Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.4.23.5 (
cathepsin D
)
4,130
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
mu-Calpain quickly split the alpha-connectin in myofibrils into beta-connectin, and then produced a 1700-kDa component. Cathepsin D also split alpha-connectin into beta-connectin, further degrading it to fragments smaller than the 1700-kDa component with increasing incubation time. The action of
cathepsin D
on the connectin molecule was distinctly different from that of
mu-calpain
in terms of the splitting rate and manner. When freshly excised muscle was exposed to a temperature of 37 degrees C, complete disappearance of connectin (alpha, beta and 1700-kDa component) was observed within 36 h. In contrast, at 2 degrees C, about 75% of connectin was retained as beta-form even after 3 weeks. The present data suggest that the degradation of connectin in muscle might be caused by
mu-calpain
in the early stage of aging, and then with time, this action is replaced by m-calpain or
cathepsin D
. However, the possibility of other intrinsic proteases participating in the degradation of connectin still remains.
...
PMID:Cleavage of connectin by calpain and cathepsin D. 778 5
Cochlear and vestibular sensory cells undergo apoptosis when exposed to aminoglycoside antibiotics in organ culture, but mechanisms of chronic drug-induced hair cell loss in vivo are unclear. We investigated cell death pathways in a mouse model of progressive kanamycin-induced hair cell loss. Hair cell nuclei showed both apoptotic- and necrotic-like appearances but markers for classic apoptotic pathways (cytochrome c, caspase-9, caspase-3, JNK, TUNEL) were absent. In contrast, drug treatment caused EndoG translocation, activation of
mu-calpain
, and both the synthesis and activation of
cathepsin D
. Poly (ADP-ribose) polymerase 1 (PARP1) was decreased, but a caspase-derived 89 kDa PARP1 fragment was not present. The mRNA level of PARP1 remained unchanged. Thus, chronic administration of aminoglycosides causes multiple forms of cell death, without a major contribution by classic apoptosis. These results provide a better understanding of the toxic effects of aminoglycosides and are relevant to design protection from aminoglycoside-induced hearing loss.
...
PMID:Caspase-independent pathways of hair cell death induced by kanamycin in vivo. 1602 Nov 80
