Bovine β-mannosidosis: Pathologic and Genetic Findings in Salers Calves

1993 ◽  
Vol 30 (2) ◽  
pp. 130-139 ◽  
Author(s):  
L. Bryan ◽  
S. Schmutz ◽  
S. D. Hodges ◽  
F. F. Snyder
Keyword(s):  
Autosomal Recessive ◽  
Storage Disease ◽  
Autosomal Recessive Disease ◽  
Pedigree Analysis ◽  
Lymphoid Tissues ◽  
Lysosomal Storage ◽  
Gestational Weight ◽  
Head Tremor ◽  
Renal Enlargement ◽  
The Brain

β-mannosidosis is a recently recognized lysosomal storage disease in newborn Salers calves. Fourteen calves with β-mannosidase deficiency were examined. Twelve calves were from routine laboratory submissions, and two calves were the result of a breeding trial. Salers calves with β-mannosidase deficiency were of normal gestational weight, 36 ± 6 kg, but were affected at birth. The head was moderately domed, and there was mild superior brachygnathism. The calves were recumbent and had a head tremor. There was bilateral renal enlargement, severe hypomyelination in the brain and variable thyroid gland enlargement. Severe cytoplasmic vacuolation was present within neurons, tubule epithelial cells, follicular cells and macrophages of the nervous, renal, thyroid and lymphoid tissues, respectively. Pedigree analysis and breeding trial results were consistent with an autosomal recessive disease. An initial biochemical survey of 1,494 Salers cattle indicated a carrier frequency of 23%.

scholarly journals A Quest to Capture Latent Fabry’s Disease in a High-Risk Subpopulation of FMF.

2021 ◽  
Author(s):  
Tomer Maller ◽  
Ilan Ben-Zvi ◽  
Merav Lidar ◽  
Avi Livneh
Keyword(s):  
Autosomal Recessive ◽  
Storage Disease ◽  
Autosomal Recessive Disease ◽  
Lysosomal Storage ◽  
Fabry’S Disease ◽  
Fabry's Disease ◽  
Wide Range ◽  
Diagnostic Confusion ◽  
Mediterranean Fever ◽  
Alpha Galactosidase

Abstract Background: Familial Mediterranean fever (FMF) is an autosomal recessive disease, associated with mutations in the Mediterranean fever gene (MEFV), and manifests with recurrent episodes of febrile serositis. Fabry’s disease (FD) is an X-linked lysosomal storage disease caused by mutations in the alpha- galactosidase A gene, and presents with a wide range of gastrointestinal, skin, vascular, renal and neurological manifestations. FMF and FD share similar manifestations, which may lead to misdiagnosis of one as the other; mostly FD is misdiagnosed as FMF. Moreover, various overlapping manifestations may stem from comorbidities, commonly coupled to FMF, as well as from colchicine adverse effects, which may add to the diagnostic confusion. Thus, we postulated that screening FMF for FD will lead to the identification of patients falsely diagnosed as FMF, or who suffer from FD that was previously missed.Methods: To find missed FD among FMF population, we performed chemical and genetic analyses for FD in blood samples obtained from a cohort of FMF patients followed in the specialized FMF center of our institution. To increase the likelihood of detecting patients with FD, we enriched the surveyed FMF population with patients exhibiting manifestations shared by patients with FD or who deviate from the typical FMF presentation.Results and conclusions: Of 172 surveyed FMF patients in a cohort derived from a clinic dedicated to FMF, none had FD. Thus, the postulation of increased odds for detecting FD in patients with FMF was not confirmed.

β-Mannosidosis in German Shepherd Dogs

2019 ◽  
Vol 56 (5) ◽  
pp. 743-748 ◽  
Author(s):  
Robert D. Jolly ◽  
Keren E. Dittmer ◽  
Dorian J. Garrick ◽  
Anastasia Chernyavtseva ◽  
Kim M. Hemsley ◽  
...  
Keyword(s):  
Nervous Tissue ◽  
Autosomal Recessive ◽  
Storage Disease ◽  
Periodic Acid ◽  
Causative Mutation ◽  
Lysosomal Storage ◽  
German Shepherd ◽  
Periodic Acid Schiff ◽  
Genomic Studies ◽  
Renal Tubular

A neurological disease was investigated in 3 German Shepherd pups from the same litter that failed to grow normally, appeared stiff, were reluctant to move, and were deaf. They developed intermittent seizures and ataxia and had proprioceptive defects. Histopathology showed severe vacuolation of neurons, astrocytes in nervous tissue, renal tubular epithelial cells, and macrophages in nervous tissue, spleen, and liver. Vacuoles appeared empty with no storage material stained by periodic acid–Schiff (PAS) or Sudan black stains, leading to a diagnosis of a lysosomal storage disease and in particular an oligosaccharidosis. Biochemical and genomic studies showed that this was β-mannosidosis, not previously diagnosed in dogs. A c.560T>A transition in exon 4 of the MANBA gene was found, which segregated in these and other family members in a manner consistent with it being the causative mutation of an autosomal recessive disease. This mutation led to substitution of isoleucine to asparagine at position 187 of the 885 amino acid enzyme, a change expected to have functional significance.

scholarly journals Canine α-l-fucosidase in relation to the enzymic defect and storage products in canine fucosidosis

1988 ◽  
Vol 254 (3) ◽  
pp. 861-868 ◽  
Author(s):  
C Barker ◽  
A Dell ◽  
M Rogers ◽  
J A Alhadeff ◽  
B Winchester
Keyword(s):  
Fast Atom Bombardment ◽  
Storage Disease ◽  
Lysosomal Storage ◽  
Multiple Forms ◽  
Apparent Homogeneity ◽  
Storage Products ◽  
And Storage ◽  
Rate Limiting ◽  
Dog Liver ◽  
The Brain

Canine liver alpha-L-fucosidase was purified to apparent homogeneity by affinity chromatography on agarose-epsilon-aminohexanoyl-fucopyranosylamine. It is composed of multiple forms of a common active subunit of 45-50 kDa, which can aggregate in different combinations to form polymers, predominantly dimers. Antiserum was raised against the purified enzyme. There is negligible residual alpha-L-fucosidase in the tissues of English springer spaniels with the lysosomal storage disease fucosidosis. Although no alpha-L-fucosidase protein was detected by Western blotting or by the purification procedure in the affected tissues, some enzymically inactive cross-reacting material was detected in both normal and affected tissues. This suggests that another protein without alpha-L-fucosidase activity was co-purified with the enzyme. Dog liver alpha-L-fucosidase was precipitated by goat anti-(human liver alpha-L-fucosidase) IgG, indicating homology between the enzymes in the two species. Two purified storage products isolated from the brain of a dog with fucosidosis were used as natural substrates for various preparations of canine liver alpha-L-fucosidase. Analysis of the digestion mixtures by t.l.c. and fast-atom-bombardment mass spectrometry suggests that canine alpha-L-fucosidase acts preferentially on the alpha-(1-3)-linked fucose at the non-reducing end and that removal of alpha-(1-6)-linked asparagine-linked N-acetylglucosamine is rate-limiting in the lysosomal catabolism of fucosylated N-linked glycans.

scholarly journals Neurodegenerative Disease Risk in Carriers of Autosomal Recessive Disease

2021 ◽  
Vol 12 ◽  
Author(s):  
Sophia R. L. Vieira ◽  
Huw R. Morris
Keyword(s):  
Genetic Risk ◽  
Autosomal Recessive ◽  
Autosomal Recessive Disease ◽  
Disease Risk ◽  
Late Onset ◽  
Gene Mutations ◽  
Carrier Status ◽  
Lysosomal Storage ◽  
Increased Risk ◽  
Distinct Allele

Genetics has driven significant discoveries in the field of neurodegenerative diseases (NDDs). An emerging theme in neurodegeneration warrants an urgent and comprehensive update: that carrier status of early-onset autosomal recessive (AR) disease, typically considered benign, is associated with an increased risk of a spectrum of late-onset NDDs. Glucosylceramidase beta (GBA1) gene mutations, responsible for the AR lysosomal storage disorder Gaucher disease, are a prominent example of this principle, having been identified as an important genetic risk factor for Parkinson disease. Genetic analyses have revealed further examples, notably GRN, TREM2, EIF2AK3, and several other LSD and mitochondria function genes. In this Review, we discuss the evidence supporting the strikingly distinct allele-dependent clinical phenotypes observed in carriers of such gene mutations and its impact on the wider field of neurodegeneration.

scholarly journals Determination of the Carnitine and Acylcarnitine Profile in Patients with Lipoid Proteinosis

2019 ◽  
Author(s):  
Ataman Gönel ◽  
Ismail Koyuncu ◽  
Mustafa Aksoy ◽  
Hakim Celik
Keyword(s):  
Autosomal Recessive ◽  
Storage Disease ◽  
Lysosomal Storage ◽  
Serum Samples ◽  
Internal Organs ◽  
Lipoid Proteinosis ◽  
Acylcarnitine Profile ◽  
Mucous Membranes ◽  
Healthy Control

Background and objectives: Lipoid proteinosis (LP) is an autosomal recessive transfer lysosomal storage disease, characterised by the accumulation of hyalin substance in the mucous membranes, skin, internal organs and brain, for which there is no biochemical diagnostic method. The aim of this study was to determine the carnitine and acylcarnitine metabolic profile with LC-MS/MS in LP patients and thereby examine the potential of this as a new biochemical method in the determination of biochemical markers in LP patients. Materials and Methods: In this study, 27 carnitine and acylcarnitine esters were measured with LC-MS/MS in serum samples taken from 14 healthy control subjects and 14 patients who presented at the Skin and Venereal Diseases Polyclinic and were diagnosed with LP as a result of clinical, radiological and histopathological examinations. Results: The results of the study showed that C0 (free carnitine) C3, C4, C4:DC, C5DC, C6, C8, C14:1, C14:2, C16 and C18 acylcarnitines were statistically significantly reduced in the LP patients (p<0.05, p<0.01). Conclusions: It was concluded that the application of carnitine profile screening, which is an inexpensive, rapid and reliable method, could make a contribution to the differential diagnosis as aa supporting laboratory test in individuals with suspected LP.

scholarly journals M Mode Ultrasound and Tissue Doppler Imaging to Assess Diaphragm Feature in Late Onset Pompe Disease

2020 ◽  
Vol 12 (3) ◽  
pp. 55-58
Author(s):  
Paris Meng ◽  
Adam Ogna ◽  
Abdallah Fayssoil
Keyword(s):  
Tissue Doppler Imaging ◽  
Pompe Disease ◽  
Autosomal Recessive ◽  
Storage Disease ◽  
Late Onset ◽  
Tissue Doppler ◽  
Doppler Imaging ◽  
Supportive Treatment ◽  
Lysosomal Storage ◽  
Diaphragm Weakness

Late-onset Pompe disease (LOPD) is an autosomal recessive lysosomal storage disease. Clinical features include skeletal muscle deficiency and diaphragm weakness. Clinical management relies on supportive treatment and mechanical ventilation in patients with chronic respiratory failure. M mode ultrasound and sniff tissue Doppler imaging can be used to assess and follow diaphragm function.

scholarly journals A pilot trial of deferiprone in pantothenate kinase-associated neurodegeneration patients

2018 ◽  
Vol 9 (4) ◽  
Author(s):  
Mohammad Rohani ◽  
Saeed Razmeh ◽  
Gholam Ali Shahidi ◽  
Maryam Orooji
Keyword(s):  
Autosomal Recessive ◽  
Rating Scales ◽  
Autosomal Recessive Disease ◽  
Pilot Trial ◽  
Qualitative Evaluation ◽  
Iron Chelator ◽  
Pantothenate Kinase ◽  
Iron Load ◽  
Magnetic Resonance Imaging Mri ◽  
The Brain

Pantothenate kinase-associated neurodegeneration (PKAN) is the most common form of neurodegeneration with brain iron accumulation, it is an autosomal recessive disease due to mutation in PANK 2 on chromosome 20, which causes the accumulation of iron in basal ganglia and production of free radicals that cause degeneration of the cells. Deferiprone is an iron chelator that was used in treatment of thalassemia patients, it can cross the blood-brain barrier and reverse the iron deposition in the brain. Five patients with genetically confirmed PKAN received 15 mg/kg deferiprone twice daily. All patients were examined at baseline, 12 and 18 months and magnetic resonance imaging (MRI) was done at the baseline and after 18 months. In our study qualitative evaluation of MRI showed that deferiprone was able to reduce the iron load in globus pallidus of all the patients and the results of clinical rating scales show that in four patients, there is an improvement in the first 12 months. The results of our paper show that deferiprone can prevent the progression of the disease.

scholarly journals Lysosomal Storage Disease in an Emu (Dromaius novaehollandiae)

1996 ◽  
Vol 33 (3) ◽  
pp. 365-366 ◽  
Author(s):  
D. Y. Rim ◽  
D. Y. Cho ◽  
H. W. Taylor
Keyword(s):  
Spinal Cord ◽  
Lysosomal Storage Disease ◽  
Storage Disease ◽  
Histochemical Staining ◽  
Lysosomal Storage ◽  
Electron Microscopic ◽  
First Case ◽  
Dromaius Novaehollandiae ◽  
Microscopic Studies ◽  
The Brain

Lysosomal storage disease involving the brain, spinal cord, liver, and spleen was discovered in a 6-month-old male emu ( Dromaius novaehollandiae). The diagnosis was based on light and electron microscopic studies and histochemical staining characteristics. This is the first case of lysosomal storage disease reported in a ratite.

scholarly journals A Fourteen Years Old Boy with Cholesterol Ester Storage Disease

1970 ◽  
Vol 10 (2) ◽  
pp. 146-148
Author(s):  
Faizul Islum Chowdhury ◽  
Ahmedul Kabir ◽  
Jayanta Banik ◽  
Pinaki Paul ◽  
Mostofa Kamal ◽  
...  
Keyword(s):  
Liver Biopsy ◽  
Cholesterol Ester ◽  
Autosomal Recessive ◽  
Storage Disease ◽  
Specific Treatment ◽  
Autosomal Recessive Disorder ◽  
Lysosomal Storage Diseases ◽  
Lysosomal Storage ◽  
Acid Lipase ◽  
Storage Diseases

Cholesterol ester storage disease (CESD) is a rare autosomal recessive disorder resulting from lysosomal acid lipase deficiency and is usually characterized by hepatomegaly and hyperlipidemia. It is diagnosed by liver biopsy which characteristically shows microvesicular steatosis and periportal fibrosis. Here we report a fourteen years old boy who had presented with unexplained hepatomegaly, and hyperlipidemia determined incidentally. He was finally diagnosed as a case of cholesterol ester storage disease by liver biopsy. Though there is yet no specific treatment for CESD; however, the early detection of cases would make the timely control of complications possible. Keyword: Cholesterol Ester Storage Disease, Lysosomal Storage Diseases, Lipidoses    doi: 10.3329/jom.v10i2.2835   J MEDICINE 2009; 10 : 146-148

scholarly journals Compound Galactosylceramidase Gene (GALC) Heterozygosity in a Boy with Infantile Krabbe Disease (KD)

PRILOZI ◽  
2015 ◽  
Vol 36 (3) ◽  
pp. 99-101 ◽  
Author(s):  
Zoran Gucev ◽  
Velibor Tasic
Keyword(s):  
Autosomal Recessive ◽  
Storage Disease ◽  
Clinical Course ◽  
Compound Heterozygote ◽  
Krabbe Disease ◽  
Lysosomal Storage ◽  
Mental Deterioration ◽  
Severe Motor ◽  
Galc Gene ◽  
Globoid Cell

Abstract Krabbe disease (KD) (globoid cell leukodystrophy) is a degenerative, lysosomal storage disease, caused by a severe loss of galactocerebrosidase (GALC) enzymatic activity. The inheritance is autosomal recessive. KD affects the white matter of the central and peripheral nervous systems. We present a 3 year old boy in whom the disease had an ‘infantile’ or ‘classic’ presentation, with spasticity, irritability, and developmental delay. In addition the boy showed progressive severe motor and mental deterioration, difficulties in swallowing and decerebration. Molecular analysis revealed that the child is a compound heterozygote: p.Asp187Val (c.560A>T) and p.Ile250Thr (c.749T>C). The father was the carrier of p.Asp187Val (c.560A>T), while the mother was the carrier of the p.Ile250Thr (c.749T>C) in exon 6 of the GALC gene. The clinical course in this compound heterozygote is severe and the patient passed away at the age of 3 years. Genotype-phenotype relations are discussed in this Macedonian patient with KD.

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