Role of cellular prion protein on LTP expression in aged mice

Maglio, Laura E.; Martins, Vilma R.; Izquierdo, Iván; Ramírez, Oscar A.

doi:10.1016/j.brainres.2006.04.056

Cited by 39 publications

(33 citation statements)

References 47 publications

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“…A defect in nitric oxide signaling (Keshet et al, 1999), which is required for mossy fiber-granule cell LTP (Maffei et al, 2003), could explain the absence of presynaptic changes needed to generate EPSC potentiation (Sola et al, 2004). Therefore, PrP knock-out may directly affect the LTP mechanism, as originally proposed for hippocampal synapses (Collinge et al, 1994;Curtis et al, 2003;Maglio et al, 2004Maglio et al, , 2006 (but see Lledo et al, 1996).…”

Section: Discussionmentioning

confidence: 95%

“…However, subsequent analysis revealed several motor, cognitive, and emotional abnormalities (Roesler et al, 1999;Criado et al, 2005) and increased susceptibility to seizures . Recordings from brain slices of PrP 0/0 mice showed reduced synaptic inhibition and long-term potentiation (LTP) (a neural correlate of learning) (Bliss and Collingridge, 1993) in the hippocampus (Collinge et al, 1994;Curtis et al, 2003;Maglio et al, 2004Maglio et al, , 2006, but this observation was not confirmed (Lledo et al, 1996). Several abnormalities have been observed in PrP 0/0 neurons in culture, including reduced Ca 2ϩ -dependent K ϩ currents (Colling et al, 1996;Herms et al, 2001;Mallucci et al, 2002) and cytoplasmic Ca 2ϩ levels (Herms et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

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Altered Neuron Excitability and Synaptic Plasticity in the Cerebellar Granular Layer of Juvenile Prion Protein Knock-Out Mice with Impaired Motor Control

et al. 2008

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Section: Discussionmentioning

confidence: 95%

Section: Introductionmentioning

confidence: 99%

Altered Neuron Excitability and Synaptic Plasticity in the Cerebellar Granular Layer of Juvenile Prion Protein Knock-Out Mice with Impaired Motor Control

et al. 2008

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“…Mitochondrial dysfunction is thought to be a key factor in agerelated diseases of humans [19] and should therefore be investigated in the cattle. Biological relationships between aging and PrP C , including antioxidant-like activity [2], synaptic transmission [15], and the expression of PrP C in brain homogenates after PK treatment. The samples after PK treatment were separated by SDS-PAGE, transferred onto PVDF membranes and reacted with mAb 44B1.…”

Section: Discussionmentioning

confidence: 99%

Proteasome Activity and Biological Properties of Normal Prion Protein: A Comparison between Young and Aged Cattle

Yoshioka

Ishiguro

Inoshima

2010

The Journal of Veterinary Medical Science

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ABSTRACT. Atypical bovine spongiform encephalopathy (atypical BSE) has recently been identified in several countries including Japan. Most cases of atypical BSE have been reported in cattle older than 8 years of age. To clarify the association between age and occurrence of atypical BSE, we investigated both the physiological properties and amount of cellular prion protein (PrP C ) in brain homogenates from young and aged cattle by enzyme-linked immunosorbent assay and immunoblotting. The amount of PrP C in the brain homogenates was not significantly different between young and aged cattle, but the amount in the detergent-insoluble fraction in the aged cattle was significantly higher than that of young cattle. Significant differences were observed in neither of the glycosylation forms nor in proteinase K sensitivity in young and aged cattle. Age-related changes included deposition of lipofuscin pigment and a decrease of 33% in proteasome activity in the brains of aged cattle compared to that of young cattle.KEY WORDS: atypical BSE, brain homogenate, cattle, prion, proteasome.J. Vet. Med. Sci. 72(12): 1583-1587, 2010 Prion diseases, also known as transmissible spongiform encephalopathies (TSE), are a group of fatal neurodegenerative disorders caused by accumulation of the proteinase K (PK)-resistant pathogenic isoform (PrP res ) in the host cellular prion protein (PrP C ) [17]. TSE, which have been found in humans and other mammalian species, include bovine spongiform encephalopathies (BSE) in cattle and scrapie in sheep and goats. Only one strain of BSE prion was originally thought to exist, in contrast to the many different scrapie strains found around the world [3]. Recently, however, a strain of atypical BSE, which is different from the classical BSE, was independently reported in Italy [5], France [1], and Japan [21]. Atypical BSE is classified into two different types: H-type, characterized by a higher molecular mass associated with the unglycosylated protein band, and L-type or a bovine amyloidotic spongiform encephalopathy (BASE), characterized by an unglycosylated protein band with a lower molecular mass and the predominance of a monoglycosylated band [1,5].To date, more than 40 cases of atypical BSE, including 2 cases in Japan [13,21], have been documented globally through active surveillance systems. Most atypical BSE cases have occurred in cattle over 8 years of age, although classical BSE cases occur mostly in animals between 4 and 6 years of age. This indicates that atypical BSE might be associated with cattle age or age-related retrogressions such as proteasome activity. However, the biochemical properties and expression of PrP C in the brain of aged cattle remain largely unclear.To clarify the existence of any relationship between cattle age and occurrence of atypical BSE, the physiological properties and amount of PrP C expression in brain homogenates were compared between young and aged cattle. Relative expressions of PrP C in brain homogenates were not significantly different between the young a...

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“…In addition, PrP c , by Cu 2+ binding, may participate in the control of calcium flux and redox stage of the presynaptic terminal (Vassallo and Herms, 2003). Lastly, pioneering electrophysiological studies (using PrP c knockout slices) by Collinge established that PrP c participates in long-term potentiation (Collinge et al, 1994;Curtis et al, 2003;Maglio et al, 2006). More recently, it has been shown that the absence of PrP c alters the expression of several neurotransmitter receptors (see (Maglio et al, 2004;Rangel et al, 2007) for examples).…”

Section: Introductionmentioning

confidence: 99%

New insights into cellular prion protein (PrPc) functions: The “ying and yang” of a relevant protein

Nicolas

Gavı́n

Rı́o

2009

Brain Research Reviews

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Role of cellular prion protein on LTP expression in aged mice

Cited by 39 publications

References 47 publications

Altered Neuron Excitability and Synaptic Plasticity in the Cerebellar Granular Layer of Juvenile Prion Protein Knock-Out Mice with Impaired Motor Control

Altered Neuron Excitability and Synaptic Plasticity in the Cerebellar Granular Layer of Juvenile Prion Protein Knock-Out Mice with Impaired Motor Control

Proteasome Activity and Biological Properties of Normal Prion Protein: A Comparison between Young and Aged Cattle

New insights into cellular prion protein (PrPc) functions: The “ying and yang” of a relevant protein

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