Cloning and Characterization of the Bovine Fas

Yoo, Jakyoung; Stone, R. T.; Beattie, Craig W.

doi:10.1089/dna.1996.15.227

Cited by 18 publications

(14 citation statements)

References 42 publications

(54 reference statements)

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“…Specificity of this band was determined by preincubation of the antibody with an excess of its immunizing peptide that prevented antibody binding to the 60 kDa protein. The size of bovine Fas mRNA is similar to that of the human [43], and therefore, the protein is expected to be of similar size. Fas is believed to aggregate in trimeric proteins at the cell surface, but the observed 60 kDa product is not likely a result of aggregation, because this would lead to protein bands with a molecular mass of approximately 200 kDa [44].…”

Section: Discussionmentioning

confidence: 98%

Role of Fas-Mediated Apoptosis and Follicle-Stimulating Hormone on the Developmental Capacity of Bovine Cumulus Oocyte Complexes In Vitro1

Pomar¹,

Roelen²,

Slot³

et al. 2004

Biology of Reproduction

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Follicular atresia is believed to be largely regulated by apoptosis. To further understand how apoptosis can affect cumulus cells and oocytes we have evaluated the incidence and regulation of apoptosis affecting bovine cumulus oocyte complexes in vitro. Expression of components of the Fas signaling pathway was studied in both oocytes and cumulus cells by polymerase chain reaction after reverse transcription, immunoblotting, and indirect immunofluorescence. Furthermore, the Fas signaling pathway was activated in cumulus oocyte complexes with an agonistic anti-Fas antibody during in vitro maturation in the presence or absence of FSH. Viability and incidence of apoptosis in cumulus cells were evaluated by assessing membrane integrity and nuclear morphology. Oocyte nuclear maturation was also analyzed, as well as cleavage rates, blastocyst formation rates, and blastocyst quality, following in vitro fertilization. Fas mRNA and protein were expressed both in oocytes and cumulus cells. FasL protein was found in cumulus cells but could not be detected in oocytes, despite its mRNA expression. Both activation of the Fas pathway and presence of FSH during in vitro maturation increased the incidence of apoptosis in cumulus cells, affecting predominantly the middle and peripheral regions of the cumulus. The observed increase, however, had no effect on the developmental competence of the oocytes.

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Section: Discussionmentioning

confidence: 98%

Role of Fas-Mediated Apoptosis and Follicle-Stimulating Hormone on the Developmental Capacity of Bovine Cumulus Oocyte Complexes In Vitro1

Pomar¹,

Roelen²,

Slot³

et al. 2004

Biology of Reproduction

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“…. NLV-COOH in bovine (53). No interaction of the PDZ2 domain of PTPBL (the mouse equivalent of hPTP1E) was observed with the carboxyl terminus of mouse FAS (54).…”

Section: Zrp-1 a Novel Zyxin-related Lim Proteinmentioning

confidence: 94%

ZRP-1, a Zyxin-related Protein, Interacts with the Second PDZ Domain of the Cytosolic Protein Tyrosine Phosphatase hPTP1E

Murthy

Clark

Fortin

et al. 1999

Journal of Biological Chemistry

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Protein-protein interactions play an important role in the specificity of cellular signaling cascades. By using the yeast two-hybrid system, a specific interaction was identified between the second PDZ domain of the cytosolic protein tyrosine phosphatase hPTP1E and a novel protein, which was termed ZRP-1 to indicate its sequence similarity to the Zyxin protein family. The mRNA encoding this protein is distributed widely in human tissues and contains an open reading frame of 1428 base pairs, predicting a polypeptide of 476 amino acid residues. The deduced protein displays a prolinerich amino-terminal region and three double zinc finger LIM domains at its carboxyl terminus. The specific interaction of this novel protein with the second PDZ domain of hPTP1E was demonstrated both in vitro, using bacterially expressed proteins, and in vivo, by co-immunoprecipitation studies. Deletion analysis indicated that an intact carboxyl terminus is required for its interaction with the second PDZ domain of hPTP1E in the yeast two-hybrid system and suggested that other sequences, including the LIM domains, also participate in the interaction. The genomic organization of the ZRP-1 coding sequence is identical to that of the lipoma preferred partner gene, another Zyxin-related protein, suggesting that the two genes have evolved from a recent gene duplication event.Protein-protein interactions play a crucial role in maintaining the normal function of cells. Such interactions are important in the transmission of signals within the cell. Scaffolding, anchoring, and adaptor proteins, which bring together the various signaling molecules through such interactions, are determinant in fine-tuning these pathways and often contain modular structural domains mediating protein-protein interactions (1-3). A partial list of these domains include Src homology 2 and 3 (SH2 and SH3) domains (4), Tyr(P) binding domains (5), pleckstrin homology domain (6, 7), and PDZ domain (8, 9).PDZ domains consist of a motif of approximately 90 amino acid residues, found in one or multiple copies in a variety of signaling proteins. This domain derives its name from the three proteins originally shown to contain these sequences as follows: post-synaptic density protein, PSD-95 (10), the Drosophila septate junction protein discs-large tumor suppressor, Dlg (11), and the epithelial tight junction protein, ZO-1 (12). Other PDZ domain-containing proteins include nitric oxide synthase (13), the Drosophila dishevelled protein, Dsh (14), the channel-interacting PDZ domain protein (15), etc. (for reviews see Refs. 9 and 16).PDZ domains have also been found in a subfamily of protein tyrosine phosphatases (PTPs), 1 which includes PTPH1 (17), PTPMEG (18), and hPTP1E (19). The latter, also called PTP-BAS, PTPL1, and FAP-1, is a cytosolic PTPase and contains five PDZ domains in addition to a single tyrosine phosphatase catalytic domain. This protein also contains other distinct structural elements including a band 4.1 homology domain and five PEST regions (19 -22). A recent st...

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“…The molecular weights of well-known apoptosismediating receptors, Fas and TNFR1, are 45-46 and 65 kD, respectively [157][158][159], and the molecular weights of the granulosa cell surface antigens, PFG-5 a n d P F G -6 a n t i g e n s , a r e 5 5 a n d 4 2 k D , respectively. Fas was immunohistochemically detected in the granulosa cells and luteal cells of both healthy and atretic follicles in rodent ovaries and in the thymus, liver, heart and lung [52,98,142], but TNFR1 was not detected in ovarian follicles or luteal bodies [121].…”

Section: Novel Cell Death Receptor and Decoy Receptor Systemmentioning

confidence: 99%

Regulation Mechanism of Selective Atresia in Porcine Follicles: Regulation of Granulosa Cell Apoptosis during Atresia

Manabe

Goto

Matsuda‐Minehata

et al. 2004

Journal of Reproduction and Development

186

139

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Abstract. More than 99% of follicles undergo a degenerative process known as "atresia", in mammalian ovaries, and only a few follicles ovulate during ovarian follicular development. We have investigated the molecular mechanism of selective follicular atresia in mammalian ovaries, and have reported that follicular selection dominantly depends on granulosa cell apoptosis. However, we have little knowledge of the molecular mechanisms that control apoptotic cell death in granulosa cells during follicle selection. To date, at least five cell death ligand-receptor systems [tumor necrosis factor (TNF)α and receptors, Fas (also called APO-1/CD95) ligand and receptors, TNF-related apoptosisinducing ligand (TRAIL; also called APO-2) and receptors, APO-3 ligand and receptors, and PFG-5 ligand and receptors] have been reported in granulosa cells of porcine ovaries. Some cell death ligand-receptor systems have "decoy" receptors, which act as inhibitors of cell death ligand-induced apoptosis in granulosa cells. Moreover, we showed that the porcine granulosa cell is a type II apoptotic cell, which has the mitochondrion-dependent apoptosis-signaling pathway. Briefly, the cell death receptor-mediated apoptosis signaling pathway in granulosa cells has been suggested to be as follows. (1) (7) Cytochrome c and ATP-dependent oligimerization of apoptotic protease-activating factor-1 (Apaf-1) allows recruitment of procaspase-9 into the apoptosome complex. Activation of procaspase-9 is mediated by means of a conformational change. (8) The activated caspase-9 cleaves downstream effector caspases (caspase-3). (9) Finally, apoptosis is induced. Recently, we found two intracellular inhibitor proteins [cellular FLICE-like inhibitory protein short form (cFLIPS) and long form (cFLIPL)], which were strongly expressed in granulosa cells, and they may act as anti-apoptotic/survival factors. Further in vivo and in vitro studies will elucidate the largely unknown molecular mechanisms, e. g.

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Cloning and Characterization of the Bovine Fas

Cited by 18 publications

References 42 publications

Role of Fas-Mediated Apoptosis and Follicle-Stimulating Hormone on the Developmental Capacity of Bovine Cumulus Oocyte Complexes In Vitro1

Role of Fas-Mediated Apoptosis and Follicle-Stimulating Hormone on the Developmental Capacity of Bovine Cumulus Oocyte Complexes In Vitro1

ZRP-1, a Zyxin-related Protein, Interacts with the Second PDZ Domain of the Cytosolic Protein Tyrosine Phosphatase hPTP1E

Regulation Mechanism of Selective Atresia in Porcine Follicles: Regulation of Granulosa Cell Apoptosis during Atresia

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