Elevated expression of PDI family proteins during differentiation of mouse F9 teratocarcinoma cells

Miyaishi, Osamu; Kozaki, Ken Ichi; Iida, Ken Ichi; Isobe, K; Hashizume, Yoshio; Saga, Shinsuke

doi:10.1002/(sici)1097-4644(19980315)68:4<436::aid-jcb4>3.0.co;2-r

Cited by 21 publications

(12 citation statements)

References 45 publications

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“…Another example of a protein that we identified that may also have a significant role in α7 nAChR-related nervous system development is protein disulfide-isomerase A3, which is a member of an enzyme family that catalyzes the rearrangement of disulfide bonds in proteins 80. Although we present the first evidence that this enzyme may interact with the disulfide-bind containing α7 nAChR, there are reports in the literature of the function of protein disulfide-isomerases in developmental regulation 81–83. These proteins, and others that we have identified, may have developmentally regulated roles for the localization and/or folding α7 nAChR.…”

Section: Discussionmentioning

confidence: 77%

Proteomic Analysis of an α7 Nicotinic Acetylcholine Receptor Interactome

2009

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The α7 nicotinic acetylcholine receptor (nAChR) is well established as the principal high-affinity α-bungarotoxin-binding protein in the mammalian brain. We isolated carbachol-sensitive α-bungarotoxin-binding complexes from total mouse brain tissue by affinity immobilization followed by selective elution, and these proteins were fractionated by SDS-PAGE. The proteins in subdivided gel lane segments were tryptically digested, and the resulting peptides were analyzed by standard mass spectrometry. We identified 55 proteins in wild-type samples that were not present in comparable brain samples from α7 nAChR knockout mice that had been processed in a parallel fashion. Many of these 55 proteins are novel proteomic candidates for interaction partners of the α7 nAChR, and many are associated with multiple signaling pathways that may be implicated in α7 function in the central nervous system. The newly identified potential protein interactions, together with the general methodology that we introduce for α-bungarotoxin-binding protein complexes, form a new platform for many interesting follow-up studies aimed at elucidating the physiological role of neuronal α7 nAChRs.

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Section: Discussionmentioning

confidence: 77%

Proteomic Analysis of an α7 Nicotinic Acetylcholine Receptor Interactome

2009

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“…However, this method may only catch a small fraction of the natural ERp57 substrates, and it should be noted that these results do not mean that these proteins are exclusively substrates for ERp57. For example, laminin β‐1 and γ‐1 have previously been shown to coimmunoprecipitate equally well with ERp57, ERp72, and PDI [96]. Although it is an extremely interesting and powerful technique that has allowed a unique insight into ERp57 function in vivo , there are several potential limitations with the use of the C‐terminal active site cysteine mutants in determining substrate specificity even after excluding possible problems of the mutation altering the specificity of the enzyme.…”

Section: Pdi Substrate Interactions Without Crosslinkersmentioning

confidence: 99%

Substrate recognition by the protein disulfide isomerases

2007

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Protein folding in the endoplasmic reticulum is often associated with the formation of native disulfide bonds. Their primary function is to stabilize the folded structure of the protein, although disulfide bond formation can also play a regulatory role. Native disulfide bond formation is not trivial, so it is often the rate‐limiting step of protein folding both in vivo and in vitro. Complex coordinated systems of molecular chaperones and protein folding catalysts have evolved to help proteins attain their correct folded conformation. This includes a family of enzymes involved in catalyzing thiol–disulfide exchange in the endoplasmic reticulum, the protein disulfide isomerase (PDI) family. There are now 17 reported PDI family members in the endoplasmic reticulum of human cells, but the functional differentiation of these is far from complete. Despite PDI being the first catalyst of protein folding reported, there is much that is still not known about its mechanisms of action. This review will focus on the interactions of the human PDI family members with substrates, including recent research on identifying and characterizing their substrate‐binding sites and on determining their natural substrates in vivo.

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“…This was also observed in vivo for thyroglobulin and thrombospondin [33]. In addition, ERp72 was shown to co‐precipitate with laminin during differentiation of mouse F9 teratocarcinoma cells [34]. On the other hand, hPDIR protein has three different a domains with the following active site sequences: CSMC, CGHC, CPHC, respectively.…”

Section: Discussionmentioning

confidence: 57%

Hcc‐2, a novel mammalian ER thioredoxin that is differentially expressed in hepatocellular carcinoma

Nissom

et al. 2006

FEBS Letters

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Hepatocellular carcinoma (HCC) is the most common primary cancer of the liver. Thus there is great interest to identify novel HCC diagnostic markers for early detection of the disease and tumour specific associated proteins as potential therapeutic targets in the treatment of HCC. Currently, we are screening for early biomarkers as well as studying the development of HCC by identifying the differentially expressed proteins of HCC tissues during different stages of disease progression. We have isolated, by reverse transcriptase and polymerase chain reaction (RT-PCR), a 1741 bp cDNA encoding a protein that is differentially expressed in HCC. This novel protein was initially identified by proteome analysis and we designate it as Hcc-2. The protein is upregulated in poorlydifferentiated HCC but unchanged in well-differentiated HCC. The full-length transcript encodes a protein of 363 amino acids that has three thioredoxin (Trx) (CGHC) domains and an ER retention signal motif (KDEL). Fluorescence GFP tagging to this protein confirmed that it is localized predominantly to the cytoplasm when expressed in mammalian cells. Protein alignment analysis shows that it is a variant of the TXNDC5 gene, and the human variants found in Genbank all show close similarity in protein sequence. Functionally, it exhibits the anticipated reductase activity in the insulin disulfide reduction assay, but its other biological role in cell function remains to be elucidated. This work demonstrates that an integrated proteomics and genomics approach can be a very powerful means of discovering potential diagnostic and therapeutic protein targets for cancer therapy.

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Elevated expression of PDI family proteins during differentiation of mouse F9 teratocarcinoma cells

Cited by 21 publications

References 45 publications

Proteomic Analysis of an α7 Nicotinic Acetylcholine Receptor Interactome

Proteomic Analysis of an α7 Nicotinic Acetylcholine Receptor Interactome

Substrate recognition by the protein disulfide isomerases

Hcc‐2, a novel mammalian ER thioredoxin that is differentially expressed in hepatocellular carcinoma

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