The formation of intracellular aggregates containing @entity8095 (a- @entity15735 ) is one of the key steps in the progression of @entity191 and @entity303 with @entity1832 . Recently, it was reported that pathological a- @entity15735 fibrils can undergo cell-to-cell transmission and form Lewy body-like aggregates. However, little is known about how they form a- @entity15735 aggregates from fibril seeds. Here, we developed an assay to study the process of aggregate formation using fluorescent protein-tagged a- @entity15735 -expressing cells and examined the aggregate forming activity of exogenous a- @entity15735 fibrils. a- @entity15735 fibril-induced formation of intracellular aggregates was suppressed by a @entity467 specific inhibitor, but not by a @entity10815 inhibitor. a- @entity15735 fibrils pretreated with @entity467 in vitro enhanced seeding activity in cells. Knockdown of @entity467 also reduced fibril-induced aggregate formation. Moreover, using @entity3220 immunocytochemistry and live-cell imaging, we observed that these aggregates initially occurred in the lysosome. They then rapidly grew larger and moved outside the boundary of the lysosome within one day. These results suggest that the lysosomal protease @entity467 is involved in triggering intracellular aggregate formation by a- @entity15735 fibrils.

Lysosomal enzyme XXXX enhances the aggregate forming activity of exogenous @entity8095 fibrils.

@entity10815 :: ('1509', 'Gene') :: ['cathepsin D'] @entity15735 :: ('23336', 'Gene') :: ['Syn'] @entity3220 :: ('3916', 'Gene') :: ['LAMP-1'] @entity8095 :: ('6622', 'Gene') :: ['a-synuclein'] @entity303 :: ('MESH:D003704', 'Disease') :: ['dementia'] @entity467 :: ('1508', 'Gene') :: ['cathepsin B'] @entity191 :: ('MESH:D010300', 'Disease') :: ["Parkinson's disease"] @entity1832 :: ('MESH:D020961', 'Disease') :: ['Lewy bodies']
@entity467 :: (1508,Gene) :: ['cathepsin B']
