DEVELOPMENTAL EXPRESSION OF Ca++/Mg++-DEPENDENT ENDONUCLEASE ACTIVITY IN RAT GRANULOSA AND LUTEAL CELLS

Zeleznik, Anthony J.; Ihrig, Lynda; Bassett, Steven G.

doi:10.1210/endo-125-4-2218

Cited by 131 publications

(48 citation statements)

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“…63 Another physiological process in which apoptosis has been implicated is regression of the Corpus luteum (CL). 64 CL is an organ within the ovary which differentiates from the ruptured follicle following ovulation. The main function of the CL is secretion of progesterone to maintain the lining of the uterus for implantation and support of a fertilized ovum.…”

Section: Induction Of Apoptosismentioning

confidence: 99%

Physiological apoptosis in hormone-dependent tissues: involvement of caspases

et al. 1999

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Physiological apoptosis in mammals is a type of programmed cell death, an important element in the developmental repertoire ensuring tissue homeostasis and proper disposal of cells that are no longer needed, such as milk-producing epithelial cells in the mammary gland after lactation, luteal cells in the post partum Corpus luteum or secretory cells in the prostate after castration. Although incompletely described, apoptosis in hormone-dependent tissues is apparently initiated and executed using common biochemical strategies. These include survival pathways governed by local and systemic factors and hormones, diverse regulatory pathways and caspase-dependent execution pathways. Using an antibody that recognizes processed effector caspases or a fluorogenic caspase substrate, we present for the first time evidence that caspases are activated in the mammary gland, in the prostate and in the ovary at the time when apoptosis occurs. Most likely phagocytosis of apoptotic cells by neighboring cells may represent an important step, since only a modest involvement of professional phagocytes is apparent. Here, we will summarize and discuss recent data and will attempt to draw a generalized picture of how physiological apoptosis may occur in these organs.

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Section: Induction Of Apoptosismentioning

confidence: 99%

Physiological apoptosis in hormone-dependent tissues: involvement of caspases

et al. 1999

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“…In mammalian ovaries, more than 99% of follicles degenerate without ovulation, and follicular granulosa cell apoptosis plays a critical role in this process [14][15][16][17]. 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].…”

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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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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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“…The mechanism of intracellular apoptosis of the ovary by GnRH has been postulated to be induced by the pathway of protein kinase C through GnRH, thus increasing the amount of intracellular calcium and changing phosphatidylinositol (26,27). Recently, when the GnRH, buserelin, was given to white rats, it was reported to decrease the expression of inducible nitric oxide synthase (iNOS) mRNA and promote cytostasis in ovarian follicular development (28).…”

Section: Discussionmentioning

confidence: 99%