The 37 kDa/67 kDa laminin receptor is required for PrPSc propagation in scrapie‐infected neuronal cells

Leucht, Christoph; Simoneau, Steve; Rey, Clémence; Vana, Karen; Rieger, R.; Lasmézas, Corinne Ida; Weiß, Stefan

doi:10.1038/sj.embor.embor820

Cited by 23 publications

(38 citation statements)

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“…A lymphotoxin-b immunoglobulin given after intraperitoneal inoculation [36,42,81] or infection by skin scarification [82] cleared PrP res from the spleen and prevented neuroinvasion, probably by interfering with FDC maturation and activation. Another candidate may be an antibody to the 37-kDa/67-kDa laminin receptor, which has a dramatic curative effect in cell culture [83], or recombinant single-chain antibodies to this receptor which were able to reduce PrP res in the spleens of intraperitoneally inoculated mice [84].…”

Section: Passive Immunizationmentioning

confidence: 99%

“…It may also bind PrP res [202] and plays a critical role in the propagation of PrP res [83]. Therefore, interfering with this putative cell surface ligand for PrP may have therapeutic consequences (for a complete review of LRP/LR therapeutic approaches, see [203]).…”

Section: Targeting the Laminin Receptor Precursor Protein (Lrp/lr)-prmentioning

confidence: 99%

“…All these approaches have been used successfully to target LRP and inhibit PrP res accumulation in cell culture [83]. No in vivo testing has been reported.…”

Section: Targeting the Laminin Receptor Precursor Protein (Lrp/lr)-prmentioning

confidence: 99%

“…In cell culture, siRNA has been shown to suppress exogenous and endogenous PrP gene (Prnp) expression [226], and siRNA corresponding to the Prnp nucleotides 392 to 410 reduced PrP res formation [227]. siRNA methods have also been used to target important PrP ligands such as LRP/LR, leading to inhibition of PrP res accumulation in cell culture [83]. A recently developed transgenic mouse ectopically expressing LRP/LR siRNA may serve as a good model for future prion research [228].…”

Section: Rna Interference and Gene Therapymentioning

confidence: 99%

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Prion Disease Therapy: Trials and Tribulations

Sim

Caughey

2010

Protein Misfolding Diseases

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Section: Passive Immunizationmentioning

confidence: 99%

Section: Targeting the Laminin Receptor Precursor Protein (Lrp/lr)-prmentioning

confidence: 99%

“…All these approaches have been used successfully to target LRP and inhibit PrP res accumulation in cell culture [83]. No in vivo testing has been reported.…”

Section: Targeting the Laminin Receptor Precursor Protein (Lrp/lr)-prmentioning

confidence: 99%

Section: Rna Interference and Gene Therapymentioning

confidence: 99%

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Prion Disease Therapy: Trials and Tribulations

Sim

Caughey

2010

Protein Misfolding Diseases

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“…Overall, the function of PrP c still remains enigmatic and allows room for presumptions, although a neuroprotective role presently appears most likely [4,[23][24][25][26][27]. The 37-kDa/67-kDa laminin receptor (LRP/LR) is one of the described potential receptors for PrP c , prion uptake and conversion co-factor for prion formation [28,29]. The spread of prions from cell to cell could be imparted by exosomes [30,31].…”

mentioning

confidence: 99%

Aptamers against prion proteins and prions

Gilch

Schätzl

2009

Cell. Mol. Life Sci.

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Prion diseases are fatal neurodegenerative and infectious disorders of humans and animals, characterized by structural transition of the host-encoded cellular prion protein (PrP(c)) into the aberrantly folded pathologic isoform PrP(Sc). RNA, DNA or peptide aptamers are classes of molecules which can be selected from complex combinatorial libraries for high affinity and specific binding to prion proteins and which might therefore be useful in diagnosis and therapy of prion diseases. Nucleic acid aptamers, which can be chemically synthesized, stabilized and immobilized, appear more suitable for diagnostic purposes, allowing use of PrP(Sc) as selection target. Peptide aptamers facilitate appropriate intracellular expression, targeting and re-routing without losing their binding properties to PrP, a requirement for potential therapeutic gene transfer experiments in vivo. Elucidation of structural properties of peptide aptamers might be used as basis for rational drug design, providing another attractive application of peptide aptamers in the search for effective anti-prion strategies.

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Overexpression of PrPc, combined with MGr1‐Ag/37LRP, is predictive of poor prognosis in gastric cancer

Zhou

Shang

Liu

et al. 2014

Intl Journal of Cancer

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Prion protein (PrPc) has been previously reported to be involved in gastric cancer (GC) development and progression. However, the association between expression of PrPc and GC prognosis is yet poorly characterized. In the present study, the expressions of PrPc and MGr1-Ag/37LRP, a protein interacting with PrPc, were detected using the tissue microarray technique and immunohistochemical method to compare clinicopathological parameters of 238 GC patients. We found that the expressions of PrPc and MGr1-Ag/37LRP were upregulated in GC lesions compared with their expressions in adjacent noncancerous tissues (p < 0.01). High expression of PrPc was detected in 37.39% (89/238) of GC patients and positively correlated with the expression of MGr1-Ag/37LRP (r = 0.532, p < 0.001). PrPc expression was associated with a number of clinicopathological parameters including depth of invasion and lymph node metastasis of the tumor (p < 0.001). High expression of PrPc brought a poorer prognosis than low PrPc expression. Moreover, GC patients with high level of PrPc and high level of MGr1-Ag/37LRP had the poorest prognosis. Multivariate survival analysis suggested that, along with other parameters, combined expression of PrPc and MGr1-Ag/37LRP was independent prognostic factors for GC patients. These data indicates that overexpression of PrPc, combined with MGr1-Ag/37LRP, is predictive of poor prognosis in GC and thereby could be used to guide the clinical decision.What's new?Prion protein was originally exclusively associated with prion disease but has now been linked to other processes such as cancer and inflammation. Here the authors examined the role of prion protein and its receptor MGr1-Ag/37LRP in gastric cancer. They found that both factors were upregulated in gastric cancer, and not in neighboring healthy, tissues and established the combined expression of prion protein and MGr1-Ag/37LRP as an independent prognostic factor for gastric cancer patients. These studies support a new role of prion protein in cancer and identify a new biomarker for a more accurate prediction of prognosis in gastric cancer patients.

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The 37 kDa/67 kDa laminin receptor is required for PrPSc propagation in scrapie‐infected neuronal cells

Abstract: ERRATUMIn the February 2003 issue of EMBO reports (4, 159-165), we published an incorrect structure for [N-β-oxo-octanoyl]-homoserine lactam. The correct structure is shown below.

Cited by 23 publications

References 0 publications

Prion Disease Therapy: Trials and Tribulations

Prion Disease Therapy: Trials and Tribulations

Aptamers against prion proteins and prions

Overexpression of PrPc, combined with MGr1‐Ag/37LRP, is predictive of poor prognosis in gastric cancer

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