Jaana Tyynelä

TL;DR: It is reasonable to suggest that cathepsin D deficiency caused by mutations in the corresponding gene may underlie all cases of congenital NCL and should be considered as a possible diagnosis in microcephalic neonates, who present with seizures at or before birth.

TL;DR: It is postulate that CathD promotes 'synucleinase' activity, and that enhancing its function may lower aSyn concentrations in vivo, which would imply that ctsd gene mutations result in a lysosomal storage disorder that includes microscopic and biochemical evidence of aSyn misprocessing.

TL;DR: A novel form of NCL is shown, congenital ovine NCL, is caused by a deficiency in the lysosomal aspartyl proteinase cathepsin D, resulting in severe cerebrocortical atrophy and early death, providing strong evidence for an important role of cathePSin D in neuronal development and/or homeostasis.

TL;DR: The ability of human tumor cell-derived trypsin-2 to activate latent MMPs suggests a role for trypsIn-2 in initiating the proteinase cascade that mediates tumor invasion and metastasis formation.

TL;DR: This work identified in five individuals one of two disease-causing mutations, c.346_348delCTC and c.344T>G, in DNAJC5 encoding cysteine-string protein alpha (CSPα), which confirms a neuroprotective role for CSPα in humans and demonstrates the need for detailed investigation of CSP α in the neuronal ceroid lipofuscinoses and other neurodegenerative diseases presenting with neuronal protein aggregation.