title: Cutaneous amyloidoses: a minimum common denominator in their amino acid sequence.
abstract: BACKGROUND
  Peptides forming amyloid fibrils in cutaneous amyloidoses are derived from various precursors, often unrelated to each other. We aimed to identify an amino acid pattern shared by disease-relevant peptides associated with newly reported and already known cutaneous amyloidoses.
  
  
  METHODS
  We probed proteins of cutaneous and non-cutaneous amyloidoses for the amyloid motif identified previously ("D/E/N/Q, A/G, D/E/N/Q, 4-20X, V/I/L/M, D/E/N/Q, R/K/H, 0-6X, V/I/L/M, 0-5X, F/Y/W, 4-5X, D/E/N/Q, 0-2X, R/K/H, 0-12X, A/G, V/I/L/M, 0-3X, V/I/L/M, 0-2X, A/G"). Once segments containing the motif were found, these were subject to multiple alignment to detect similarities and dissimilarities between them.
  
  
  RESULTS
  The amyloid motif was present, totally or partially, in all proteins; in turn, it was contained, completely or incompletely, in segments of such proteins known to be deposited in the corresponding amyloidoses. The aligned segments of the cutaneous amiloidoses were more similar to each other than to those of the noncutaneous amyloidoses.
  
  
  CONCLUSIONS
  The motif-based approach can contribute to the multidisciplinary solution of the complex problem of the pathogenesis of amyloidosis, and could help to identify possible new amyloid forming proteins.
authors.affiliation: Department of Clinical and Experimental Medicine, University of Messina, Messina, Italy. Electronic address: f.guarneri@tiscali.it.
authors.forename: Fabrizio
authors.initials: F
authors.lastname: Guarneri
authors.affiliation: Department of Clinical and Experimental Medicine, University of Messina, Messina, Italy.
authors.forename: Serafinella Patrizia
authors.initials: SP
authors.lastname: Cannavò
authors.affiliation: Department of Clinical and Experimental Medicine, University of Messina, Messina, Italy; Master Program on Childhood, Adolescent and Women׳s Endocrine Health, University of Messina, Messina, Italy; Interdepartmental Program on Molecular & Clinical Endocrinology and Women׳s Endocrine Health, University Hospital, Policlinico G. Martino, Messina, Italy.
authors.forename: Salvatore
authors.initials: S
authors.lastname: Benvenga
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry*; D028226:Amyloidosis, Familial / Q000378:metabolism*; D019295:Computational Biology / Q000379:methods; D003198:Computer Simulation; D006801:Humans; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D012873:Skin Diseases, Genetic / Q000378:metabolism*; D012984:Software
chemical_list: D000682:Amyloid; D010455:Peptides
keywords: Amino acid sequence homology; Amyloidosis; Bioinformatics; Dermatology; Pathogenesis