The mouse neuronal apoptosis inhibitory protein gene maps to a conserved syntenic region of mouse chromosome 13

1997 ◽  
Vol 8 (3) ◽  
pp. 222-222 ◽  
Author(s):  
Christine J. DiDonato ◽  
Joseph H. Nadeau ◽  
Louise R. Simard
1999 ◽  
Vol 264 (3) ◽  
pp. 998-1006 ◽  
Author(s):  
Kenji Yamamoto ◽  
Harumi Sakai ◽  
Shinji Hadano ◽  
Yoichi Gondo ◽  
Joh-E Ikeda

1996 ◽  
Vol 133 (1) ◽  
pp. 43-47 ◽  
Author(s):  
Y Ando-Akatsuka ◽  
M Saitou ◽  
T Hirase ◽  
M Kishi ◽  
A Sakakibara ◽  
...  

Occludin has been identified from chick liver as a novel integral membrane protein localizing at tight junctions (Furuse, M., T. Hirase, M. Itoh, A. Nagafuchi, S. Yonemura, Sa. Tsukita, and Sh. Tsukita. 1993. J. Cell Biol. 123:1777-1788). To analyze and modulate the functions of tight junctions, it would be advantageous to know the mammalian homologues of occludin and their genes. Here we describe the nucleotide sequences of full length cDNAs encoding occludin of rat-kangaroo (potoroo), human, mouse, and dog. Rat-kangaroo occludin cDNA was prepared from RNA isolated from PtK2 cell culture, using a mAb against chicken occludin, whereas the others were amplified by polymerase chain reaction based on the sequence found around the human neuronal apoptosis inhibitory protein gene. The amino acid sequences of the three mammalian (human, murine, and canine) occludins were very closely related to each other (approximately 90% identity), whereas they diverged considerably from those of chicken and rat-kangaroo (approximately 50% identity). Implications of these data and novel experimental options in cell biological research are discussed.


2010 ◽  
Vol 292 (2) ◽  
pp. 176-185 ◽  
Author(s):  
Helen H.L. Chiu ◽  
Theresa M.K. Yong ◽  
Jun Wang ◽  
Yuwei Wang ◽  
Robert L. Vessella ◽  
...  

2005 ◽  
Vol 25 (7) ◽  
pp. 794-806 ◽  
Author(s):  
Yoshinori Okada ◽  
Harumi Sakai ◽  
Eri Kohiki ◽  
Etsuko Suga ◽  
Yoshiko Yanagisawa ◽  
...  

Neuronal apoptosis inhibitory protein (NAIP/BIRC1), the inhibitor of apoptosis protein (IAP) family member, suppresses neuronal cell death induced by a variety of insults, including cell death from ischemia and stroke. The goal of the present study was to develop an efficient method for identification of compounds with the ability to upregulate endogenous NAIP and to determine the effects on these compounds on the cellular response to ischemia. A novel NAIP-enzyme-linked immunosorbent assay (ELISA)-based in vitro drug-screening system is established. Use of this system identified an antagonist of dopamine D4 receptor, termed L-745,870, with a potent NAIP upregulatory effect. L-745,870-mediated NAIP upregulation in neuronal and nonneuronal cultured cells resulted in decreased vulnerability to oxidative stress-induced apoptosis. Reducing NAIP expression via RNA interference techniques resulted in prevention of L-745,870-mediated protection from oxidative stress. Further, systemic administration of L-745,870 attenuated ischemia-induced damage of the hippocampal CA1 neurons and upregulated NAIP expression in the rescued hippocampal CA1 neurons in a gerbil model. These data suggest that the NAIP upregulating compound, L-745,870, has therapeutic potential in acute ischemic disorders and that our NAIP-ELISA-based drug screening may facilitate the discovery of novel neuroprotective compounds.


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