Ontology highlight
ABSTRACT:
SUBMITTER: Levinson RT
PROVIDER: S-EPMC3575045 | biostudies-literature | 2013
REPOSITORIES: biostudies-literature
Levinson Rebecca T RT Olatoye Oludare O OO Randles Edward G EG Howell Kyle G KG DiCostanzo Ara Celi AC Ramirez-Alvarado Marina M
Scientific reports 20130101
Light chain (AL) amyloidosis is characterized by the misfolding of immunoglobulin light chains, accumulating as amyloid fibrils in vital organs. Multiple reports have indicated that amyloidogenic light chains internalize into a variety of cell types, but these studies used urine-derived proteins without indicating any protein sequence information. As a result, the role of somatic mutations in amyloidogenic protein internalization has not been yet studied. We characterized the internalization of ...[more]