Cotransfection of Genes Encoding Human Tyrosinase and Tyrosinase-Related Protein-1 Prevents Melanocyte Death and Enhances Melanin Pigmentation and Gene Expression of Lamp-1

1994 ◽  
Vol 213 (1) ◽  
pp. 231-241 ◽  
Author(s):  
Dong Luo ◽  
Hua Chen ◽  
Kowichi Jimbow
Author(s):  
Julia Steitz ◽  
J�rgen Br�ck ◽  
Kerstin Steinbrink ◽  
Alexander Enk ◽  
J�rgen Knop ◽  
...  

1998 ◽  
Vol 7 (4) ◽  
pp. 198-204 ◽  
Author(s):  
Raymond E. Boissy ◽  
Chie Sakai ◽  
Huiquan Zhao ◽  
Takeshi Kobayashi ◽  
Vincent J. Hearing

1994 ◽  
Vol 219 (1-2) ◽  
pp. 127-134 ◽  
Author(s):  
Brigitte BOUCHARD ◽  
Veronique MARMOL ◽  
Ian J. JACKSON ◽  
Dorra CHERIF ◽  
Louis DUBERTRET

1995 ◽  
Vol 95 (2) ◽  
Author(s):  
ScottC. Wildenberg ◽  
RichardA. King ◽  
WilliamS. Oetting

2006 ◽  
Vol 17 (9) ◽  
pp. 4027-4038 ◽  
Author(s):  
Santiago M. Di Pietro ◽  
Juan M. Falcón-Pérez ◽  
Danièle Tenza ◽  
Subba R.G. Setty ◽  
Michael S. Marks ◽  
...  

The adaptor protein (AP)-3 complex is a component of the cellular machinery that controls protein sorting from endosomes to lysosomes and specialized related organelles such as melanosomes. Mutations in an AP-3 subunit underlie a form of Hermansky-Pudlak syndrome (HPS), a disorder characterized by abnormalities in lysosome-related organelles. HPS in humans can also be caused by mutations in genes encoding subunits of three complexes of unclear function, named biogenesis of lysosome-related organelles complex (BLOC)-1, -2, and -3. Here, we report that BLOC-1 interacts physically and functionally with AP-3 to facilitate the trafficking of a known AP-3 cargo, CD63, and of tyrosinase-related protein 1 (Tyrp1), a melanosomal membrane protein previously thought to traffic only independently of AP-3. BLOC-1 also interacts with BLOC-2 to facilitate Tyrp1 trafficking by a mechanism apparently independent of AP-3 function. Both BLOC-1 and -2 localize mainly to early endosome-associated tubules as determined by immunoelectron microscopy. These findings support the idea that BLOC-1 and -2 represent hitherto unknown components of the endosomal protein trafficking machinery.


2017 ◽  
Vol 56 (33) ◽  
pp. 9812-9815 ◽  
Author(s):  
Xuelei Lai ◽  
Harry J. Wichers ◽  
Montserrat Soler‐Lopez ◽  
Bauke W. Dijkstra

Author(s):  
Chidi Duru ◽  
Ijeoma Duru ◽  
Chiagoziem Chidiebere

Many researchers have widely explored the need to replace the harmful compound hydroquinone in skin-lightening creams with more skin-friendly compounds that can give similar results. Some compounds from the plant kingdom have been shown to possess human tyrosinase inhibitory action with no adverse effect on the skin. In this study, the virtual screen of glabridin, kojic acid, arbutin, niacinamide, ascorbic acid, salicin, lactic acid, glutathione, azelaic acid, linoleic acid, glycolic acid, acclaimed to possess this activity as well as the synthetic compound hydroquinone, as human tyrosinase-related protein 1 inhibitor was investigated using computational methods. Site-directed docking was performed at the binding pocket on the enzyme carrying the cocrystallized ligand tropolone. The binding affinity of salicin (-6.7 kcal/mol), a-arbutin (-6.3 kcal/mol), glutathione (-6.2 kcal/mol), ascorbic acid (-5.7 kcal/mol), and niacinamide (-5.7 kcal/mol) were higher than that of the cocrystallized ligand tropolone (-5.5 kcal/mol) and the synthetic skin lightening compound hydroquinone (-4.8 kcal/mol). a-arbutin and glutathione also interacted with similar amino acids units as hydroquinone, suggesting that they followed the exact mechanism of action. These findings strongly corroborate the claim that these natural products could inhibit melanin production and may serve to replace hydroquinone in skin lightening creams.


1992 ◽  
Vol 184 (2) ◽  
pp. 568-575 ◽  
Author(s):  
Koushi Shibata ◽  
Kazuhisa Takeda ◽  
Yasushi Tomita ◽  
Hachiro Tagami ◽  
Shigeki Shibahara

Author(s):  
Shintaro Amae ◽  
Ken-ichi Yasumoto ◽  
Kazuhisa Takeda ◽  
Tetsuo Udono ◽  
Kazuhiro Takahashi ◽  
...  

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