of intraarticular injection of recombinant human stromelysin (SLN) on the matrix composition and physical properties of cartilage from lapine stifle joints and the modulation of these effects by the systemic administration of an N-carboxyalkyl synthetic matrix metalloproteinase inhibitor, L-696,418 [20].

Analytical, diagnostic and therapeutic context of SLN

  • Immunofluorescence and immunoblotting of transfected cells by using anti-FLAG antibodies indicated that NF-SLN and PLN tagged at its N terminus with the FLAG epitope, even when overexpressed, were restricted to the ER [7].
  • Circular dichroism spectroscopy showed that SLN is a predominantly alpha-helical protein and that the secondary structure is highly resistant to SDS and thermal denaturation [18].
  • Western blotting showed expression and co-immunoprecipitation showed physical interaction between NF-SLN and SERCA2a [14].
  • Overexpression of SLN resulted in significant reductions in both twitch and tetanic peak force amplitude and maximal rates of contraction and relaxation and increased fatigability with repeated electrical stimulation [24].
  • Female 6-8-week-old New Zealand white rabbits received an intraarticular injection of 100 micrograms activated SLN in 1 stifle joint and buffer in the contralateral control knee; these animals were killed after 1 hour [20].


  1. Cardiac-specific elevations in thyroid hormone enhance contractility and prevent pressure overload-induced cardiac dysfunction. Trivieri, M.G., Oudit, G.Y., Sah, R., Kerfant, B.G., Sun, H., O Gramolini, A., Pan, Y., Wickenden, A.D., Croteau, W., Morreale de Escobar, G., Pekhletski, R., St Germain, D., Maclennan, D.H., Backx, P.H. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  2. Regulation of sarco(endo)plasmic reticulum Ca2+ adenosine triphosphatase by phospholamban and sarcolipin: implication for cardiac hypertrophy and failure. Asahi, M., Nakayama, H., Tada, M., Otsu, K. Trends Cardiovasc. Med. (2003) [Pubmed]
  3. Rapid, high-yield expression and purification of Ca2+-ATPase regulatory proteins for high-resolution structural studies. Douglas, J.L., Trieber, C.A., Afara, M., Young, H.S. Protein Expr. Purif. (2005) [Pubmed]
  4. Down-regulation of sarcolipin mRNA expression in chronic atrial fibrillation. Uemura, N., Ohkusa, T., Hamano, K., Nakagome, M., Hori, H., Shimizu, M., Matsuzaki, M., Mochizuki, S., Minamisawa, S., Ishikawa, Y. Eur. J. Clin. Invest. (2004) [Pubmed]
  5. Identification of superior markers for polymerase chain reaction detection of breast cancer metastases in sentinel lymph nodes. Min, C.J., Tafra, L., Verbanac, K.M. Cancer Res. (1998) [Pubmed]
  6. Evaluation of a breast cancer nomogram for prediction of non-sentinel lymph node positivity. Soni, N.K., Carmalt, H.L., Gillett, D.J., Spillane, A.J. European journal of surgical oncology : the journal of the European Society of Surgical Oncology and the British Association of Surgical Oncology. (2005) [Pubmed]
  7. Sarcolipin retention in the endoplasmic reticulum depends on its C-terminal RSYQY sequence and its interaction with sarco(endo)plasmic Ca(2+)-ATPases. Gramolini, A.O., Kislinger, T., Asahi, M., Li, W., Emili, A., MacLennan, D.H. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  8. Sarcolipin regulates sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) by binding to transmembrane helices alone or in association with phospholamban. Asahi, M., Sugita, Y., Kurzydlowski, K., De Leon, S., Tada, M., Toyoshima, C., MacLennan, D.H. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  9. A calcium pump made visible. Lee, A.G. Curr. Opin. Struct. Biol. (2002) [Pubmed]
  10. Gene expression profiling in dysferlinopathies using a dedicated muscle microarray. Campanaro, S., Romualdi, C., Fanin, M., Celegato, B., Pacchioni, B., Trevisan, S., Laveder, P., De Pittà, C., Pegoraro, E., Hayashi, Y.K., Valle, G., Angelini, C., Lanfranchi, G. Hum. Mol. Genet. (2002) [Pubmed]
  11. Lymph node dissection in cutaneous melanoma: surgical and oncological implications. Peter, R.U., Krähn, G., Kaskel, P. Langenbeck's archives of surgery / Deutsche Gesellschaft für Chirurgie. (2000) [Pubmed]
  12. Characterization of the gene encoding human sarcolipin (SLN), a proteolipid associated with SERCA1: absence of structural mutations in five patients with Brody disease. Odermatt, A., Taschner, P.E., Scherer, S.W., Beatty, B., Khanna, V.K., Cornblath, D.R., Chaudhry, V., Yee, W.C., Schrank, B., Karpati, G., Breuning, M.H., Knoers, N., MacLennan, D.H. Genomics (1997) [Pubmed]
  13. Two-dimensional solid-state NMR reveals two topologies of sarcolipin in oriented lipid bilayers. Buffy, J.J., Traaseth, N.J., Mascioni, A., Gor'kov, P.L., Chekmenev, E.Y., Brey, W.W., Veglia, G. Biochemistry (2006) [Pubmed]
  14. Sarcolipin overexpression in rat slow twitch muscle inhibits sarcoplasmic reticulum Ca2+ uptake and impairs contractile function. Tupling, A.R., Asahi, M., MacLennan, D.H. J. Biol. Chem. (2002) [Pubmed]
  15. Sarcolipin uncouples hydrolysis of ATP from accumulation of Ca2+ by the Ca2+-ATPase of skeletal-muscle sarcoplasmic reticulum. Smith, W.S., Broadbridge, R., East, J.M., Lee, A.G. Biochem. J. (2002) [Pubmed]
  16. Sarcolipin regulates the activity of SERCA1, the fast-twitch skeletal muscle sarcoplasmic reticulum Ca2+-ATPase. Odermatt, A., Becker, S., Khanna, V.K., Kurzydlowski, K., Leisner, E., Pette, D., MacLennan, D.H. J. Biol. Chem. (1998) [Pubmed]
  17. Sarcolipin inhibits polymerization of phospholamban to induce superinhibition of sarco(endo)plasmic reticulum Ca2+-ATPases (SERCAs). Asahi, M., Kurzydlowski, K., Tada, M., MacLennan, D.H. J. Biol. Chem. (2002) [Pubmed]
  18. Sarcolipin, the shorter homologue of phospholamban, forms oligomeric structures in detergent micelles and in liposomes. Hellstern, S., Pegoraro, S., Karim, C.B., Lustig, A., Thomas, D.D., Moroder, L., Engel, J. J. Biol. Chem. (2001) [Pubmed]
  19. Structure and orientation of sarcolipin in lipid environments. Mascioni, A., Karim, C., Barany, G., Thomas, D.D., Veglia, G. Biochemistry (2002) [Pubmed]
  20. In vivo effects of stromelysin on the composition and physical properties of rabbit articular cartilage in the presence and absence of a synthetic inhibitor. Bonassar, L.J., Jeffries, K.A., Frank, E.H., Moore, V.L., Lark, M.W., Bayne, E.K., McDonnell, J., Olszewski, J., Hagmann, W., Chapman, K. Arthritis Rheum. (1995) [Pubmed]
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  22. Cholesteryl butyrate solid lipid nanoparticles inhibit adhesion of human neutrophils to endothelial cells. Dianzani, C., Cavalli, R., Zara, G.P., Gallicchio, M., Lombardi, G., Gasco, M.R., Panzanelli, P., Fantozzi, R. Br. J. Pharmacol. (2006) [Pubmed]
  23. The gamma-subunit of (Na+,K+)-ATPase: a representative example of human single transmembrane protein with a key regulatory role. Berrebi-Bertran, I., Robert, P., Camelin, J.C., Bril, A., Souchet, M. Cell. Mol. Biol. (Noisy-le-grand) (2001) [Pubmed]
  24. The regulation of SERCA-type pumps by phospholamban and sarcolipin. MacLennan, D.H., Asahi, M., Tupling, A.R. Ann. N. Y. Acad. Sci. (2003) [Pubmed]
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