Structural and functional analysis of the ovine laminin receptor gene (RPSA): Possible involvement of the LRP/LR protein in scrapie response

Marcos-Carcavilla, Ane; Calvo, J.H.; Gonzalez, Claudette Hajaj; Serrano, Carmen; Moazami‐Goudarzi, Katayoun; Laurent, Pascal; Bertaud, Maud; Hayes, Hélène; Beattie, A. E.; Lyahyai, Jaber; Martín-Burriel, Inmaculada; Torres, Juan María; Serrano, M.

doi:10.1007/s00335-007-9085-6

Cited by 7 publications

(16 citation statements)

References 61 publications

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“…Real-time quantitative PCR should be performed to investigate the absolute quantitation of the active RPSA gene mRNA expression level in different tissues. Real-time RT-PCR revealed a significant decrease in ovine RPSA mRNA in the cerebellum after scrapie infection (Marcos-Carcavilla et al 2008). Previous research in ovine brain has shown that the highest level of expression of RPSA was in the neocortex using RT-PCR (Marcos-Carcavilla et al 2008;Qiao et al 2009).…”

Section: Discussionmentioning

confidence: 95%

“…The interactions of PrP and RPSA are not restricted to the cell surface but also occur in intracellular compartments, which suggest a putative role of RPSA in the trafficking of PrP molecules (Nikles et al 2008). Real-time RT-PCR revealed a significant decrease in ovine RPSA mRNA in the cerebellum after scrapie infection (Marcos-Carcavilla et al 2008). RPSA mRNA levels were much higher in neuronal tissues than in peripheral tissues and may be involved in the regulation of PrP Sc propagation in sheep (Qiao et al 2009).…”

Section: Introductionmentioning

confidence: 97%

“…Polymorphisms associated with resistance to scrapie infection have been identified in sheep RPSA at interesting amino acid positions (241, 272, and 290), which could participate in the species barrier to scrapie (Marcos-Carcavilla et al 2008). The RPSA gene has been isolated in some species, including human, mouse, cattle, chicken, pig, and sheep (Yow et al 1988;Rao et al 1989;Grosso et al 1991;Clausse et al 1996;Knorr et al 2007;Marcos-Carcavilla et al 2008;Qiao et al 2008). In humans, 17 copies of the human 37 kDa laminin receptor precursor are processed pseudogenes arising from retropositional events .…”

Section: Introductionmentioning

confidence: 98%

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Molecular Characterization of the Full-Length Coding Sequence of the Caprine Laminin Receptor Gene (RPSA)

Zhou

Zheng

et al. 2010

Biochem Genet

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Scrapie is a prion disease in sheep and goats. Ribosomal protein SA (RPSA), also called 37 kDa laminin receptor precursor/67 kDa laminin receptor has been demonstrated to be a putative cell surface receptor for prion. To investigate the caprine RPSA, we cloned the full-length coding sequence of the gene of goat and submitted it to GenBank. The length of the open reading frame is 888 bp, encoding 295 amino acids. The putative amino acid sequence is highly similar to that of other mammals. The caprine amino acid sequence of RPSA is shown to be identical to the sequence of species susceptible to scrapie at positions 241, 272, and 291. The phylogenetic tree analysis revealed that the genetic distance between sheep and goat is the smallest. Moreover, RT-PCR results of 11 tissues indicated that RPSA mRNA is expressed in all selected caprine tissues.

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Section: Discussionmentioning

confidence: 95%

Section: Introductionmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 98%

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Molecular Characterization of the Full-Length Coding Sequence of the Caprine Laminin Receptor Gene (RPSA)

Zhou

Zheng

et al. 2010

Biochem Genet

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“…Eight of our 19 mutations were also present in the Spanish breeds examined by Marcos-Carcavilla et al (2008). They neither found polymorphisms that cause an amino acid change.…”

Section: Mutation Detection Of the Rpsa Gene In Sheepmentioning

confidence: 90%

“…Furthermore, some species like rabbits, pigs, and dogs seem to be completely resistant to natural infection of prion diseases and this resistance is probably a consequence of the conformation of the prion protein of the host species and therefore the amino acid sequence of PrP (Lysek et al, 2005). Nevertheless, as the RPSA protein is necessary for prion propagation, differences in both the RPSA conformation and the PRP conformation can affect the binding between both proteins and have a putative role in the strength of the species barrier (Marcos-Carcavilla et al, 2008). Mutation detection of the RPSA gene, however, has been hampered by the presence of multiple pseudogenes, with sequences highly similar to the functional full-length gene.…”

mentioning

confidence: 99%

Ribosomal protein SA and its pseudogenes in ruminants: an extremely conserved gene family

Broeke¹,

Poucke²,

Zeveren³

et al. 2013

CZECH J ANIM SCI

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ABSTRACT:The ribosomal protein SA (RPSA), also known as 37-kDa laminin receptor precursor/67-kDa laminin receptor (LRP/LR), has been identified as a multifunctional protein, playing an important role in multiple pathologies like cancer and prion diseases. Since RPSA is involved in the binding and internalization of the prion protein, mutations in the ovine RPSA gene, influencing the RPSA-PrP C /PrP Sc binding, can potentially play a part in the resistance to prion diseases. Our goal was to further characterize the complex RPSA gene family and to detect structural mutations which can play a role in this disease. In a prior study, 11 ovine pseudogenes were detected experimentally. As the whole genome shotgun ovine genome became accessible, an in silico genome-wide screening was performed and 37 new pseudogenes (36 processed and one semi-processed pseudogene) were detected, bringing the total to 48 ovine RPSA pseudogenes. Additionally, the complete bovine genome was screened in silico and 56 pseudogenes were identified. Once these sequences were known, it was possible to analyze the presence of mutations in the coding sequence and exon-flanking regions of the ovine functional full-length RPSA gene without the interference of pseudogenic sequences. Nineteen mutations were found: one in the 5' UTR, a silent one in the coding region, and seventeen in the exon-flanking regions, including an interesting mutation in the SNORA62 gene, localized in intron 4 of RPSA, leading to potential ribosomal defects. Structural mutations of the RPSA gene can be ruled out to play a role in transmissible spongiform encephalopathies but regulatory mutations still can have an effect on these diseases.

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Cloning and characterization of full-length coding sequence (CDS) of the ovine 37/67-kDa laminin receptor (RPSA)

Qiao

Wang

et al. 2008

Mol Biol Rep

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The 37-kDa Laminin Receptor Precursor (LRP)/67-kDa Laminin Receptor (LR), also known as ribosomal protein SA (RPSA), had been identified as a putative cell surface receptor for prions. Herein, we isolated the full-length coding sequence (CDS) of the ovine 37/67-kDa LRP/LR gene and submitted it to the GenBank under accession number EF649775. The open reading frame (ORF) of the 37/67-kDa LRP/LR CDS is 885 bp in length, containing six exons encoding a protein of 295 amino acids. The nucleotide sequence presented here is well coincided with the whole ovine genome of the 37/67-kDa LRP/LR previously published. Moreover, we identified four novel single nucleotide polymorphism sites (SNPs) at position 324 in exon 4, positions at 809, 875, and 881 in exon 7, respectively. Further, based on the deduced amino acid sequence alignment of the 37/67-kDa LRP/LR from human, cattle, mice, pig, chicken, and sheep, we also identified three polymorphic amino acid sites (PAAs) at residues 241, 272, and a novel site at residue 270 in the putative indirect prion protein (PrP) interaction region (180-285) on 37/67-kDa LRP/LR. Prediction of protein secondary structure further indicated that PAAs at residues 241, 270 and 272 may cause protein conformation changes as predicted, which may affect on the binding with prion protein. In addition, multiple-tissues RT-PCR results revealed that 37/67-kDa LRP/LR mRNA is expressed in all the 11 selected ovine tissues.

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Structural and functional analysis of the ovine laminin receptor gene (RPSA): Possible involvement of the LRP/LR protein in scrapie response

Cited by 7 publications

References 61 publications

Molecular Characterization of the Full-Length Coding Sequence of the Caprine Laminin Receptor Gene (RPSA)

Molecular Characterization of the Full-Length Coding Sequence of the Caprine Laminin Receptor Gene (RPSA)

Ribosomal protein SA and its pseudogenes in ruminants: an extremely conserved gene family

Cloning and characterization of full-length coding sequence (CDS) of the ovine 37/67-kDa laminin receptor (RPSA)

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