Generalized Glycogen Storage Disease in Japanese Quail (<i>Coturnix coturnix</i>japonica)

Matsui, Tsutomu; Kuroda, Shinji; Mizutani, Makoto; Kiuchi, Yoshihiro; Suzuki, Kazuhiro; Ono, Tsutomu

doi:10.1177/030098588302000307

Cited by 34 publications

(31 citation statements)

References 12 publications

(8 reference statements)

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“…The 1057?TA, a lethal mutation in the gene of the acid alpha-glucosidase, which causes generalized glycogenosis in Brahman cattle, was detected by PCR in paraffin embedded tissues of affected animals on which post-mortem examination was performed. Clinical, histological and molecular findings were similar to previous descriptions of generalized glycogenosis (Walvoort 1985), gato (Sandstrom et al 1969), ovelha (Manktelow & Hartley 1975) e codorna japonesa (Matsui et al 1983). Esta doença é determinada por mutação no gene da glicosidase alfa ácida, o que impede parte ou toda a biossíntese da enzima e, conseqüentemente, a degradação lisossomal de glicogênio (Bijvoet et al 1998).…”

supporting

confidence: 84%

Glicogenose hereditária em bovinos Brahman no Brasil

et al. 2005

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Relata-se uma enfermidade hereditária em bovinos caracterizada por acúmulo lisossomal de glicogênio em diversos órgãos. A doença foi diagnosticada em um rebanho da raça Brahman, no município de Porto Lucena, Rio Grande do Sul, Brasil. Os animais afetados, a partir de 1 mês de idade, apresentavam dificuldade em acompanhar a mãe e crescimento retardado, desenvolviam fraqueza e tremores musculares, letargia e perda de condição corporal progressivos. Todos os bezerros eram descendentes do mesmo touro. Foi realizada necropsia em três bezerros doentes; palidez muscular do tronco e membros foi a única alteração macroscópica encontrada. Vacuolização citoplasmática de diversos órgãos foi a principal alteração histológica observada. Os vacúolos citoplasmáticos eram mais evidentes na musculatura esquelética, miocárdio, especialmente nas fibras de Purkinje e em neurônios do Sistema Nervoso Central (SNC). Nos tecidos mais afetados foi observada grande quantidade de grânulos ácido periódico de Schiff (PAS), positivos e negativos quando o tecido era tratado previamente com diastase. Uma mutação no gene da glicosidase alfa ácida, causadora da glicogenose generalizada em bovinos Brahman, a 1057?TA, foi detectada pela técnica de reação em cadeia de polimerase (PCR) em tecidos dos animais necropsiados. Também foi detectada a presença dessa mutação em amostras de sangue de animais parentes dos bezerros doentes. Os achados clínicos, patológicos e moleculares são semelhante ás descrições de glicogenose tipo II em bovinos da raça Brahman descritos na Austrália. Não foram encontrados relatos anteriores em revistas indexadas sobre glicogenose hereditária em bovinos Brahman no Brasil.

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confidence: 84%

Glicogenose hereditária em bovinos Brahman no Brasil

et al. 2005

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“…Indeed, neural pathology is prominent in the majority of lysosomal storage disorders, and there is evidence that lysosomal dysfunction can lead to neuronal cell death (Bellettato and Scarpa, 2010). Substantial glycogen accumulation is present in the central nervous system of Pompe patients (DeRuisseau et al, 2009; Gambetti et al, 1971; Mancall et al, 1965; Martin et al, 1973; Martini et al, 2001; Teng et al, 2004; Thurberg et al, 2006) as well as animal models including mice and quail (DeRuisseau et al, 2009; Matsui et al, 1983; Sidman et al, 2008). Clinical case reports have also described extensive neuropathology in Pompe tissues obtained on autopsy.…”

Section: The Central Nervous System Breathing and Pompe Diseasementioning

confidence: 99%

The respiratory neuromuscular system in Pompe disease

Fuller

ElMallah

Smith

et al. 2013

Respiratory Physiology & Neurobiology

109

117

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Pompe disease is due to mutations in the gene encoding the lysosomal enzyme acid α-glucosidase (GAA). Absence of functional GAA typically results in cardiorespiratory failure in the first year; reduced GAA activity is associated with progressive respiratory failure later in life. While skeletal muscle pathology contributes to respiratory insufficiency in Pompe disease, emerging evidence indicates that respiratory neuron dysfunction is also a significant part of dysfunction in motor units. Animal models show profound glycogen accumulation in spinal and medullary respiratory neurons and altered neural activity. Tissues from Pompe patients show central nervous system glycogen accumulation and motoneuron pathology. A neural mechanism raises considerations about the current clinical approach of enzyme replacement since the recombinant protein does not cross the blood-brain-barrier. Indeed, clinical data suggest that enzyme replacement therapy delays symptom progression, but many patients eventually require ventilatory assistance, especially during sleep. We propose that treatments which restore GAA activity to respiratory muscles, neurons and networks will be required to fully correct ventilatory insufficiency in Pompe disease.

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“…This deficiency results in cellular lysosomal and cytoplasmic glycogen accumulation (Byrne et al, 2011a). Myopathy is a hallmark of this disease, but a growing database indicates that motor failure in Pompe disease also involves CNS pathology (Hogan et al, 1969;Martin et al, 1973;Matsui et al, 1983;Teng et al, 2004;Sidman et al, 2008;DeRuisseau et al, 2009;Burrow et al, 2010;Mah et al, 2010). However, the current clinical strategy of intravenous infusion of recombinant GAA (Beck, 2009;Byrne et al, 2011b) will not mitigate CNS glycogen accumulation (DeRuisseau et al, 2009;Lee et al, 2011;Qiu et al, 2012).…”

Section: Pompe Disease and Aav9mentioning

confidence: 99%

Retrograde Gene Delivery to Hypoglossal Motoneurons Using Adeno-Associated Virus Serotype 9

ElMallah

Falk

Lane

et al. 2012

Human Gene Therapy Methods

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Retrograde viral transport (i.e., muscle to motoneuron) enables targeted gene delivery to specific motor pools. Recombinant adeno-associated virus serotype 9 (AAV9) robustly infects motoneurons, but the retrograde transport capabilities of AAV9 have not been systematically evaluated. Accordingly, we evaluated the retrograde transduction efficiency of AAV9 after direct tongue injection in 129SVE mice as well as a mouse model that displays neuromuscular pathology (Gaa -/ -). Hypoglossal (XII) motoneurons were histologically evaluated 8 weeks after tongue injection with AAV9 encoding green fluorescent protein (GFP) with expression driven by the chicken b-actin promoter (1 · 10 11 vector genomes). On average, GFP expression was detected in 234 -43 XII motoneurons 8 weeks after AAV9-GFP tongue injection. In contrast, tongue injection with a highly efficient retrograde anatomical tracer (cholera toxin b subunit, CT-b) resulted in infection of 818 -88 XII motoneurons per mouse. The retrograde transduction efficiency of AAV9 was similar between the 129SVE mice and those with neuromuscular disease (Gaa -/ -). Routine hematoxylin and eosin staining and cluster of differentiation (CD) immunostaining for T cells (CD3) indicated no persistent inflammation within the tongue or XII nucleus after AAV9 injection. Additional experiments indicated no adverse effects of AAV9 on the pattern of breathing. We conclude that AAV9 can retrogradely infect a significant portion of a given motoneuron pool in normal and dystrophic mice, and that its transduction efficiency is approximately 30% of what can be achieved with CT-b.

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Generalized Glycogen Storage Disease in Japanese Quail (Coturnix coturnixjaponica)

Cited by 34 publications

References 12 publications

Glicogenose hereditária em bovinos Brahman no Brasil

Glicogenose hereditária em bovinos Brahman no Brasil

The respiratory neuromuscular system in Pompe disease

Retrograde Gene Delivery to Hypoglossal Motoneurons Using Adeno-Associated Virus Serotype 9

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