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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

Scand1  -  SCAN domain-containing 1

Mus musculus

Synonyms: 2310003H23Rik, Leap1, PGC-2, Ppargc2
 
 
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Disease relevance of Scand1

  • It has been proposed that impaired degradation is the cause of amyloid A (AA) formation in reactive amyloidosis (Ham et al., Scand J Immunol 1997; 45: 354-60) [1].
  • The activity changes of acid hydrolases quantitatively well reflect the severity of histopathological changes during the myopathy (for review see Salminen, Acta Physiol Scand [Suppl 539] 1985) [2].
 

High impact information on Scand1

  • It has long been known from the results of ultrastructural studies that complement- and immunoglobulin G (IgG)-opsonized particles are phagocytosed differently by macrophages (Kaplan. G. 1977. Scand. J. Immunol. 6:797-807) [3].
  • Ectopic expression of PGC-2 in preadipocytes containing endogenous PPARgamma causes a dramatic increase in fat cell differentiation at both the morphological and molecular levels [4].
  • SDP1 shares a high degree of amino acid sequence identity with PGC-2, a previously identified PPAR gamma 2 co-activator from the mouse [5].

References

  1. Generation of amyloid A protein by the cell lines from amyloid-susceptible and -resistant mice. Ham, D., Skoryna, S.C. Scand. J. Immunol. (2004) [Pubmed]
  2. Food deprivation decreases the exertion-induced acid hydrolase response in mouse skeletal muscle. Kihlström, M., Salminen, A., Vihko, V. European journal of applied physiology and occupational physiology. (1988) [Pubmed]
  3. Molecular definition of distinct cytoskeletal structures involved in complement- and Fc receptor-mediated phagocytosis in macrophages. Allen, L.A., Aderem, A. J. Exp. Med. (1996) [Pubmed]
  4. An adipogenic cofactor bound by the differentiation domain of PPARgamma. Castillo, G., Brun, R.P., Rosenfield, J.K., Hauser, S., Park, C.W., Troy, A.E., Wright, M.E., Spiegelman, B.M. EMBO J. (1999) [Pubmed]
  5. SDP1 is a peroxisome-proliferator-activated receptor gamma 2 co-activator that binds through its SCAN domain. Babb, R., Bowen, B.R. Biochem. J. (2003) [Pubmed]
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