Two-dimensional mapping and microsequencing of lysosomal proteins from human placenta

Chataway, Tim; Whittle, Alison M.; Lewis, Martin; Bindloss, Colleen A.; Davey, Richard; Moritz, Robert L.; Simpson, Richard J.; Hopwood, John J.; Meikle, Peter J.

doi:10.1016/s0143-4004(98)90026-1

Cited by 16 publications

(9 citation statements)

References 60 publications

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“…If the S-palm peptides enter the cell by endocytic mechanisms involving passage through lysosomes, then it would be expected that the acyl groups would be removed from the peptides by palmitoyl protein thioesterases, which are a major component of the lysosome (29). However, it has recently been shown that small hydrophobic or lipid-containing molecules can enter macrophages via several other pathways (reviewed in Ref.…”

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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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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“…This discrepancy may be due to the method of protein detection as most of these studies rely upon the fact that the majority of lysosomal hydrolases are targeted to the lysosome by the mannose 6-phosphate (M6P) pathway [for more details, see review in Ref. (110)], and therefore have utilized immobilized M6P-receptors as a purification method (111–120). Consequently, with the exception of one study (120), proteins trafficked to the lysosome by M6P-independent mechanisms are missing from these data sets.…”

Section: Hyaluronan Catabolism and Generation Of Ha Fragmentsmentioning

confidence: 99%

Hyaluronan, a Crucial Regulator of Inflammation

2014

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Hyaluronan (HA), a major component of the extracellular matrix (ECM), plays a key role in regulating inflammation. Inflammation is associated with accumulation and turnover of HA polymers by multiple cell types. Increasingly through the years, HA has become recognized as an active participant in inflammatory, angiogenic, fibrotic, and cancer promoting processes. HA and its binding proteins regulate the expression of inflammatory genes, the recruitment of inflammatory cells, the release of inflammatory cytokines, and can attenuate the course of inflammation, providing protection against tissue damage. A growing body of evidence suggests the cell responses are HA molecular weight dependent. HA fragments generated by multiple mechanisms throughout the course of inflammatory pathologies, elicit cellular responses distinct from intact HA. This review focuses on the role of HA in the promotion and resolution of inflammation.

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“…Fractionation of a proteome into subproteomes is based on the macromolecular architecture of the cell, including subcellular compartments, organelles, macromolecular structures, and multiprotein complexes (Jung et al, 2000a). To date, 2D electrophoresis reference maps have been constructed for speci®c organelles, including mitochondria, lysosomes, peroxisomes, endoplasmic reticulum, Golgi apparatus, and nucleus (Bell et al, 2001;Chataway et al, 1998;Fialka et al, 1999;Jung et al, 2000b;Rabilloud et al, 1998;Taylor et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Analysis of the Arabidopsis nuclear proteome and its response to cold stress

Bae¹,

Cho²,

et al. 2003

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These authors contributed equally to the work. SummaryThe nucleus is the subcellular organelle that contains nearly all the genetic information required for the regulated expression of cellular proteins. In this study, we comprehensively characterized the Arabidopsis nuclear proteome. Nuclear proteins were isolated and analyzed using two-dimensional (2D) gel electrophoresis and matrix-assisted laser desorption/ionization time-of-¯ight mass spectrometry (MALDI-TOF MS). Approximately 500±700 spots were detected in reference 2D gels of nuclear proteins. Proteomic analyses led to the identi®cation of 184 spots corresponding to 158 different proteins implicated in a variety of cellular functions. We additionally analyzed the changes in the nuclear proteome in response to cold stress. Of the 184 identi®ed proteins, 54 were up-or downregulated with a greater than twofold change in response to cold treatment. Among these, six proteins were selected for further characterization. Northern analysis data revealed that gene expression of these proteins was also altered by cold stress. Following transient expression in BY-2 protoplasts, two proteins were detected in both the cytoplasm and the nucleus and four others were detected exclusively in the nucleus, which correlates well with the nuclear localization patterns of the proteomic data. Our study provides an initial insight into the Arabidopsis nuclear proteome and its response to cold stress.

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Two-dimensional mapping and microsequencing of lysosomal proteins from human placenta

Cited by 16 publications

References 60 publications

Thiopalmitoylation of Myelin Proteolipid Protein Epitopes Enhances Immunogenicity and Encephalitogenicity

Thiopalmitoylation of Myelin Proteolipid Protein Epitopes Enhances Immunogenicity and Encephalitogenicity

Hyaluronan, a Crucial Regulator of Inflammation

Analysis of the Arabidopsis nuclear proteome and its response to cold stress

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