Functional characterization of novel variants in SMPD1 in Indian Patients with Acid sphingomyelinase deficiency

2021 ◽  
Author(s):  
Dipti Deshpande ◽  
Shailesh Kumar Gupta ◽  
Asodu Sandeep Sarma ◽  
Prajnya Ranganath ◽  
Jamal Mohammed Nurul Jain S. ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Acid Sphingomyelinase ◽  
Sphingomyelinase Deficiency ◽  
Indian Patients ◽  
Novel Variants

Acid sphingomyelinase deficiency: Prevalence and characterization of an intermediate phenotype of Niemann-Pick disease

2006 ◽  
Vol 149 (4) ◽  
pp. 554-559 ◽  
Author(s):  
Melissa P. Wasserstein ◽  
Alan Aron ◽  
Scott E. Brodie ◽  
Calogera Simonaro ◽  
Robert J. Desnick ◽  
...  
Keyword(s):  
Acid Sphingomyelinase ◽  
Intermediate Phenotype ◽  
Sphingomyelinase Deficiency ◽  
Niemann Pick Disease ◽  
Niemann Pick ◽  
Pick Disease

Functional characterization of the postulated intramolecular sphingolipid activator protein domain of human acid sphingomyelinase

2004 ◽  
Vol 385 (12) ◽  
Author(s):  
Melanie Kölzer ◽  
Klaus Ferlinz ◽  
Oliver Bartelsen ◽  
Silvia Locatelli Hoops ◽  
Florian Lang ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Acid Sphingomyelinase ◽  
Protein Domain ◽  
Activator Protein ◽  
Human Acid

Niemann–Pick type C disease: Novel NPC1 mutations and characterization of the concomitant acid sphingomyelinase deficiency

2006 ◽  
Vol 87 (2) ◽  
pp. 113-121 ◽  
Author(s):  
H TAMURA ◽  
T TAKAHASHI ◽  
N BAN ◽  
H TORISU ◽  
H NINOMIYA ◽  
...  
Keyword(s):  
Acid Sphingomyelinase ◽  
Sphingomyelinase Deficiency ◽  
Type C ◽  
Niemann Pick

scholarly journals Structural and Functional Characterization of Four Novel Fibrinogen Mutations in FGB Causing Congenital Fibrinogen Disorder

2022 ◽  
Vol 23 (2) ◽  
pp. 721
Author(s):  
Eliška Ceznerová ◽  
Jiřina Kaufmanová ◽  
Žofie Sovová ◽  
Jana Štikarová ◽  
Jan Loužil ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Abnormal Development ◽  
Screening Tests ◽  
Morphological Properties ◽  
Fiber Density ◽  
Reverse Phase ◽  
Gene Coding ◽  
Novel Variants ◽  
Fiber Thickness

Congenital fibrinogen disorders are caused by mutations in genes coding for fibrinogen and may lead to various clinical phenotypes. Here, we present a functional and structural analysis of 4 novel variants located in the FGB gene coding for fibrinogen Bβ chain-heterozygous missense BβY416C and BβA68S, homozygous nonsense BβY345*, and heterozygous nonsense BβW403* mutations. The cases were identified by coagulation screening tests and further investigated by various methods. Fibrin polymerization had abnormal development with decreased maximal absorbance in all patients. Plasmin-induced fibrin degradation revealed different lytic phases of BβY416C and BβW403* than those of the control. Fibrinopeptide cleavage measured by reverse phase high pressure liquid chromatography of BβA68S showed impaired release of fibrinopeptide B. Morphological properties, studied through scanning electron microscopy, differed significantly in the fiber thickness of BβY416C, BβA68S, and BβW403*, and in the fiber density of BβY416C and BβW403*. Finally, homology modeling of BβA68S showed that mutation caused negligible alternations in the protein structure. In conclusion, all mutations altered the correct fibrinogen function or structure that led to congenital fibrinogen disorders.

Functional characterization of novel variants in the CETP promoter and the LIPC gene in subjects with hyperalphalipoproteinemia

2013 ◽  
Vol 416 ◽  
pp. 92-95 ◽  
Author(s):  
Wanee Plengpanich ◽  
Siraprapa Tongkobpetch ◽  
Vorasuk Shotelersuk ◽  
Wilfried Le Goff ◽  
Weerapan Khovidhunkit
Keyword(s):  
Functional Characterization ◽  
Novel Variants

scholarly journals Functional Characterization of the N-glycosylation Sites of Human Acid Sphingomyelinase by Site-Directed Mutagenesis

1997 ◽  
Vol 243 (1-2) ◽  
pp. 511-517 ◽  
Author(s):  
Klaus Ferlinz ◽  
Robert Hurwitz ◽  
Heidi Moczall ◽  
Stephanie Lansmann ◽  
Edward H. Schuchman ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Acid Sphingomyelinase ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Glycosylation Sites ◽  
Human Acid
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