Anion transport function of mouse erythroid band 3 protein (AE1) does not require acylation of cysteine residue 861

Kang, Dongchon; Karbach, Doris; Passow, Hermann

doi:10.1016/0005-2736(94)90317-4

Cited by 19 publications

(10 citation statements)

References 12 publications

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“…In our previous work, we have shown that S-palm PLP peptides enhanced the development and chronicity of EAE and have suggested that naturally occurring Spalm PLP peptides generated as a consequence of myelin breakdown during MS may contribute to the chronic immune attack characteristic of this disease (9,34). In addition to MS, other common human autoimmune diseases, e.g., insulin-dependent diabetes mellitus and rheumatoid arthritis, have been linked to carriage of particular MHC class II molecules, and several wellcharacterized autoantigens are known to be thioacylated, e.g., GAD-65 (in insulin-dependent diabetes mellitus), P0 (autoimmune neuritis), erythrocyte band 3 (autoimmune hemolytic anemia), rhodopsin (autoimmune uveoretinitis), and myelinassociated glycoprotein (autoimmune sensory neuropathy) (35)(36)(37)(38)(39). We postulate that these Ags may be made more autoantigenic by the presence of the thioacyl chain.…”

Section: Discussionmentioning

confidence: 99%

Route of Uptake of Palmitoylated Encephalitogenic Peptides of Myelin Proteolipid Protein by Antigen-Presenting Cells: Importance of the Type of Bond between Lipid Chain and Peptide and Relevance to Autoimmunity

Pfender

Grosch

Roussel

et al. 2008

The Journal of Immunology

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Previously, we have shown that thiopalmitoylation of peptides of myelin proteolipid protein, as occurs naturally in vivo, increases their ability to induce experimental autoimmune encephalomyelitis, the animal model of multiple sclerosis, and skews the autoimmune response toward a CD4+-mediated response. In contrast, the same peptide, when synthesized with a stable amide bond between peptide and lipid, inhibits experimental autoimmune encephalomyelitis and skews the response toward a CD8+ response. The aim of the current study was to determine the mechanisms responsible for these observations. We show that proteolipid protein lipopeptides, when synthesized with a thioester bond between the lipid and the peptide, are taken up into APCs via an actin-independent endocytic route, the thioester bond is cleaved in the endosome, and the peptide is subsequently displayed on the surface of the APC in the context of MHC class II. The same peptide, when synthesized with the lipid attached via a stable amide bond, rapidly enters into the cytoplasm of the APC and forms micelles; however, the bond between peptide and lipid is not cleaved, and the micelles travel via the endoplasmic reticulum to complex with MHC class I. These findings have implications for vaccine development and for the development of MHC class II-restricted autoimmune diseases, as many human autoantigens thus far identified are thioacylated.

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Section: Discussionmentioning

confidence: 99%

Route of Uptake of Palmitoylated Encephalitogenic Peptides of Myelin Proteolipid Protein by Antigen-Presenting Cells: Importance of the Type of Bond between Lipid Chain and Peptide and Relevance to Autoimmunity

Pfender

Grosch

Roussel

et al. 2008

The Journal of Immunology

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“…For example, GAD-65, P0, erythrocyte band 3, and rhodopsin, putative autoantigens for insulin-dependent diabetes mellitus, autoimmune neuritis, autoimmune hemolytic anemia, and autoimmune uveoretinitis, respectively, are all thioacylated (51)(52)(53)(54). An increased uptake of thioacylated peptide Ags and/or increased activation of APC due to the presence of the thioacyl side chain might result in a greater tendency for autoreactivity to spread to thioacylated Ags.…”

Section: Discussionmentioning

confidence: 99%

Thiopalmitoylation of Myelin Proteolipid Protein Epitopes Enhances Immunogenicity and Encephalitogenicity

Greer

Denis

Sobel

et al. 2001

The Journal of Immunology

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Proteolipid protein (PLP) is the most abundant protein of CNS myelin, and is posttranslationally acylated by covalent attachment of long chain fatty acids to cysteine residues via a thioester linkage. Two of the acylation sites are within epitopes of PLP that are encephalitogenic in SJL/J mice (PLP104–117 and PLP139–151) and against which increased immune responses have been detected in some multiple sclerosis patients. It is known that attachment of certain types of lipid side chains to peptides can result in their enhanced immunogenicity. The aim of this study was to determine whether thioacylated PLP peptides, as occur in the native protein, are more immunogenic than their nonacylated counterparts, and whether thioacylation influences the development of autoreactivity and experimental autoimmune encephalomyelitis. The results show that in comparison with nonacylated peptides, thioacylated PLP lipopeptides can induce greater T cell and Ab responses to both the acylated and nonacylated peptides. They also enhanced the development and chronicity of experimental autoimmune encephalomyelitis. Synthetic peptides in which the fatty acid was attached via an amide linkage at the N terminus were not encephalitogenic, and they induced greater proportions of CD8+ cells in initial in vitro stimulation. Therefore, the lability and the site of the linkage between the peptide and fatty acid may be important for induction of encephalitogenic CD4+ T cells. These results suggest that immune responses induced by endogenous thioacylated lipopeptides may contribute to the immunopathogenesis of chronic experimental demyelinating diseases and multiple sclerosis.

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“…A cysteine residue (Cys916) at the putative intracellular end of TM12 is palmitoylated in the related transporter AE1 (698). However, this Cys residue is not necessary for the function or surface expression in heterologous systems of either AE1 (154,465) or NBCe1 (471).…”

Section: Iii) Tms 6 -14 (Subdomain 8)mentioning

confidence: 99%

The Divergence, Actions, Roles, and Relatives of Sodium-Coupled Bicarbonate Transporters

Parker

Boron

2013

Physiological Reviews

247

262

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The mammalian Slc4 (Solute carrier 4) family of transporters is a functionally diverse group of 10 multi-spanning membrane proteins that includes three Cl-HCO3 exchangers (AE1-3), five Na(+)-coupled HCO3(-) transporters (NCBTs), and two other unusual members (AE4, BTR1). In this review, we mainly focus on the five mammalian NCBTs-NBCe1, NBCe2, NBCn1, NDCBE, and NBCn2. Each plays a specialized role in maintaining intracellular pH and, by contributing to the movement of HCO3(-) across epithelia, in maintaining whole-body pH and otherwise contributing to epithelial transport. Disruptions involving NCBT genes are linked to blindness, deafness, proximal renal tubular acidosis, mental retardation, and epilepsy. We also review AE1-3, AE4, and BTR1, addressing their relevance to the study of NCBTs. This review draws together recent advances in our understanding of the phylogenetic origins and physiological relevance of NCBTs and their progenitors. Underlying these advances is progress in such diverse disciplines as physiology, molecular biology, genetics, immunocytochemistry, proteomics, and structural biology. This review highlights the key similarities and differences between individual NCBTs and the genes that encode them and also clarifies the sometimes confusing NCBT nomenclature.

show abstract

Anion transport function of mouse erythroid band 3 protein (AE1) does not require acylation of cysteine residue 861

Cited by 19 publications

References 12 publications

Route of Uptake of Palmitoylated Encephalitogenic Peptides of Myelin Proteolipid Protein by Antigen-Presenting Cells: Importance of the Type of Bond between Lipid Chain and Peptide and Relevance to Autoimmunity

Route of Uptake of Palmitoylated Encephalitogenic Peptides of Myelin Proteolipid Protein by Antigen-Presenting Cells: Importance of the Type of Bond between Lipid Chain and Peptide and Relevance to Autoimmunity

Thiopalmitoylation of Myelin Proteolipid Protein Epitopes Enhances Immunogenicity and Encephalitogenicity

The Divergence, Actions, Roles, and Relatives of Sodium-Coupled Bicarbonate Transporters

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