Caspase 8 and menin expressions are not correlated in human parathyroid tumors

Yu, Dong; Nagamura, Yuko; Shimazu, Satoko; Naito, Junko; Kaji, Hiroshi; Wada, Seiki; Honda, Munehiro; Xue, Ling; Tsukada, Toshihiko

doi:10.1507/endocrj.k10e-085

Cited by 2 publications

(3 citation statements)

References 21 publications

(30 reference statements)

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“…Given the clinical relevance of menin deficiency in pNEN, menin protein expression was analyzed in two pNEN cell lines BON1 and QGP1 and compared with HEK293T 36 , 37 , 38 , 39 and HeLa cells 40 that are known to express high menin protein levels (please refer to Figure 2A ). Having proven significant menin expression, MEN1 ‐knockout CRISPR/Cas9 pNEN cell lines (MEN1‐KO) were established for further investigations.…”

Section: Resultsmentioning

confidence: 99%

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The link between menin and pleiotrophin in the tumor biology of pancreatic neuroendocrine neoplasms

Boulant

Stanifer

et al. 2022

Cancer Science

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MEN1, which encodes menin protein, is the most frequently mutated gene in pancreatic neuroendocrine neoplasms (pNEN). Pleiotrophin (PTN) has been reported as a downstream factor of menin that promotes metastasis in different tumor entities. In this study, the effect of menin and its link to PTN were assessed using features of pNEN cells and the outcome of patients with pNEN. The expression levels of menin and PTN in tissues from patients with pNEN were examined using qRT‐PCR and western blot and compared with their metastasis status. Functional assays, including transwell migration/invasion and scratch wound‐healing assays, were performed on specifically designed CRISPR/Cas9‐mediated MEN1‐knockout (MEN1‐KO) pNEN cell lines (BON1MEN1‐KO and QGP1MEN1‐KO) to study the metastasis of pNEN. Among 30 patients with menin‐negative pNEN, 21 revealed a strong protein expression of PTN. This combination was associated with metastasis and shorter disease‐free survival. Accordingly, in BON1MEN1‐KO and QGP1MEN1‐KO cells, PTN protein expression was positively associated with enhanced cell migration and invasion, which could be reversed using PTN silencing. PTN is a predicting factor of metastatic behavior of menin‐deficient‐pNEN. In vitro, menin is able to both promote and suppress the metastasis of pNEN by regulating PTN expression depending on the tumoral origin of pNEN cells.

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Section: Resultsmentioning

confidence: 99%

“… Design of CRISPR/Cas9 MEN1 ‐knockout in BON1 and QGP1 cells. (A) HEK293T cells 40 and HeLa cells 36 , 37 , 38 , 39 are used as a menin‐positive control. All lines HEK293T, HeLa, QGP1 and BON1 showed high menin and PTN protein expression.…”

Section: Resultsmentioning

confidence: 99%

The link between menin and pleiotrophin in the tumor biology of pancreatic neuroendocrine neoplasms

Boulant

Stanifer

et al. 2022

Cancer Science

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“…Caspase-3 is responsible either wholly or in part for the proteolytic cleavage of many key proteins, including poly(ADP-ribose) polymerase and lamin A (12)(13)(14). The existence of another apoptosis pathway derives from the observation that caspase-8 is activated when challenged with tissue necrosis factor (TNF-␣) or Fas ligand (15)(16)(17)(18). Loss of caspase activity is observed in cells that express the viral proteins CrmA, from cowpox, and p35, from baculovirus (19 -23).…”

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confidence: 99%

Inhibitor of Apoptosis (IAP)-like Protein Lacks a Baculovirus IAP Repeat (BIR) Domain and Attenuates Cell Death in Plant and Animal Systems

Kim

Lee

Jung

et al. 2011

Journal of Biological Chemistry

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A novel Arabidopsis thaliana inhibitor of apoptosis was identified by sequence homology to other known inhibitor of apoptosis (IAP) proteins. Arabidopsis IAP-like protein (AtILP) contained a C-terminal RING finger domain but lacked a baculovirus IAP repeat (BIR) domain, which is essential for antiapoptotic activity in other IAP family members. The expression of AtILP in HeLa cells conferred resistance against tumor necrosis factor (TNF)-␣/ActD-induced apoptosis through the inactivation of caspase activity. In contrast to the C-terminal RING domain of AtILP, which did not inhibit the activity of caspase-3, the N-terminal region, despite displaying no homology to known BIR domains, potently inhibited the activity of caspase-3 in vitro and blocked TNF-␣/ActD-induced apoptosis. The antiapoptotic activity of the AtILP N-terminal domain observed in plants was reproduced in an animal system. Transgenic Arabidopsis lines overexpressing AtILP exhibited anti-apoptotic activity when challenged with the fungal toxin fumonisin B1, an agent that induces apoptosis-like cell death in plants. In AtIPL transgenic plants, suppression of cell death was accompanied by inhibition of caspase activation and DNA fragmentation. Overexpression of AtILP also attenuated effector protein-induced cell death and increased the growth of an avirulent bacterial pathogen. The current results demonstrated the existence of a novel plant IAP-like protein that prevents caspase activation in Arabidopsis and showed that a plant anti-apoptosis gene functions similarly in plant and animal systems.All living organisms use a process of cell suicide to achieve and maintain homeostasis during normal development as well as in response to environmental stress or during pathogen challenge (1). This functionally conserved process, known as programmed cell death (PCD) 5 or apoptosis, is genetically regulated and associated with distinct morphological and biochemical characteristics. Extensive study over the past decade has illuminated the biological and molecular mechanisms of the regulation of apoptosis in animal systems (2-7). Apoptosis is triggered by the sequential activation of cysteine proteases known as caspases, which results in protein cleavage and the breakdown of DNA molecules. This apoptotic cascade is regulated by both initiators and inhibitors and can be activated by diverse stimuli. Caspases are synthesized as zymogens that are activated by proteolytic cleavage at specific aspartic acid residues in the P1 position (8). Compartmentalization of caspases and their cofactors suggests that two major apoptotic pathways exist. One pathway of apoptosis, observed in animal systems, can be induced by the deprivation of serum from tissue culture cells, leading to the release of cytochrome c from mitochondria. Apoptosis activating factor-1 (Apaf1) and cytochrome c form a complex with procaspase-9, which is then activated. Active caspase-9 triggers the common caspase cascade by cleaving procaspase-3 (9 -11). Caspase-3 is responsible either wholly or in part fo...

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Caspase 8 and menin expressions are not correlated in human parathyroid tumors

Cited by 2 publications

References 21 publications

The link between menin and pleiotrophin in the tumor biology of pancreatic neuroendocrine neoplasms

The link between menin and pleiotrophin in the tumor biology of pancreatic neuroendocrine neoplasms

Inhibitor of Apoptosis (IAP)-like Protein Lacks a Baculovirus IAP Repeat (BIR) Domain and Attenuates Cell Death in Plant and Animal Systems

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