cathD encodes a protein involved in apoptosis and the defense response to Gram-negative bacteria. [Date last reviewed: 2019-09-19] (FlyBase Gene Snapshot)

Jan 29, 2021 · Our findings identify cathD as a dual-function molecule, whose functional switch is regulated by environmental pH and its maturation state, and reveal a novel regulatory role of cathD in...

Sep 18, 2024 · NM_143756.3 → NP_652013.1 cathepsin D, isoform A [Drosophila melanogaster] See identical proteins and their annotated locations for NP_652013.1 Status: REVIEWED

Oct 24, 2013 · The most abundant isoform of purified porcine cathepsin D is a double-chain protein formed by a 15-kDa light chain and a 31-kDa heavy chain, although a 43-kDa single-chain intermediate can also be isolated (Barth and Afting 1984).

The main lysosomal protease cathepsin D (cathD) is essential for maintaining tissue homeostasis via its degradative function, and its loss leads to ceroid accumulation in the mammalian nervous system, which results in progressive neurodegeneration. ...

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Apr 23, 2020 · Using the lepidopteran insect Helicoverpa armigera, a serious agricultural pest, as a model, we revealed the dual functions and regulatory mechanisms of CTSD secretion, expression, and maturation. Glycosylation of asparagine 233 (N233) determined pro-CTSD secretion. The steroid hormone 20-hydroxyecdysone (20E) promoted CTSD expression.

Cathepsin D (cathD) is traditionally regarded as a lysosomal protease that degrades substrates in acidic compartments. Here we report cathD plays an unconventional role as a cofilin phosphatase orchestrating actin remodeling.

Feb 4, 2010 · We discovered that, β 1A-integrin isoform is not only the most abundant isoform, but also that down-modulating cellular PSAP levels significantly reduced its expression in the highly invasive and metastatic PCa cell lines, PC-3, DU-145, and C4-2B (data not shown).

Earlier studies indicated that density-arrested cancer cells released an unidentified growth inhibitor whose secretion was prevented by overexpression of the lysosomal protease cathepsin D (cath...