Regulatory Mechanisms of Granulosa Cell Apoptosis in Ovarian Follicle Atresia

Manabe, Noboru; Kimura, Yuichi; Uchio, Kozue; Tajima, Chiemi; Matsushita, Hiroko; Nakayama, Mizuho; Sugimoto, Mitsuhiro; Miyamoto, Hajime

doi:10.1007/0-306-46869-7_60

Cited by 22 publications

(55 citation statements)

References 14 publications

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“…Overexpression of pFADD and pprocaspase-8 induced cell death in the HeLa-K cells. To date, we have investigated the follicular atretic mechanisms of follicular atresia in porcine ovaries [18][19][20][21][22][26][27][28][29][30][31] and have shown that g r a n u l o s a c e l l a p o p t o s i s i s a d o m i n a n t phenomenon in follicular atresia. Therefore, we examined whether overexpressed pFADD and pprocaspase-8 can induce apoptosis in the granulosa cells of human, murine, and porcine origin (KGN, KK1 and JC410, respectively).…”

Section: Apoptosis Inductivitymentioning

confidence: 99%

“…Cell death ligand and receptor systems [such as the Fas ligand (FasL)/Fas system and TNF relating apoptosis inducing ligand (TRAIL)/TRAIL-receptor system] mediate apoptosis during follicular aresia in porcine ovaries [18][19][20][21][22][23][24][25][26][27]. In porcine granulosa cells, apoptosis is regulated by a cell death ligand and receptor system, TRAIL/TRAIL-R, as follows [22].…”

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confidence: 99%

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Molecular Characteristics of Porcine Fas-associated Death Domain (FADD) and Procaspase-8

Inoue

Matsuda‐Minehata

Goto

et al. 2007

Journal of Reproduction and Development

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Abstract. To reveal the intracellular signal transduction molecules involved in granulosa cell apoptosis in porcine ovarian follicles, we cloned the porcine Fas-associated death domain (FADD), an adaptor protein for the cell death receptor, and procaspase-8, an initiator caspase. Porcine FADD (pFADD) was 636 bp (211 amino acids: aa) long and showed 74.0 and 65.4% homology with human and murine FADD, respectively. Porcine procaspase-8 (pprocaspase-8) was 1,431 bp (476 aa) long and 70.6 and 63.4% homologous with human and murine procaspase-8, respectively. To confirm the apoptosis-inducing abilities, we constructed pFADD and pprocaspase-8 cDNA expression vectors with enhanced green fluorescence protein (EGFP) and then transfected them into human uterine cervix tumor (HeLa-K), human granulosa cell-derived (KGN), murine granulosa-derived tumor (KK1), and porcine granulosa cell-derived (JC410) cells. When pFADD and pprocaspase-8 were overexpressed, cell death was induced in these transfected cells. However when caspase-inhibitor p35 was cotransfected, cell death was inhibited. The pFADD and pprocaspase-8 genes are well conserved, as are the physiological functions of their products. Key words: Apoptosis, Caspase-8, Fas-associated death domain (FADD), Granulosa cell, Porcine ovary (J. Reprod. Dev. 53: [427][428][429][430][431][432][433][434][435][436] 2007) poptosis is an important phenomenon involved i n c e l l s u r v i v a l a n d / o r d e a t h d u r i n g differentiation and development [1,2]. The death ligand and receptor systems are considered to be apoptosis-inducing factors [3][4][5][6][7]. Death receptors, which belong to the tumor necrosis factor (TNF) receptor family, are membrane-binding proteins with a death domain (DD) in their intracellular regions. An adaptor protein, such as Fasassociating death domain protein (FADD), which has a DD in the C-terminal region and a death effector domain (DED) in the N-terminal region, is recruited when each specific ligand binds to its r e c e p t o r [ 8 -1 0 ] . T h e n , F A D D b i n d s w i t h procaspase-8 (also called FLICE), which has two DEDs in the N-teminal region [11,12]. These molecules compose the death-inducing signaling complex (DISC). As a result of the proteolytic autoactivation of procaspase-8 [13], subunit protein 18 (p18) and 11 (p11) are released into the cytoplasm and reform a proteolytic component that c l e a v e s m a n y s u b s t r a t e p r o t e i n s , s u c h a s

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Section: Apoptosis Inductivitymentioning

confidence: 99%

mentioning

confidence: 99%

Molecular Characteristics of Porcine Fas-associated Death Domain (FADD) and Procaspase-8

Inoue

Matsuda‐Minehata

Goto

et al. 2007

Journal of Reproduction and Development

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“…Ovarian sections were stained by the TUNEL method using a commercial kit (Apop Tag; Intergen, Purchase, NY, USA) according to a modification of the method reported previously [6][7][8][9][10] to allow visualization of the apoptotic cells. Briefly, the sections were fixed in 10% neutralbuffered formalin (pH.…”

Section: Histochemistrymentioning

confidence: 99%

“…Recent findings have suggested that apoptosis, originally described by Kerr et al [5], is the mechanism underlying ovarian follicular atresia. Ovarian follicular atresia is affected by various factors such as steroids, gonadotrophins and cytokines, but the mechanism that regulates follicle selection during follicular development is not well understood [6][7][8]. Our previous studies of follicular atresia in porcine ovaries demonstrated that degeneration of the atretic follicles can be explained partly by apoptosis of granulosa cells [9,10].…”

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confidence: 99%

“…In the present study, the expression of classic cadherins and β-catenin, which is associated with the membrane-anchored cytoplasmic domain of classic cadherins [13], in developing and/or atretic follicles of porcine ovaries was investigated by immunocytochemical analysis. The principal aims were: first, to determine what types of cadherins are expressed in porcine follicles; second, to investigate the pattern of expression in follicles during follicular atresia, especially in granulosa cells, apoptotic cell death of which is considered to be a key phenomenon in follicular atresia and which contributes to determination of the follicle population in each estrous cycle [6][7][8][9][10]; and third, to determine whether there are any differences in expression of cadherins in differentiating follicular cells.…”

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Changes in Cell Adhesion Molecules during Follicular Atresia in Porcine Ovaries.

Nishihara

Manabe

Nakayama

et al. 2000

Journal of Reproduction and Development

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Abstract. Determination of the expression level and localization of cell adhesion molecules is crucial for understanding the mechanism of maintenance and remodeling of the ovarian follicle structure. We immunocytochemically investigated expression of the cell adhesion molecules, "classic" cadherins and β-catenin, in developing and/or atretic follicles of porcine ovaries. Healthy follicles showed strong staining for cadherin-8 and β-catenin in granulosa cells tightly attached to the basement membrane, and moderate/weak staining was seen on the inner surface of the granulosa cell layer. Strong VE-cadherin expression was seen in a single cell layer attached to the basement membrane in the theca interna layer of healthy follicles. The expression of cadherin-8, β-catenin and VE-cadherin decreased during follicular atresia. No positive staining was observed for R-cadherin, E-cadherin, Tcadherin, BR-cadherin or P-cadherin, and a weak positive reaction for N-cadherin was seen only in the granulosa cells of healthy and early atretic follicles. These findings indicate that cadherin-8, Ncadherin and VE-cadherin have important roles in follicular development and/or degeneration, and that decreases in the expression of these cadherins are involved in follicular atresia in porcine follicles.

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et al. 2000

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Previously, we prepared an IgM monoclonal antibody(PFG-1) which specifically recognized a cell-membraneglycoprotein (PFG-1 antigen; 55 kD, pI 5.9),immunohistochemically reacted with granulosa cells ofhealthy follicles but not of atretic follicles, andinduced granulosa cell apoptosis. In the presentstudy, an IgM monoclonal antibody (PFG-3) capable ofinducing granulosa cell apoptosis and an IgGmonoclonal antibody (PFG-4) not capable of inducingapoptosis were produced against granulosa cellsprepared from healthy antral follicles of porcineovaries. Two-dimensional Western blotting analysisrevealed that PFG-3 specifically recognized twocell-membrane proteins (named PFG-3-1 andPFG-3-2/PFG-1 antigens; 42 kD, pI 5.2 and 55 kD, pI5.9, respectively) of healthy granulosa cells, andthat PFG-4 recognized the same two cell-membraneproteins. In atretic granulosa cells, PFG-3-2/PFG-1antigen disappeared. Immunochemical reactions of theseantibodies were only detected in follicular granulosacells but not any other ovarian tissues or organs.PFG-3 and PFG-4 immunohistochemically reacted withgranulosa cells of healthy and atretic follicles. Whenthe isolated granulosa cells prepared from healthyfollicles were cultured in medium containing PFG-3,the cells underwent apoptosis, and co-incubation withPFG-4 inhibited PFG-3-inducible apoptosis. Theseobservations suggested that PFG-3-2/PFG-1 antigen isa novel cell death receptor which is different fromthe apoptosis-mediating receptors (Fas/Apo-1/CD95 orTNF receptor), and that PFG-3-1 antigen may act as adecoy receptor and inhibit apoptotic signal transmission.

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Regulatory Mechanisms of Granulosa Cell Apoptosis in Ovarian Follicle Atresia

Cited by 22 publications

References 14 publications

Molecular Characteristics of Porcine Fas-associated Death Domain (FADD) and Procaspase-8

Molecular Characteristics of Porcine Fas-associated Death Domain (FADD) and Procaspase-8

Changes in Cell Adhesion Molecules during Follicular Atresia in Porcine Ovaries.

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