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Herpes Zoster Lesions on Reconstructed Breast Skin: Rare Objective Proof of Reinervation
Weitgasser, Laurenz,Valina, Stephan Wolfgang,Schoeller, Thomas,Ehebruster, Gudrun Korean Society of Plastic and Reconstructive Surge 2017 Archives of Plastic Surgery Vol.44 No.1
Blazed up Herpes zoster lesions have been described in very few patients after free and pedicled flap transfer for reconstructive purpose. Although sensory recovery after flap reconstructions has been studied extensively most studies addressed subjective perceptions of sensation. Objective investigations of spontaneous reinervation of free and pedicled flaps are rare. We would like to present a witnessed herpes zoster infection of a latissimus dorsi skin flap 2 years after breast reconstruction.
Herpes Zoster Lesions on Reconstructed Breast Skin: Rare Objective Proof of Reinervation
Laurenz Weitgasser,Stephan Wolfgang Valina,Thomas Schoeller,Gudrun Ehebruster 대한성형외과학회 2017 Archives of Plastic Surgery Vol.44 No.1
Blazed up Herpes zoster lesions have been described in very few patients after free and pedicled flap transfer for reconstructive purpose. Although sensory recovery after flap reconstructions has been studied extensively most studies addressed subjective perceptions of sensation. Objective investigations of spontaneous reinervation of free and pedicled flaps are rare. We would like to present a witnessed herpes zoster infection of a latissimus dorsi skin flap 2 years after breast reconstruction.
Augmentation of poly(ADP-ribose) polymerase-dependent neuronal cell death by acidosis
Zhang, Jian,Li, Xiaoling,Kwansa, Herman,Kim, Yun Tai,Yi, Liye,Hong, Gina,Andrabi, Shaida A,Dawson, Valina L,Dawson, Ted M,Koehler, Raymond C,Yang, Zeng-Jin SAGE Publications 2017 Journal of cerebral blood flow and metabolism Vol.37 No.6
<P> Tissue acidosis is a key component of cerebral ischemic injury, but its influence on cell death signaling pathways is not well defined. One such pathway is parthanatos, in which oxidative damage to DNA results in activation of poly(ADP-ribose) polymerase and generation of poly(ADP-ribose) polymers that trigger release of mitochondrial apoptosis-inducing factor. In primary neuronal cultures, we first investigated whether acidosis per sé is capable of augmenting parthanatos signaling initiated pharmacologically with the DNA alkylating agent, N-methyl- N′-nitro- N-nitrosoguanidine. Exposure of neurons to medium at pH 6.2 for 4 h after N-methyl- N′-nitro- N-nitrosoguanidine washout increased intracellular calcium and augmented the N-methyl- N′-nitro- N-nitrosoguanidine-evoked increase in poly(ADP-ribose) polymers, nuclear apoptosis-inducing factor , and cell death. The augmented nuclear apoptosis-inducing factor and cell death were blocked by the acid-sensitive ion channel-1a inhibitor, psalmotoxin. In vivo, acute hyperglycemia during transient focal cerebral ischemia augmented tissue acidosis, poly(ADP-ribose) polymers formation, and nuclear apoptosis-inducing factor , which was attenuated by a poly(ADP-ribose) polymerase inhibitor. Infarct volume from hyperglycemic ischemia was decreased in poly(ADP-ribose) polymerase 1-null mice. Collectively, these results demonstrate that acidosis can directly amplify neuronal parthanatos in the absence of ischemia through acid-sensitive ion channel-1a . The results further support parthanatos as one of the mechanisms by which ischemia-associated tissue acidosis augments cell death. </P>
Parkin loss leads to PARIS-dependent declines in mitochondrial mass and respiration
Stevens, Daniel A.,Lee, Yunjong,Kang, Ho Chul,Lee, Byoung Dae,Lee, Yun-Il,Bower, Aaron,Jiang, Haisong,Kang, Sung-Ung,Andrabi, Shaida A.,Dawson, Valina L.,Shin, Joo-Ho,Dawson, Ted M. National Academy of Sciences 2015 PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF Vol.112 No.37
<P><B>Significance</B></P><P>Mutations or inactivation of parkin causes Parkinson’s disease (PD) in humans. Recent studies have focused on parkin’s role in mitochondrial quality control in the pathogenesis of PD, including defects in mitophagy, mitochondrial fission, fusion, and transport. This study shows that parkin also controls mitochondrial biogenesis and that defects in mitochondrial biogenesis drive the loss of dopamine (DA) neurons due to the absence of parkin. The findings support the role of parkin in regulating multiple arms of mitochondrial quality control and suggest that maintaining mitochondrial biogenesis is critically important in the survival of DA neurons.</P><P>Mutations in parkin lead to early-onset autosomal recessive Parkinson’s disease (PD) and inactivation of parkin is thought to contribute to sporadic PD. Adult knockout of parkin in the ventral midbrain of mice leads to an age-dependent loss of dopamine neurons that is dependent on the accumulation of parkin interacting substrate (PARIS), zinc finger protein 746 (ZNF746), and its transcriptional repression of PGC-1α. Here we show that adult knockout of parkin in mouse ventral midbrain leads to decreases in mitochondrial size, number, and protein markers consistent with a defect in mitochondrial biogenesis. This decrease in mitochondrial mass is prevented by short hairpin RNA knockdown of PARIS. PARIS overexpression in mouse ventral midbrain leads to decreases in mitochondrial number and protein markers and PGC-1α–dependent deficits in mitochondrial respiration. Taken together, these results suggest that parkin loss impairs mitochondrial biogenesis, leading to declining function of the mitochondrial pool and cell death.</P>
PINK1-dependent recruitment of Parkin to mitochondria in mitophagy.
Vives-Bauza, Cristofol,Zhou, Chun,Huang, Yong,Cui, Mei,de Vries, Rosa L A,Kim, Jiho,May, Jessica,Tocilescu, Maja Aleksandra,Liu, Wencheng,Ko, Han Seok,Magran?, Jordi,Moore, Darren J,Dawson, Valina L,G National Academy of Sciences 2010 PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF Vol.107 No.1
<P>Phosphatase and tensin homolog (PTEN)-induced putative kinase 1 (PINK1) and PARK2/Parkin mutations cause autosomal recessive forms of Parkinson's disease. Upon a loss of mitochondrial membrane potential (DeltaPsi(m)) in human cells, cytosolic Parkin has been reported to be recruited to mitochondria, which is followed by a stimulation of mitochondrial autophagy. Here, we show that the relocation of Parkin to mitochondria induced by a collapse of DeltaPsi(m) relies on PINK1 expression and that overexpression of WT but not of mutated PINK1 causes Parkin translocation to mitochondria, even in cells with normal DeltaPsi(m). We also show that once at the mitochondria, Parkin is in close proximity to PINK1, but we find no evidence that Parkin catalyzes PINK1 ubiquitination or that PINK1 phosphorylates Parkin. However, co-overexpression of Parkin and PINK1 collapses the normal tubular mitochondrial network into mitochondrial aggregates and/or large perinuclear clusters, many of which are surrounded by autophagic vacuoles. Our results suggest that Parkin, together with PINK1, modulates mitochondrial trafficking, especially to the perinuclear region, a subcellular area associated with autophagy. Thus by impairing this process, mutations in either Parkin or PINK1 may alter mitochondrial turnover which, in turn, may cause the accumulation of defective mitochondria and, ultimately, neurodegeneration in Parkinson's disease.</P>