A human homologue of mouse Mater, a maternal effect gene essential for early embryonic development

Tong, Zhi-Bin; Bondy, Carolyn A.; Zhou, Jiang; Nelson, Lawrence M.

doi:10.1093/humrep/17.4.903

Cited by 95 publications

(45 citation statements)

References 35 publications

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“…This expression pattern is largely consistent with a role for POP2 in regulating CLR-dependent events in immune cells. CLR proteins also play a role in embryogenesis as illustrated by MATER, a nonpyrin CLR family member required for cell division in fertilized eggs (43,44). Likewise, mouse NALP14 is also believed to have developmental function (45).…”

Section: Discussionmentioning

confidence: 99%

Pyrin-Only Protein 2 Modulates NF-κB and Disrupts ASC:CLR Interactions

Bedoya

Sandler

Harton

2007

The Journal of Immunology

147

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NF-κB is pivotal for transactivation of cell-cycle regulatory, cytokine, and adhesion molecule genes and is dysregulated in many cancers, neurodegenerative disorders, and inflammatory diseases. Proteins with pyrin and/or caspase recruitment domains have roles in apoptosis, innate immunity, and inflammation. Many pyrin domain (PYD) proteins modulate NF-κB activity as well as participate in assembling both the perinuclear “apoptotic speck” and the pro-IL1β/IL-18-converting inflammasome complex. “Pyrin-only” proteins (POP) are attractive as negative regulators of PYD-mediated functions and one such protein, POP1, has been reported. We report the identification and initial characterization of a second POP. POP2 is a 294 nt single exon gene located on human chromosome 3 encoding a 97-aa protein with sequence and predicted structural similarity to other PYDs. Highly similar to PYDs in CATERPILLER (CLR, NLR, NALP) family proteins, POP2 is less like the prototypic pyrin and ASC PYDs. POP2 is expressed principally in peripheral blood leukocytes and displays both cytoplasmic and nuclear expression patterns in transfected cells. TNF-α-stimulated and p65 (RelA)-induced NF-κB-dependent gene transcription is inhibited by POP2 in vitro by a mechanism involving changes in NF-κB nuclear import or distribution. While colocalizing with ASC in perinuclear specks, POP2 also inhibits the formation of specks by the CLR protein CIAS1/NALP3. Together, these observations demonstrate that POP2 is a negative regulator of NF-κB activity that may influence the assembly of PYD-dependent complexes.

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Section: Discussionmentioning

confidence: 99%

Pyrin-Only Protein 2 Modulates NF-κB and Disrupts ASC:CLR Interactions

Bedoya

Sandler

Harton

2007

The Journal of Immunology

147

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“…NALP5 (also known under the name of MATER) displays oocyterestricted basal expression in mouse and human. 105,106 NALP5-deficient female mice are sterile because of an arrest in the development of the embryos at the two-cell stage. 105 Other NALPs such as the mouse NALP4 and NALP9 paralogues, NALP4a (also termed NALP9d, see Table 1), NALP4b, NALP4c, NALP4f, NALP9b, NALP9c and bovine NALP5 appear to be expressed exclusively in the ovary whereas mouse NALP9a, NALP14 and bovine NALP9 and NALP8 seem to be essentially expressed both in the ovary and the testis.…”

Section: Intracellular Flagellin: Detection By the Nlr Proteins Naip mentioning

confidence: 99%

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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“…These oocyte specific genes, stored in the growing oocyte, are involved in the regulation of early cleavage, and their knockout often results in the inability of the embryo to develop beyond the first cleavage. Zar1, MATER, NPM2, are among the MEG that were later seen to be conserved in all the studied mammalian species, as bovine (Pennetier et al, 2004;Thelie et al, 2007;Uzbekova et al, 2006), human (Tong et al, 2002;Uzbekova et al, 2006;Wu et al, 2003b), swine and sheep .…”

Section: Animal Models: Peculiarities and Advantages Of Different Mammentioning

confidence: 96%

Safety in Assisted Reproductive Technologies: Insights from Gene Expression Studies During Preimplantation Development

Bebbere¹,

Bogliolo²,

Ariu³

et al. 2012

In Vitro Fertilization - Innovative Clinical and Laboratory Aspects

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A human homologue of mouse Mater, a maternal effect gene essential for early embryonic development

Abstract: The human MATER and mouse Mater genes and proteins are conserved. Characterization of the human MATER and its protein provides a basis for investigating their clinical implications in autoimmune premature ovarian failure and infertility in women.

Cited by 95 publications

References 35 publications

Pyrin-Only Protein 2 Modulates NF-κB and Disrupts ASC:CLR Interactions

Pyrin-Only Protein 2 Modulates NF-κB and Disrupts ASC:CLR Interactions

Inflammatory caspases and inflammasomes: master switches of inflammation

Safety in Assisted Reproductive Technologies: Insights from Gene Expression Studies During Preimplantation Development

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