scholarly journals Molecular Cloning of ILP-2, a Novel Member of the Inhibitor of Apoptosis Protein Family

2001 ◽  
Vol 21 (13) ◽  
pp. 4292-4301 ◽  
Author(s):  
Bettina W. M. Richter ◽  
Samy S. Mir ◽  
Lisa J. Eiben ◽  
Jennifer Lewis ◽  
Stephanie Birkey Reffey ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Inhibitor Of Apoptosis ◽  
Physical Interaction ◽  
Caspase 9 ◽  
Inhibitor Of Apoptosis Protein ◽  
Normal Tissues ◽  
Apoptosis Protein ◽  
Processed Form

ABSTRACT Inhibitor of apoptosis protein (IAP)-like protein-1 (ILP-1) (also known as X-linked IAP [XIAP] and mammalian IAP homolog A [MIHA]) is a potent inhibitor of apoptosis and exerts its effects, at least in part, by the direct association with and inhibition of specific caspases. Here, we describe the molecular cloning and characterization of a human gene related to ILP-1, termed ILP-2. Despite high homology to ILP-1, ILP-2 is encoded by a distinct gene, which in normal tissues is expressed solely in testis. In contrast to ILP-1, overexpression of ILP-2 had no protective effect on apoptosis mediated by Fas (also known as CD95) or tumor necrosis factor. However, ILP-2 potently inhibited apoptosis induced by overexpression of Bax or by coexpression of caspase 9 with Apaf-1, and preincubation of cytosolic extracts with ILP-2 abrogated caspase activation in vitro. A processed form of caspase 9 could be coprecipitated with ILP-2 from cells, suggesting a physical interaction between ILP-2 and caspase 9. Thus, ILP-2 is a novel IAP family member with restricted specificity for caspase 9.

scholarly journals Molecular cloning and characterization of an inhibitor of apoptosis protein (IAP) from the tiger shrimp, Penaeus monodon

2008 ◽  
Vol 32 (2) ◽  
pp. 121-133 ◽  
Author(s):  
Jiann-Horng Leu ◽  
Yu-Chen Kuo ◽  
Guang-Hsiung Kou ◽  
Chu-Fang Lo
Keyword(s):  
Molecular Cloning ◽  
Penaeus Monodon ◽  
Inhibitor Of Apoptosis ◽  
Inhibitor Of Apoptosis Protein ◽  
Tiger Shrimp ◽  
Apoptosis Protein

Molecular cloning and characterization of a novel inhibitor of apoptosis protein from Xenopus laevis

2003 ◽  
Vol 301 (1) ◽  
pp. 236-242 ◽  
Author(s):  
Kwang-Hoon Song ◽  
Tae-Moon Kim ◽  
Han-Jong Kim ◽  
Jung Woo Kim ◽  
Hong-Hee Kim ◽  
...  
Keyword(s):  
Xenopus Laevis ◽  
Molecular Cloning ◽  
Inhibitor Of Apoptosis ◽  
Inhibitor Of Apoptosis Protein ◽  
Apoptosis Protein

Genomic Characterization of the Mouse Inhibitor of Apoptosis Protein 1 and 2 Genes

Genomics ◽  
1997 ◽  
Vol 46 (3) ◽  
pp. 495-503 ◽  
Author(s):  
Peter Liston ◽  
Charles Lefebvre ◽  
Wai Gin Fong ◽  
Jian Ying Xuan ◽  
Robert G. Korneluk
Keyword(s):  
Inhibitor Of Apoptosis ◽  
Inhibitor Of Apoptosis Protein ◽  
Apoptosis Protein ◽  
Genomic Characterization

scholarly journals Molecular characterization of an inhibitor of apoptosis protein (IAPs) in freshwater pearl mussel, Hyriopsis schlegelii

Bioengineered ◽  
2019 ◽  
Vol 10 (1) ◽  
pp. 365-373 ◽  
Author(s):  
Di Wu ◽  
Chengyuan Wang ◽  
Wanchang Zhang ◽  
Kou Peng ◽  
Junqing Sheng ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Inhibitor Of Apoptosis ◽  
Pearl Mussel ◽  
Freshwater Pearl Mussel ◽  
Inhibitor Of Apoptosis Protein ◽  
Apoptosis Protein

Cellular inhibitor of apoptosis protein 2 controls human colonic epithelial restitution, migration, and Rac1 activation

2015 ◽  
Vol 308 (2) ◽  
pp. G92-G99 ◽  
Author(s):  
Jakob Benedict Seidelin ◽  
Sylvester Larsen ◽  
Dorte Linnemann ◽  
Ben Vainer ◽  
Mehmet Coskun ◽  
...  
Keyword(s):  
Wound Healing ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β ◽  
Human Colon ◽  
Inhibitor Of Apoptosis ◽  
Experimental Ulcer ◽  
Inhibitor Of Apoptosis Protein ◽  
Apoptosis Protein

Identification of pathways involved in wound healing is important for understanding the pathogenesis of various intestinal diseases. Cellular inhibitor of apoptosis protein 2 (cIAP2) regulates proliferation and migration in nonepithelial cells and is expressed in human colonocytes. The aim of the study was to investigate the role of cIAP2 for wound healing in the normal human colon. Wound tissue was generated by taking rectosigmoidal biopsies across an experimental ulcer in healthy subjects after 5, 24, and 48 h. In experimental ulcers, the expression of cIAP2 in regenerating intestinal epithelial cells (IECs) was increased at the wound edge after 24 h ( P < 0.05), returned to normal after reepithelialization, and correlated with the inflammatory reaction in the experimental wounds ( P < 0.001). cIAP2 was induced in vitro in regenerating Caco2 IECs after wound infliction ( P < 0.01). Knockdown of cIAP2 caused a substantial impairment of the IEC regeneration through inhibition of migration ( P < 0.005). cIAP2 overexpression lead to formation of migrating IECs and upregulation of expression of RhoA and Rac1 as well as GTP-activation of Rac1. Transforming growth factor-β1 enhanced the expression of cIAP2 but was not upregulated in wounds in vivo and in vitro. NF-κB and MAPK pathways did not affect cIAP2 expression. cIAP2 is in conclusion a regulator of human intestinal wound healing through enhanced migration along with activation of Rac1, and the findings suggest that cIAP2 could be a future therapeutic target to improve intestinal wound healing.

Vascular Endothelial Genes That Are Responsive to Tumor Necrosis Factor- In Vitro Are Expressed in Atherosclerotic Lesions, Including Inhibitor of Apoptosis Protein-1, Stannin, and Two Novel Genes

Blood ◽  
1999 ◽  
Vol 93 (10) ◽  
pp. 3418-3431 ◽  
Author(s):  
Anton J.G. Horrevoets ◽  
Ruud D. Fontijn ◽  
Anton Jan van Zonneveld ◽  
Carlie J.M. de Vries ◽  
Jan Wouter ten Cate ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Tumor Necrosis ◽  
Inhibitor Of Apoptosis ◽  
Vascular Endothelial ◽  
Inhibitor Of Apoptosis Protein ◽  
Atherosclerotic Lesions ◽  
Apoptosis Protein ◽  
Novel Transcripts ◽  
Necrosis Factor

Activation and dysfunction of endothelial cells play a prominent role in patho-physiological processes such as atherosclerosis. We describe the identification by differential display of 106 cytokine-responsive gene fragments from endothelial cells, activated by monocyte conditioned medium or tumor necrosis factor-. A minority of the fragments (22/106) represent known genes involved in various processes, including leukocyte trafficking, vesicular transport, cell cycle control, apoptosis, and cellular protection against oxidative stress. Full-length cDNA clones were obtained for five novel transcripts that were induced or repressed more than 10-fold in vitro. These novel human cDNAs CA2_1, CG12_1, GG10_2, AG8_1, and GG2_1 encode inhibitor of apoptosis protein-1 (hIAP-1), homologues of apolipoprotein-L, mouse rabkinesin-6, rat stannin, and a novel 188 amino acid protein, respectively. Expression of 4 novel transcripts is shown by in situ hybridization on healthy and atherosclerotic vascular tissue, using monocyte chemotactic protein-1 as a marker for inflammation. CA2_1 (hIAP-1) and AG8_1 are expressed by endothelial cells and macrophage foam cells of the inflamed vascular wall. CG12_1 (apolipoprotein-L like) was specifically expressed in endothelial cells lining the normal and atherosclerotic iliac artery and aorta. These results substantiate the complex change in the gene expression pattern of vascular endothelial cells, which accompanies the inflammatory reaction of atherosclerotic lesions.

scholarly journals Diablo Promotes Apoptosis by Removing Miha/Xiap from Processed Caspase 9

2001 ◽  
Vol 152 (3) ◽  
pp. 483-490 ◽  
Author(s):  
Paul G. Ekert ◽  
John Silke ◽  
Christine J. Hawkins ◽  
Anne M. Verhagen ◽  
David L. Vaux
Keyword(s):  
Cell Death ◽  
Cytochrome C ◽  
Caspase 3 ◽  
Direct Interaction ◽  
Inhibitor Of Apoptosis ◽  
Caspase 9 ◽  
Inhibitor Of Apoptosis Protein ◽  
Grim Reaper ◽  
Apoptosis Protein ◽  
Mammalian Protein

MIHA is an inhibitor of apoptosis protein (IAP) that can inhibit cell death by direct interaction with caspases, the effector proteases of apoptosis. DIABLO is a mammalian protein that can bind to IAPs and antagonize their antiapoptotic effect, a function analogous to that of the proapoptotic Drosophila molecules, Grim, Reaper, and HID. Here, we show that after UV radiation, MIHA prevented apoptosis by inhibiting caspase 9 and caspase 3 activation. Unlike Bcl-2, MIHA functioned after release of cytochrome c and DIABLO from the mitochondria and was able to bind to both processed caspase 9 and processed caspase 3 to prevent feedback activation of their zymogen forms. Once released into the cytosol, DIABLO bound to MIHA and disrupted its association with processed caspase 9, thereby allowing caspase 9 to activate caspase 3, resulting in apoptosis.

Sign in / Sign up

Export Citation Format

Share Document