The C-terminal peptide of antitrypsin (AAT) increases LDL binding in HepG2 cells
β Scribed by S. Janciauskiene; S. Lindgren
- Book ID
- 118568300
- Publisher
- Elsevier Science
- Year
- 1998
- Tongue
- English
- Weight
- 176 KB
- Volume
- 28
- Category
- Article
- ISSN
- 0168-8278
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π SIMILAR VOLUMES
Amyloid fibrils of diverse origin are known to disturb vital cellular functions and induce cell death. In this study, the effects of amyloid fibrils from the C-terminal fragment (C-36) of cleaved alpha1-antitrypsin (AAT) on low-density lipoprotein (LDL) metabolism were investigated in HepG2 cells. T
SPAAT (short piece of a 1 -antitrypsin [AAT]), the 44-residue C-terminal peptide of AAT, was originally isolated from human placenta [Niemann et al. (1992): Matrix 12:233-241]. It was shown to be a competitive inhibitor of serine proteases [Niemann et al. (in press): Biochem Biophys Acta]. The bindi