Disulfide-dependent multimeric assembly of Resistin family hormones

Science

Volumn 304, Issue 5674, 2004, Pages 1154-1158

  Patel, Saurabh D ^a   Rajala, Michael W ^b   Rossetti, Luciano ^b   Scherer, Philipp E ^b   Shapiro, Lawrence ^a,c,d  

^a Och Spine at New York Presbyterian Hospitals   (United States)

^b ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^c NewYork Presbyterian Hospital   (United States)

^d New York Presbyterian Hospital   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL ORGANS; CHEMICAL BONDS; CRYSTAL STRUCTURE; DISEASES;

DIABETES; OBESITY; RESISTIN-LIKE MOLECULE (RELM) HORMONES;

HORMONES;

2,4 THIAZOLIDINEDIONE DERIVATIVE; ADIPONECTIN; INSULIN; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR AGONIST; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; RESISTIN;

BIOLOGY;

ADIPOCYTE; ANIMAL CELL; ARTICLE; CRYSTAL STRUCTURE; DIABETES MELLITUS; DISEASE ASSOCIATION; DISULFIDE BOND; DYSLIPIDEMIA; INSULIN RESISTANCE; NON INSULIN DEPENDENT DIABETES MELLITUS; NONHUMAN; OBESITY; PRIORITY JOURNAL; PROTEIN ASSEMBLY; STRUCTURE ANALYSIS;

ADIPOCYTES; ADIPONECTIN; AMINO ACID SEQUENCE; ANIMALS; CELL LINE; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; CULTURE MEDIA, CONDITIONED; DISULFIDES; GLUCOSE; HORMONES, ECTOPIC; HUMANS; INSULIN; INSULIN RESISTANCE; INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS; LIVER; MICE; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; MUTATION; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEINS; RESISTIN;

ANIMALIA;

EID: 2442707674     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1093466     Document Type: Article

References (35)

1. C. L. Ogden, K. M. Flegat, M. D. Carroll, C. L. Johnson, JAMA 288, 1728 (2002).
2. K. M. Flegal, M. D. Carroll, C. L. Ogden, C. L. Johnson, JAMA 288, 1723 (2002).
3. J. J. Reilly et al., Arch. Dis. Child. 88, 748 (2003).
4. U. S. Census, Bureau of the Census, 2000 Census Estimates; www.cdc.gov/diabetes/pubs/estimates.htm.
5. I. H. Jazet, H. Pijl, A. E. Meinders, Neth. J. Med. 61, 194 (2003).
6. T. Fujita et al., Diabetes 32, 804 (1983).
7. T. Fujiwara, S. Yoshioka, T. Yoshioka, I. Ushiyama, H. Horikoshi, Diabetes 37, 1549 (1988).
8. P. E. Beales, P. Pozzilli, Diabetes Metab. Res. Rev. 18, 114 (2002).
9. H. Hauner, Diabetes Metab. Res. Rev. 18 (suppl. 2), S10 (2002).
10. R. R. Henry, Endocrinol. Metab. Clin. North Am. 26, 553 (1997).
11. M. W. Rajala, P. E. Scherer, Endocrinology 144, 3765 (2003).
12. A. H. Berg, T. P. Combs, X. Du, M. Brownlee, P. E. Scherer, Nature Med. 7, 947 (2001).
13. C. M. Steppan et al., Nature 409, 307 (2001).
14. T. P. Combs et al., Endocrinology 143, 998 (2002).
15. I. N. Holcomb et al., EMBO J. 19, 4046 (2000).
16. K. H. Kim, K. Lee, Y. S. Moon, H. S. Sul, J. Biol. Chem. 276, 11252 (2001).
17. H. W. Rajala et al., Mol. Endocrinol. 16, 1920 (2002).
18. C. M. Steppan et al., Proc. Natl. Acad. Sci. U.S.A. 98, 502 (2001).
19. B. Gerstmayer et al., Genomics 81, 588 (2003).
20. M. W. Rajala, S. Obici, P. E. Scherer, L. Rossetti, J. Clin. Invest. 111, 225 (2003).
21. R. R. Banerjee et al., Science 303, 119S (2004).
22. T. P. Combs, A. H. Berg, S. Obici, P. E. Scherer, L Rossetti, J. Clin. Invest. 108, 1875 (2001).
23. P. E. Scherer, S. Williams, H. Fogliano, G. Baldini, H. F. Lodish, J. Biol. Chem. 270, 26746 (1995).
24. L. Shapiro, P. E. Scherer, Curr. Biol. 8, 335 (1998).
25. U. B. Pajvani et al., J. Biol. Chem. 278, 9073 (2003).
26. U. B. Pajvani et al., J. Biol. Chem. 279, 12152 (2004).
27. Materials and methods are available as supporting material on Science Online.
28. Z. Dauter, M. Dauter, K. R. Rajashankar, Acta Crystallogr. D Biol. Crystallogr. 56, 232 (2000).
29. L. Holm, C. Sander, Nucleic Acids Res. 26, 316 (1998).
30. R. R. Banerjee, M. A. Lazar, J. Biol. Chem. 276, 25970 (2001).
31. D. L. Brasaemle et al., J. Lipid Res. 38, 2249 (1997).
32. T. Anelli et al., EMBO J. 22, 5015 (2003).
33. W. L. DeLano (2002), http://pymol.sourceforge.net
34. H. Nielsen, J. Engelbrecht, S. Brunak, G. von Heijne, Protein Eng. 10, 1 (1997).
35. We thank the personnel of Advanced Photon Source (APS) beamlines 31-ID and 32-ID; National Synchrotron Light Source beamlines X4, X9, and X25; and A. Gogos and T. Boggon for help with data collection; M. Collins, A. Gogos, and D. Brasaemle for help with biochemical experiments; and F. P. Davis and A. Sali for help with solvent accessibility calculations. We also thank Z. Wang, J.-Y. Kim, and A. Narwocki for help at various stages of this project. We are grateful to W. A. Hendrickson and P. D. Kwong for critical comments. The structures reported in this paper have been deposited in the PDB as 1RFX, 1RGX, and 1RH7. This work was supported in part by grants from NIH and the Research to Prevent Blindness Foundation. Part of this work was performed as part of the National Institute of General Medical Sciences' New York Structural Genomics Research Consortium (NYS-GXRC). Use of the APS was supported by the U.S. Department of Energy, Office of Science, Office of Basic Energy Science, under Contract No. W-31-109-Eng-38. Use of the SGX Collaborative Access Team (SGX-CAT) beamline facilities at sector 31 of the APS was provided by Structural GenomiX, Inc., which constructed and operates the facility.