UVA/B-induced apoptosis in human melanocytes involves translocation of cathepsins and Bcl-2 family members

The Journal of Investigative Dermatology
Cecilia BivikK Ollinger

Abstract

We demonstrate UVA/B to induce apoptosis in human melanocytes through the mitochondrial pathway, displaying cytochrome c release, caspase-3 activation, and fragmentation of nuclei. The outcome of a death signal depends on the balance between positive and negative apoptotic regulators, such as members of the Bcl-2 protein family. Apoptotic melanocytes, containing fragmented nucleus, show translocation of the proapoptotic proteins Bax and Bid from the cytosol to punctate mitochondrial-like structures. Bcl-2, generally thought to be attached only to membranes, was in melanocytes localized in the cytosol as well. In the fraction of surviving melanocytes, that is, cells with morphologically unchanged nucleus, the antiapoptotic proteins Bcl-2 and Bcl-X(L) were translocated to mitochondria following UVA/B. The lysosomal proteases, cathepsin B and D, which may act as proapoptotic mediators, were released from lysosomes to the cytosol after UVA/B exposure. Proapoptotic action of the cytosolic cathepsins was confirmed by microinjection of cathepsin B, which induced nuclear fragmentation. Bax translocation and apoptosis were markedly reduced in melanocytes after pretreatment with either cysteine or aspartic cathepsin inhibitors. No initia...Continue Reading

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Citations

Jul 25, 2008·Apoptosis : an International Journal on Programmed Cell Death·Cecilia Bivik, Karin Ollinger
Jan 16, 2010·Apoptosis : an International Journal on Programmed Cell Death·Ann-Charlotte JohanssonKarin Ollinger
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Dec 16, 2020·Physical Biology·Pooja Dnyane, Chetan Gadgil
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