The gene for neuronal apoptosis inhibitory protein is partially deleted in individuals with spinal muscular atrophy

Roy, Natalie; Mahadevan, Mani S.; McLean, Michael D.; Shutter, Gary; Yaraghi, Zahra; Farahani, Reza Masteri; Baird, Stephen; Besner-Johnston, Anne; Lefebvre, Charles; Kang, Xin; Salih, Maysoon; Aubry, Huguette L.; Tamai, Katsuyuki; Guan, Xiaoping; Ioannou, Panayiotis A.; Crawford, Thomas O.; Jong, Pieter J. de; Surh, Linda; Ikeda, Joh E.; Korneluk, Robert G.; MacKenzie, Alex

doi:10.1016/0092-8674(95)90461-1

Cited by 895 publications

(591 citation statements)

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“…56 Despite the absence of a CARD, the neuronal apoptosis inhibitor protein (NAIP) shares with IPAF the highest sequence similarity of the NACHT and LRR domains, suggesting that these molecules are evolutionary and functionally related. 57 Instead of a CARD, NAIP harbors three N-terminal baculovirus inhibitor-of-apoptosis repeats (BIR), 58 which were proposed to act as caspase inhibitors. 59 Mutations in NAIP are associated with the development of spinal muscular atrophy.…”

Section: Activation Of Inflammatory Caspases: Inflammasomes and Othermentioning

confidence: 99%

“…59 Mutations in NAIP are associated with the development of spinal muscular atrophy. 58 Mouse NAIP is mainly expressed in macrophages and is encoded by seven paralogous genes, naip1 to naip7. 60 NAIP was proposed to interact with IPAF indicating that it may be part of the same caspase-1 activating complex 61 (Figure 2).…”

Section: Activation Of Inflammatory Caspases: Inflammasomes and Othermentioning

confidence: 99%

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Inflammatory caspases and inflammasomes: master switches of inflammation

2006

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Fifteen years have passed since the cloning and characterization of the interleukin-1b-converting enzyme (ICE/caspase-1), the first identified member of a family of proteases currently known as caspases. Caspase-1 is the prototypical member of a subclass of caspases involved in cytokine maturation termed inflammatory caspases that also include caspase-4 caspase -5, caspase -11 and caspase -12. Efforts to elucidate the molecular mechanisms involved in the activation of these proteases have uncovered an important role for the NLR family members, NALPs, NAIP and IPAF. These proteins promote the assembly of multiprotein complexes termed inflammasomes, which are required for activation of inflammatory caspases. This article will review some evolutionary aspects, biochemical evidences and genetic studies, underlining the role of inflammasomes and inflammatory caspases in innate immunity against pathogens, autoinflammatory syndromes and in the biology of reproduction. Inflammatory CaspasesThe history of caspases began with the identification of an aspartate-specific protease activity involved in the conversion of the 31 kDa proIL-1b precursor to its active 17 kDa biologically active form, 1,2 and the identification of caspase-1 as the protease responsible for proIL-1b maturation. 3,4 The subsequent discovery of ced-3, that shares similarities with caspase-1 and which is involved in programmed cell death (PCD) in Caenorhabditis elegans, suggested that caspases might play fundamental roles in apoptosis. 5 As reviewed in the papers accompanying this issue of Cell Death and Differentiation, the role of apoptotic caspases in C. elegans and in vertebrates is crucial and deal with many facets of cell biology, development and diseases. In this review, we will focus on a subset of caspases present only in vertebrates and known as inflammatory caspases.Inflammatory caspases (also known as group I caspases) are encoded by three main genes in humans caspase-1, caspase-4 and caspase-5 and three main genes in mouse, caspase-1, caspase-11 and caspase-12. 6,7 In mammals, these caspases are characterized by the presence of a CARD domain at the N-terminus (Figure 1a). Human, chimp and mouse inflammatory caspases share significant similarity and are organized in a single locus (Figure 1c). Phylogenetic analysis of the conserved CARD domain suggests that the inflammatory caspases can be separated in evolutionaryrelated clusters (Figure 1b). The caspase-1 cluster contains caspase-1 and four other genes encoding decoy caspases: cop, inca1, inca2 and iceberg. These decoy caspase-1-like genes are absent in the mouse genome, suggesting that they have arisen recently by duplication of caspase-1. Although human and mouse caspase-1 are likely orthologues, sequence analysis suggests that human caspase-4 and caspase-5 have originated from a duplication of caspase-11. 7 However, the human caspase-12 gene, which in the chimp genome contains an SHG box important for it enzymatic activity, 8 evolved towards an enzymatically inactive form at some stage...

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Section: Activation Of Inflammatory Caspases: Inflammasomes and Othermentioning

confidence: 99%

Section: Activation Of Inflammatory Caspases: Inflammasomes and Othermentioning

confidence: 99%

Inflammatory caspases and inflammasomes: master switches of inflammation

2006

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“…It has also been reported that apoptosis may have a critical role in neuodegenerative diseases (Gschwind and Huber, 1995;Roy et al, 1995;Ham et al, 2000).…”

mentioning

confidence: 94%

Synthetic retinoids as inducers of apoptosis in ovarian carcinoma cell lines

Holmes¹,

Soprano²,

Soprano³

2004

Journal Cellular Physiology

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Apoptosis is also known as programmed cell death. Apoptosis plays an essential role in maintaining normal tissue and cell physiology in multicellular organisms. Clearance of aberrant or pre-cancerous cells occurs through the induction of apoptosis. It has been reported that many tumors and tumor cell lines have dysfunctional apoptosis signaling, causing these tumors to escape immune monitoring and internal cellular control mechanisms. One potential cause of this dysfunctional apoptosis is the tumor suppressor p53, an important regulator of growth arrest and apoptosis that is mutated in over 50% of all cancers. Retinoids have great potential in the areas of cancer therapy and chemoprevention. While some tumor cells are sensitive to the growth inhibitory effects of natural retinoids such as all-trans-retinoic acid (ATRA), many ovarian tumor cells are not. 6-[3-(1-Admantyl)]-4-hydroxyphenyl]-2-naphthalene carboxylic acid (CD437) and fenretinide N-[4-hydroxyphenyl] retinamide (4-HPR) are conformationally restricted synthetic retinoids that induce growth arrest and apoptosis in both ATRA-sensitive and ATRA-resistant ovarian tumor cell lines. Recently, we have identified the molecular pathways of apoptosis induced by treatment of ovarian carcinoma cells with mutated p53 by CD437 and 4-HPR.

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“…Human NAIP lies within a tract of four other genes that have undergone a 500-kb inverted duplication. The duplicated NAIP copy appears to be a pseudogene [17]. This duplication is specific to humans, while in other primates a pericentromeric inversion (chimpanzee and bonobo) and a translocation to Chromosome 19 (gorilla) have repositioned NAIP [18].…”

Section: Introductionmentioning

confidence: 94%

Repeated Recruitment of LTR Retrotransposons as Promoters by the Anti-apoptotic Locus NAIP During Mammalian Evolution

Romanish¹,

Lock²,

Lagemaat³

et al. 2005

PLoS Genet

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Neuronal apoptosis inhibitory protein (NAIP, also known as BIRC1) is a member of the conserved inhibitor of apoptosis protein (IAP) family. Lineage-specific rearrangements and expansions of this locus have yielded different copy numbers among primates and rodents, with human retaining a single functional copy and mouse possessing several copies, depending on the strain. Roles for this gene in disease have been documented, but little is known about transcriptional regulation of NAIP. We show here that NAIP has multiple promoters sharing no similarity between human and rodents. Moreover, we demonstrate that multiple, domesticated long terminal repeats (LTRs) of endogenous retroviral elements provide NAIP promoter function in human, mouse, and rat. In human, an LTR serves as a tissue-specific promoter, active primarily in testis. However, in rodents, our evidence indicates that an ancestral LTR common to all rodent genes is the major, constitutive promoter for these genes, and that a second LTR found in two of the mouse genes is a minor promoter. Thus, independently acquired LTRs have assumed regulatory roles for orthologous genes, a remarkable evolutionary scenario. We also demonstrate that 59 flanking regions of IAP family genes as a group, in both human and mouse are enriched for LTR insertions compared to average genes. We propose several potential explanations for these findings, including a hypothesis that recruitment of LTRs near NAIP or other IAP genes may represent a host-cell adaptation to modulate apoptotic responses.

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The gene for neuronal apoptosis inhibitory protein is partially deleted in individuals with spinal muscular atrophy

Cited by 895 publications

References 40 publications

Inflammatory caspases and inflammasomes: master switches of inflammation

Inflammatory caspases and inflammasomes: master switches of inflammation

Synthetic retinoids as inducers of apoptosis in ovarian carcinoma cell lines

Repeated Recruitment of LTR Retrotransposons as Promoters by the Anti-apoptotic Locus NAIP During Mammalian Evolution

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