Subcellular distribution of glycosylphosphatidylinositol-specific phospholipase D in rat liver

Hari, Thomas; Kunze, H.; Bohn, Ernst; Brodbeck, Urs; Bütikofer, Peter

doi:10.1042/bj3200315

Cited by 26 publications

(7 citation statements)

References 37 publications

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“…The endosome becomes increasingly acidic20 and fuses with a lysosome21. In the lysosome FA is released22 and lysosomal GPI-specific phospholipase D23 cleaves off the GPI anchor on FRα, which is then set free. Free FRα translocates into the nucleus where it binds to cis -regulatory elements of target genes and directly activates transcription.…”

Section: Discussionmentioning

confidence: 99%

Nuclear localization of folate receptor alpha: a new role as a transcription factor

Boshnjaku

Shim

Tsurubuchi

et al. 2012

Sci Rep

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Folic acid (FA) has traditionally been associated with prevention of neural tube defects; more recent work suggests that it may also be involved in in the prevention of adult onset diseases. As the role of FA in human health and disease expands, it also becomes more critical to understand the mechanisms behind FA action. In this work we examined the hypothesis that folate receptor alpha (FRα) acts as a transcription factor. FRα is a GPI-anchored protein and a component of the caveolae fraction. The work described here shows that FRα translocates to the nucleus, where it binds to cis-regulatory elements at promoter regions of Fgfr4 and Hes1, and regulates their expression. The FRα recognition domain mapped to AT rich regions on the promoters. Until this time FRα has only been considered as a folate transporter, these studies describe a novel role for FRα as a transcription factor.

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Section: Discussionmentioning

confidence: 99%

Nuclear localization of folate receptor alpha: a new role as a transcription factor

Boshnjaku

Shim

Tsurubuchi

et al. 2012

Sci Rep

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“…This study is the first study to suggest that endogenous GPI-PLD plays a role in the release of this antigen from colorectal carcinoma cells. The exact GPI-PLD cell location and the GPI-anchor cutting location that is either cell-level or intracellular is still unknown [29,37,38]. Therefore, CEA is either free from cell surface or intracellular, and is unclear.…”

Section: Resultsmentioning

confidence: 99%

Identification of carcinoma embryonic antigen release mechanism Carcinoembryonic Antigen (CEA) from the surface of colorectal cancer cells

Asadi¹,

M²,

Mohammadzadeh³

2017

Res Rev Insights

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Background and aim: Carcinoembryonic antigen (CEA) carcinoembryonic antigen is one of the tumor markers that is expressed in many colorectal, stomach, pancreatic, lung and chest cancers. The exact mechanism for releasing this antigen from the cell surface to the cancer patients is still unknown. Carcinoma-embryonic antigen proteins are bound to a cell membrane through a glycosyl-phosphate tidal inositol (GPI-anchor) linkage. There is evidence that specific phospholipase enzymes interfere with the breakdown of GPI binding and the removal of CEA from the cell surface. Considering these evidence and data, we investigated the probable role of glycosyl phosphatidyl inositol phospholipase (GPI-PLD) D in hydrolysis and the release of carcinoma amniobiline antigens. Materials and methods: In this study, we demonstrated the expression of GPI-PLD in some cell lines of adenocarcinoma of colorectal using RT-PCR. The level of carcinogenic amniotic antinase released by one of the cancer cell lines (LS-180), which freely releases large amounts of carcinoma ambrionic antigen in the culture medium, was detected in the presence and absence of specific inhibitors and activators of this enzyme.

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“…GPI-PLD activity is abundant in serum, cerebrospinal fluid (40)(41)(42), and synovial fluid and is secreted by activated neutrophils (43). The activity has also been described as enriched in lysosomal fractions of bovine liver (44). GPI-PLD is taken up into cells from culture medium and proteolyzed to smaller fragments, a process that is inhibited by the lysosomotropic agent chloroquine (45), which raises the possibility of lysosomal targeting.…”

Section: Glycosylphosphatidylinositol-anchored and N-myristoylated Prmentioning

confidence: 99%

Thematic review series: Lipid Posttranslational Modifications. Lysosomal metabolism of lipid-modified proteins

Hofmann

2006

Journal of Lipid Research

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Much is now understood concerning the synthesis of prenylated and palmitoylated proteins, but what is known of their metabolic fate? This review details metabolic pathways for the lysosomal degradation of S-fatty acylated and prenylated proteins. Central to these pathways are two lysosomal enzymes, palmitoyl-protein thioesterase (PPT1) and prenylcysteine lyase (PCL). PPT1 is a soluble lipase that cleaves fatty acids from cysteine residues in proteins during lysosomal protein degradation. Notably, deficiency in the enzyme causes a neurodegenerative lysosomal storage disorder, infantile neuronal ceroid lipofuscinosis. PCL is a membrane-associated flavin-containing lysosomal monooxygenase that metabolizes prenylcysteine to prenyl aldehyde through a completely novel mechanism.The eventual metabolic fates of other lipidated proteins (such as glycosylphosphatidylinositol-anchored and N-myristoylated proteins) are poorly understood, suggesting directions for future research.

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Subcellular distribution of glycosylphosphatidylinositol-specific phospholipase D in rat liver

Cited by 26 publications

References 37 publications

Nuclear localization of folate receptor alpha: a new role as a transcription factor

Nuclear localization of folate receptor alpha: a new role as a transcription factor

Identification of carcinoma embryonic antigen release mechanism Carcinoembryonic Antigen (CEA) from the surface of colorectal cancer cells

Thematic review series: Lipid Posttranslational Modifications. Lysosomal metabolism of lipid-modified proteins

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