This case report explores the difficulties with rapid lipid-lowering therapies in a resource-limited setting. We present a case of an individual with previously diagnosed homozygous familial hypercholesterolemia presenting with anginal chest pain concerning for non-ST elevation myocardial infarction (NSTEMI), with a low-density lipoprotein (LDL) of 984 mg/dL (reference range: 100-129 mg/dL) and a reversible perfusion defect on his nuclear medicine stress test. In addition to the standard treatment for NSTEMI, including cardiac catheterization, the patient was initiated on a proprotein convertase subtilisin/kexin type 9 inhibitor and underwent two rounds of plasmapheresis, which effectively and rapidly lowered his LDL levels.
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http://dx.doi.org/10.7759/cureus.70174 | DOI Listing |
BMC Plant Biol
December 2024
College of Advanced Agricultural Sciences, Zhejiang A & F University, Hangzhou, 311300, China.
Background: Monoacylglycerol lipase (MAGL) belongs to the serine hydrolase family; it catalyzes MAG to produce glycerol and free fatty acids (FFAs), which is the final step in triacylglycerol (TAG) hydrolysis. The effects of MAGL on comprehensive lipid metabolism and plant growth and development have not been elucidated, especially in Arachis hypogaea, an important oil crop.
Results: Herein, AhMAGL3b encoding a protein with both hydrolase and acyltransferase regions, a member of MAGL gene family, was cloned and overexpressed in Arabidopsis thaliana.
Pharmacol Res
December 2024
Department of Molecular Biochemistry and Pharmacology, Istituto di Ricerche Farmacologiche Mario Negri IRCCS, Via Mario Negri 2, 20156, Milan, Italy. Electronic address:
Alzheimer's disease, the leading cause of dementia globally, represents an unresolved clinical challenge due to its complex pathogenesis and the absence of effective treatments. Considering the multifactorial etiology of the disease, mainly characterized by the accumulation of amyloid β plaques and neurofibrillary tangles of tau protein, we discuss the A673V mutation in the gene coding for the amyloid precursor protein, which is associated with the familial form of Alzheimer's disease in a homozygous state. The mutation offers new insights into the molecular mechanisms of the disease, particularly regarding the contrasting roles of the A2V and A2T mutations in amyloid β peptide aggregation and toxicity.
View Article and Find Full Text PDFJ Pediatr Endocrinol Metab
December 2024
Department of Neurology, Ankara Etlik City Hospital, Ankara, Türkiye.
Objectives: Sialidosis type 1 is a rare autosomal recessive lysosomal storage disorder caused by pathogenic variants in the gene, which encodes the sialic acid-degrading enzyme α-neuraminidase. Sialidosis type 1 is a milder form with a late-onset phenotype, characterized by progressive myoclonic epilepsy and ataxia with cherry-red spots. Sialidosis type 2 is an early-onset and more severe form presenting with dysmorphic features, hepatosplenomegaly and cognitive delay.
View Article and Find Full Text PDFPediatr Rheumatol Online J
December 2024
Translational Genetics Research Group, La Fe Health Research Institute (IIS La Fe), Avenida Fernando Abril Martorell nº 106 Tower A, 7th Floor, Valencia, Spain.
Background: Aicardi-Goutières Syndrome is a monogenic type 1 interferonopathy with infantile onset, characterized by a variable degree of neurological damage. Approximately 7% of Aicardi-Goutières Syndrome cases are caused by pathogenic variants in the ADAR gene and are classified as Aicardi-Goutières Syndrome type 6. Here, we present a new homozygous pathogenic variant in the ADAR gene.
View Article and Find Full Text PDFZh Nevrol Psikhiatr Im S S Korsakova
December 2024
Bochkov Research Centre for Medical Genetics, Moscow, Russia.
A fifth world case of autosomal recessive Siddiqi syndrome (SIDDIS) related to ene is presented. In a consanguineous Lezgin (a Dagestan ethnicity) family, there were two affected brothers aged 28 yrs (proband, personally examined) and 32 yrs. Whole-exome sequencing followed by familial Sanger sequencing detected a novel missence variant c.
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