Mitochondria are More Numerous and Smaller in Pink-Eyed Dilution Melanoblasts and Melanocytes Than in Wild-Type Melanocytes in the Neonatal Mouse Epidermis

2008 ◽  
Vol 25 (11) ◽  
pp. 1057-1065 ◽  
Author(s):  
Tomohisa Hirobe ◽  
Kenji Ishizuka ◽  
Shigeru Ogawa ◽  
Hiroyuki Abe
2000 ◽  
Vol 279 (6) ◽  
pp. H3076-H3088 ◽  
Author(s):  
Sylvia O. Suadicani ◽  
Monique J. Vink ◽  
David C. Spray

Focal mechanical stimulation of single neonatal mouse cardiac myocytes in culture induced intercellular Ca2+ waves that propagated with mean velocities of ∼14 μm/s, reaching ∼80% of the cells in the field. Deletion of connexin43 (Cx43), the main cardiac gap junction channel protein, did not prevent communication of mechanically induced Ca2+ waves, although the velocity and number of cells communicated by the Ca2+ signal were significantly reduced. Similar effects were observed in wild-type cardiac myocytes treated with heptanol, a gap junction channel blocker. Fewer cells were involved in intercellular Ca2+ signaling in both wild-type and Cx43-null cultures in the presence of suramin, a P2-receptor blocker; blockage was more effective in Cx43-null than in wild-type cells. Thus gap junction channels provide the main pathway for communication of slow intercellular Ca2+ signals in wild-type neonatal mouse cardiac myocytes. Activation of P2-receptors induced by ATP release contributes a secondary, extracellular pathway for transmission of Ca2+ signals. The importance of such ATP-mediated Ca2+ signaling would be expected to be enhanced under ischemic conditions, when release of ATP is increased and gap junction channels conductance is significantly reduced.


1982 ◽  
Vol 23 (1-3) ◽  
pp. 243-249 ◽  
Author(s):  
Martin Ramsden ◽  
Diethard Loehren ◽  
Allan Balmain

2002 ◽  
Vol 13 (6) ◽  
pp. 1953-1964 ◽  
Author(s):  
Kun Chen ◽  
Prashiela Manga ◽  
Seth J. Orlow

The processing of tyrosinase, which catalyzes the limiting reaction in melanin synthesis, was investigated in melan-p1 melanocytes, which are null at the p locus. Endoglycosidase H digestion showed that a significant fraction of tyrosinase was retained in the endoplasmic reticulum. This retention could be rescued either by transfection of melan-p1 cells with an epitope-tagged wild-typep transcript or by treatment with either bafilomycin A1 or ammonium chloride. We found that the endoplasmic reticulum contains a significant amount of p protein, thus supporting a role for p within this compartment. Using immunofluoresence, we showed that most mature full-length tyrosinase in melan-p1 cells was located in the perinuclear area near the Golgi, in contrast to its punctate melanosomal pattern in wild-type melanocytes. Expression of p in melan-p1 cells restored tyrosinase to melanosomes. Triton X-114 phase separation revealed that an increased amount of tyrosinase was proteolyzed in melan-p1 cells compared with wild-type melanocytes. The proteolyzed tyrosinase was no longer membrane bound, but remained enzymatically active and a large proportion was secreted into the culture medium of melan-p1 cells. We conclude that p regulates posttranslational processing of tyrosinase, and hypopigmentation in melan-p1 cells is the result of altered tyrosinase processing and trafficking.


Science ◽  
1983 ◽  
Vol 221 (4614) ◽  
pp. 962-964 ◽  
Author(s):  
S Grayson ◽  
A. Johnson-Winegar ◽  
P. Elias

2007 ◽  
Vol 24 (3) ◽  
pp. 209-217 ◽  
Author(s):  
Tomohisa Hirobe ◽  
Kazumasa Wakamatsu ◽  
Shosuke Ito

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