1/79. prenatal diagnosis of mucolipidosis II--electron microscopy and biochemical evaluation.prenatal diagnosis of mucolipidosis type II (I-cell disease) can be performed quickly and reliably by electron microscopy of chorionic villus tissue. This study reports the results of studies in three prenatal assessments (two families) where the pregnancy was at one in four risk of the disorder. In all three cases, electron microscopy showed marked vacuolation in chorionic villus cells, consistent with the fetus being affected by the disorder. Further studies in cultured chorionic villus cells showed a marked deficiency of a number of lysosomal enzymes. All pregnancies were terminated. follow-up studies in fetal tissue (where available) confirmed the prenatal diagnosis as correct.- - - - - - - - - - ranking = 1keywords = lysosomal enzyme, enzyme (Clic here for more details about this article) |
2/79. MRI appearances of hip abnormalities in mucolipidosis, type III.Mucolipidosis type III (ML-III) is a lysosomal storage disease often presenting with joint involvement. We report the MRI appearance of the hips in two siblings with ML-III showing abnormal signal intensity within the hips with increased synovial thickness. Although the etiology is uncertain this may reflect a fibrous response to ML-III.- - - - - - - - - - ranking = 0.83349749119271keywords = lysosomal storage disease, lysosomal storage, storage disease, storage (Clic here for more details about this article) |
3/79. I-cell disease (Mucolipidosis II).I-cell disease (Mucolipidosis II) is one of the lysosomal storage diseases which presents in the neonatal period, and within six months will phenotypically resemble the severe forms of the group of disorders called the "mucopolysaccharidoses" but without mucopolysacchariduria. In Mucolipidosis II, fibrocytes exhibit "abnormal lysosomes". Activities of several lysosomal enzymes are low in fibroblast cultures but high in mucolipidosis II serum. We present a patient with I-cell disease diagnosed on the basis of clinical, radiological and biochemical features. The mother of this child was pregnant and the fetus was also found to be affected.- - - - - - - - - - ranking = 1.8334974911927keywords = lysosomal enzyme, lysosomal storage disease, lysosomal storage, storage disease, storage, enzyme (Clic here for more details about this article) |
4/79. Clinical presentation of congenital sialidosis in a patient with a neuraminidase gene frameshift mutation.Congenital sialidosis is a rare lysosomal storage disease caused by a primary neuraminidase deficiency which results from defects in the neuraminidase gene on chromosome 6p. The inheritance is autosomal recessive. patients exhibit excessive urinary excretion of bound sialic acid and decreased or undetectable amounts of neuraminidase activity in various tissues. The clinical expression is variable, but ascites and hepatosplenomegaly are hallmarks of the disease. Skeletal abnormalities, facial dysmorphism and inguinal herniae have been described in most of the few reported cases. We describe a baby girl with biochemically proven sialidosis, who in addition to the above clinical features, had severely dilated coronary arteries, excessive retinal vascular tortuosity and an erythematous, macular rash. Homozygosity for a frameshift mutation at residue 623 of the neuraminidase cDNA was found. We speculate that the additional features found in our patient might be associated with the here described genotype of congenital sialidosis. CONCLUSION: Severely dilated coronary arteries, excessive retinal vascular tortuosity and an erythematous macular rash might be associated features of congenital sialidosis.- - - - - - - - - - ranking = 0.83349749119271keywords = lysosomal storage disease, lysosomal storage, storage disease, storage (Clic here for more details about this article) |
5/79. Spinal anesthesia for a patient with type I sialidosis undergoing abdominal surgery.Type I and II sialidosis are autosomal recessively inherited glycoprotein storage disorders. Until now, there has been no published reports of patients with these conditions requiring anesthesia. We present the case of a 31-year-old male afflicted with type I sialidosis who underwent a surgical jejunostomy. Regional (spinal) anesthesia was carried out uneventfully. We discuss the anesthetic challenges posed by patients with type I and II sialidosis. Airway assessment and management is particularly crucial.- - - - - - - - - - ranking = 0.0025528261111444keywords = storage (Clic here for more details about this article) |
6/79. Peripheral blood lymphocyte appearance in a case of I cell disease.In general, peripheral blood smears are performed to obtain information with regard to various morphological features as an aid in the diagnosis of infection or malignancy. This report presents a patient with I cell disease (inclusion cell disease), a fatal lysosomal storage disorder caused by a defect in an enzyme responsible for the transfer of mannose-6-phosphate ligands to precursor lysosomal enzymes. As a consequence, most lysosomal enzymes are transported outside the cell instead of being correctly targeted into the lysosomes, resulting in the storage of macromolecules in lysosomes. I cell disease, with its heterogeneous clinical presentation, can be diagnosed by the presence of intracellular vacuole-like inclusions in lymphocytes and fibroblasts, high serum lysosomal enzyme activities, and a defect of N-acetylglucosamine-1-phosphotransferase. This report describes the morphological aspects of peripheral lymphocytes in a blood smear of a patient, the first clue to the final diagnosis of I cell disease. The observed vacuole-like inclusions in lymphocytes of this patient were negative for periodic acid Schiff (PAS) and sudan black B staining, in contrast to earlier reports.- - - - - - - - - - ranking = 3.1757447914451keywords = lysosomal enzyme, lysosomal storage, storage, enzyme (Clic here for more details about this article) |
7/79. Novel missense mutations in the human lysosomal sialidase gene in sialidosis patients and prediction of structural alterations of mutant enzymes.Three novel missense mutations in the human lysosomal sialidase gene causing amino acid substitutions (P80L, W240R. and P316S) in the coding region were identified in two Japanese sialidosis patients. One patient with a severe, congenital form of type 2 sialidosis was a compound heterozygote for 239C-to-T (P80L) and 718T-to-C (W240R). The other patient with a mild juvenile-onset phenotype (type 1) was a homozygote for the base substitution of 946C-to-T (P316S). None of these mutant cDNA products showed enzymatic activity toward an artificial substrate when coexpressed in galactosialidosis fibroblastic cells together with protective protein/cathepsin a (PPCA). All mutants showed a reticular immunofluorescence distribution when coexpressed with the PPCA gene in COS-1 cells, suggesting that the gene products were retained in the endoplasmic reticulum/Golgi area or rapidly degraded in the lysosomes. Homology modeling of the structural changes introduced by the mutations predicted that the P80L and P316S transversions cause large conformational changes including the active site residues responsible for binding the sialic acid carboxylate group. The W240R substitution was deduced to influence the molecular surface structure of a limited region of the constructed models, which was also influenced by previously identified V217M and G243R transversions.- - - - - - - - - - ranking = 0.00048187943061961keywords = enzyme (Clic here for more details about this article) |
8/79. Clinical variability in mucolipidosis III (pseudo-Hurler polydystrophy).Mucolipidosis III (MLIII) is caused by a deficiency of UDP-N-acetylglucosamine:lysosomal enzyme N-acetylglucosamine 1-phosphotransferase (phosphotransferase) activity, an enzyme responsible for the formation of the recognition marker on most lysosomal enzymes. The consequences of this defect are impairment of many lysosomal catabolic processes. A deficiency of phosphotransferase activity causes two phenotypically different diseases: mucolipidosis II and a rare form, mucolipidosis III (pseudo-Hurler polydystrophy). The purpose of this article is to report three patients with ML III, presenting quite different clinical courses: Patient 1 is a 13-year-old girl in whom the only symptoms of ML III were joint stiffness of the hands. patients 2 and 3 are sibs: a 5-year-old boy with a severe form of ML III and his 2-year-old sister, who is less affected than her brother at the same age. A comparison of biochemical results and the clinical picture of our patients with cases in the literature is presented.- - - - - - - - - - ranking = 2.0001204698577keywords = lysosomal enzyme, enzyme (Clic here for more details about this article) |
9/79. Severe gingival hyperplasia in a child with I-cell disease.I-cell disease (mucolipidosis II) is a rare metabolic disorder resulting from the deficiency of a specific lysosomal enzyme, N-acetylglucosamine-1-phosphotransferease. The disease presents as a mental and motor developmental delay with oral manifestations that include severe gingival hyperplasia usually seen before one year of age. The life expectancy of children with this condition is poor, with death usually occurring around the fifth year. A case report of a 3-year-old Pakistani male, with I-cell disease, is presented. The chief dental concerns of the parents were his swollen gums and delayed tooth eruption. Supportive treatment only was initiated. Differential diagnosis for severe gingival overgrowth in young patients should take account of this rare metabolic disorder in addition to hereditary and idiopathic fibromatosis and drug associated gingival overgrowth.- - - - - - - - - - ranking = 1keywords = lysosomal enzyme, enzyme (Clic here for more details about this article) |
10/79. Mucolipidosis III type C: first-trimester biochemical and molecular prenatal diagnosis.OBJECTIVES: Mucolipidosis IIIC (MLIIIC) is a rare autosomal recessive lysosomal storage disease resulting from defective mannose 6-phosphate-dependent lysosomal enzyme trafficking; mutations of the gamma subunit of N-acetylglucosamine-1 phosphotransferase (GINAcPT) were recently found to cause its pathogenesis. We report here for the first time prenatal diagnosis (PND) for MLIIIC by means of chorionic villous sampling (CVS). methods AND RESULTS: A fetus in a large Bedouin-Moslem family was found to be homozygous for the founder haplotype and the mutational SSCP pattern of MLIIIC. The diagnosis was confirmed by markedly reduced lysosomal enzyme activities in cultured chorionic villi. The molecular identification of the disease-causing mutation in this large Bedouin-Moslem kindred permitted, for the first time, identification of carriers and couples at risk. CONCLUSIONS: The feasibility of early PND for a progressive disabling disease is important for its prevention. Nevertheless, the feasibility of PND raises a serious dilemma since affected individuals might have a variable phenotype and the disease is progressive and non-lethal. In addition, religious and social constraints are important factors to be taken into consideration in the genetic counseling of couples at risk.- - - - - - - - - - ranking = 1.8336179610504keywords = lysosomal enzyme, lysosomal storage disease, lysosomal storage, storage disease, storage, enzyme (Clic here for more details about this article) |
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