Sulfatides

Merten, Michael; Motamedy, S.; Ramamurthy, S; Arnett, Frank C.

doi:10.1161/01.cir.0000095030.44185.6a

Cited by 17 publications

(6 citation statements)

References 26 publications

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“…In autoimmune diseases, antibodies to collagen molecules, phospholipids and sulfated glycolipids have been reported [Merten et al, 2003;Gergely and Poor, 2004]. It is possible that autoantibodies cross the placenta and effect the development of the fetal skeleton or interfere with vitamin K metabolism.…”

Section: Discussionmentioning

confidence: 99%

Clinical and molecular analysis of arylsulfatase E in patients with brachytelephalangic chondrodysplasia punctata

Nino

Matos-Miranda

Maeda

et al. 2008

American J of Med Genetics Pt A

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X-linked Recessive Chondrodysplasia Punctata (CDPX1) is due to a defect in arylsulfatase E (ARSE), located on Xp22.3. Neither the substrate nor function of the encoded warfarin-sensitive arylsulfatase has been identified and molecular analysis remains the only confirmatory diagnostic test. Nevertheless, the majority of patients evaluated have not had identifiable mutations in ARSE, and thus far 23 patients have been reported. The major clinical features in these patients are also present in a group now recognized as phenocopies, due to vitamin K deficiency in early gestation or maternal autoimmune disease. We evaluated the ARSE gene in 11 patients who met clinical criteria for CDPX1. We amplified all exons and intronic flanking sequence from each patient, and investigated suspected deletions or rearrangements by southern analysis. We identified mutations in seven individuals. Of the remainder, three had maternal conditions that further expand the phenocopy group. Thus, this group might represent a proportion of the mutation-negative patients in previous studies. We extracted clinical information from all prior reports over the past decade and show that there are few distinguishing features on examination between these two groups of patients. This study supports heterogeneity for CDPX1-like phenotypes and sorting these out will help to define the biological pathway and genetic contributors.

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Section: Discussionmentioning

confidence: 99%

Clinical and molecular analysis of arylsulfatase E in patients with brachytelephalangic chondrodysplasia punctata

Nino

Matos-Miranda

Maeda

et al. 2008

American J of Med Genetics Pt A

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“…New targets of aPL antibodies were identified as lyso(bis)phosphatidic acid [218], sulfatides, acidic glycosphingolipids [219]. The contemporary concepts concerning some new mechanisms of induction of aPL antibodies and their antigenic targets are comprehensively reviewed by Valesini et al [2].…”

Section: Oxidative Stressmentioning

confidence: 99%

Some Recent Insights into the Prothrombogenic Mechanisms of Antiphospholipid Antibodies

Todorova¹,

Baleva

2007

CMC

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Antiphospholipid antibodies (aPL) are a heterogeneous group of autoantibodies, detected in the sera of patients with both autoimmune and various non-autoimmune diseases. They are also detected in subjects with no overt underlying disease - the primary antiphosphilipid syndrome (PAPS). High titers of APL are associated with arterial and venous thrombosis, recurrent fetal loss and thrombocytopenia. There have been many suggestions explaining the potential mechanisms of the procoagulant effect of aPL. These include endothelial cell (EC) activation; increased adhesion molecule expression; inhibition of EC prostacyclin release, increased leucocyte adhesion to EC, downregulation of thrombomodulin expression. APL induce the procoagulant activity of monocytes via increased tissue factor expression and directly stimulate platelet hyperactivity with resultant production of enhanced amounts of the proaggregatory molecule of TXA(2). In vitro studies show that prepro-endothelin-1 mRNA is induced by human monoclonal anticardiolipin antibodies and this might contribute to vasospasm, and, ultimately, to arterial occlusion. The hypercoagulable state in APS patients is associated with alterations in the protein C/S pathway. It is suggested that aPL may impair the protein C anticoagulant system. Acquired protein C and protein S deficiency is described in patients with APS. Beta2- glycoprotein I, (Beta2-GPI) a natural anticoagulant, is involved in the regulation of protein S anticoagulant activity by preventing the binding of protein S to C4b-binding protein. APL were shown to inhibit this effect of Beta2- GP I. As the group of aPL is very heterogeneous, it is unlikely that a single mechanism is responsible for the thrombogenic activity of all aPLs associated with thrombosis.

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“…APAbs can cross-react with antigenic mimicries such as sulfatides [26] that are abundant in gangliosides. A homology of sequences between beta2-glycoprotein I and some cerebellar antigens, such as HuB (Hel-N), HuD, HuC, CV2/CRMP5, Ri (ANNA2), Tr and mGluR1 antigen, has been shown [6].…”

Section: Discussionmentioning

confidence: 99%

Antiphospholipid Antibodies and Cerebellar Ataxia: A Clinical Analysis and Literature Review

Chen

Chui

et al. 2014

Neuroimmunomodulation

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Background: Although it has been established that antiphospholipid antibodies (APAbs) bind to and modulate the signaling of cerebellar neurons in vitro, the clinical correlation between increased APAbs and cerebellar ataxia has rarely been investigated. Methods: We reviewed 10 patients presenting with cerebellar ataxia with increased blood APAbs from our database along with 3 APAb-associated cerebellar ataxia patients in the literature. Results: Of these 10 patients, 4 exhibited a subacute onset of progressive ataxia, and there were no significant structural changes in their brains that appeared to be responsible for the symptoms. Another 6 showed a chronic course of ataxia, and shared similar morphological changes that included symmetrical lesions in bilateral hemispheres, periventricular lucency and central and temporal atrophy of varying severity; the cerebellum was spared. The predominant APAbs for subacute and chronic ataxia were the anti-beta₂-glycoprotein I antibody and anticardiolipin antibody, respectively. Cancer was found in 1 patient with subacute ataxia and in 4 with chronic ataxia. The removal of the cancer, the plasmapheresis and immunosuppressive therapy successfully abolished the ataxia and increased APAb levels in all 5 patients. Conclusions: The relation between APAbs and nonvascular neurological disorders, such as cerebellar ataxia, should be further studied. APAbs may mediate neurological deficits via different mechanisms such as structural damage or functional neurotoxicity. Clinically, the examination of blood APAb levels is recommended for patients with cerebellar ataxia without a determined cause, and the further survey of systemic cancers in the case of APAb positivity is also recommended. Finally, plasmapheresis is a reasonable and effective treatment for APAb-associated cerebellar ataxia.

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Sulfatides

Cited by 17 publications

References 26 publications

Clinical and molecular analysis of arylsulfatase E in patients with brachytelephalangic chondrodysplasia punctata

Clinical and molecular analysis of arylsulfatase E in patients with brachytelephalangic chondrodysplasia punctata

Some Recent Insights into the Prothrombogenic Mechanisms of Antiphospholipid Antibodies

Antiphospholipid Antibodies and Cerebellar Ataxia: A Clinical Analysis and Literature Review

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