par Swillens, Stéphane 
;Ludgate, Marian;Mercken, Luc;Dumont, Jacques ;Vassart, Gilbert
Référence Biochemical and biophysical research communications, 137, 1, page (142-148)
Publication Publié, 1986-05
;Ludgate, Marian;Mercken, Luc;Dumont, Jacques ;Vassart, Gilbert Référence Biochemical and biophysical research communications, 137, 1, page (142-148)
Publication Publié, 1986-05
Article révisé par les pairs
| Résumé : | The homology between thyroglobulin and acetylcholinesterase (1) has been analyzed in detail. It contains 28.3% identical amino acids and extends over 544 residues, involving more than 90% of the acetylcholinesterase molecule and the C-terminal portion of thyroglobulin. The hydropathy profiles of the homologous regions have been determined and compared. Their striking resemblance suggests that both proteins adopt a similar three dimensional structure and militates for some common property. As thyroglobulin and acetylcholinesterase are known to interact with cell membranes, we suggest that the acetylcholinesterase-like domain of thyroglobulin is involved in the binding. These observations demonstrate that thyroglobulin has evolved from the condensation of a duplicated copy of the acetylcholinesterase gene with an archaic thyroglobulin gene encoding the major hormonogenic domain. The extensive homology in hydropathy profiles suggests that the two proteins may share antigenic determinants. If this were the case, it would provide a rationale for the demonstration of immunoreactive thyroglobulin in neurons (2) and the pathogenesis of Grave's ophthalmopathy. |
