| First Author | Lewis PA | Year | 2001 |
| Journal | Biochim Biophys Acta | Volume | 1537 |
| Issue | 1 | Pages | 58-62 |
| PubMed ID | 11476963 | Mgi Jnum | J:120781 |
| Mgi Id | MGI:3707978 | Doi | 10.1016/s0925-4439(01)00054-0 |
| Citation | Lewis PA, et al. (2001) Expression of BRI-amyloid beta peptide fusion proteins: a novel method for specific high-level expression of amyloid beta peptides. Biochim Biophys Acta 1537(1):58-62 |
| abstractText | In order to develop transgenic animal models that selectively overexpress various Abeta peptides, we have developed a novel expression system that selectively expresses Abeta40 or Abeta42 in the secretory pathway. This system utilizes fusion constructs in which the sequence encoding the 23-amino-acid ABri peptide at the carboxyl terminus of the 266-amino-acid type 2 transmembrane protein BRI is replaced with a sequence encoding either Abeta40 or Abeta42. Constitutive processing of the resultant BRI-Abeta fusion proteins in transfected cells results in high-level expression and secretion of the encoded Abeta peptide. Significantly, expression of Abeta42 from the BRI-Abeta42 construct resulted in no increase in secreted Abeta40, suggesting that the majority of Abeta42 is not trimmed by carboxypeptidase to Abeta40 in the secretory pathway. |
