Rapid confirmation and revision of the primary structure of bovine serum albumin by ESIMS and frit-FAB LC/MS

Hirayama, Kazuo; Akashi, Satoko; Furuya, Mami; Fukuhara, Ken-ichi

doi:10.1016/s0006-291x(05)80083-x

Cited by 523 publications

(270 citation statements)

References 19 publications

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“…Thus, after the desolva- tion procedure the nanoparticles were crosslinked, per milligram HSA, with 0.235, 0.588 or 1.175 l of an aqueous 8% glutaraldehyde solution. These glutaraldehyde concentrations equal 40, 100 and 200% of the calculated amount necessary for the quantitative crosslinking of the 59 ε-amino groups of lysine in the HSA molecules of the particle matrix (Hirayama et al, 1990;Carter and Ho, 1994). Whereas no influence of the crosslinking conditions on the resulting particle size was observed (Fig.…”

Section: Stability and Surface Charge Of The Nanoparticlesmentioning

confidence: 89%

Optimization of the preparation process for human serum albumin (HSA) nanoparticles

Langer¹,

Balthasar²,

Vogel³

et al. 2003

International Journal of Pharmaceutics

661

491

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Section: Stability and Surface Charge Of The Nanoparticlesmentioning

confidence: 89%

Optimization of the preparation process for human serum albumin (HSA) nanoparticles

Langer¹,

Balthasar²,

Vogel³

et al. 2003

International Journal of Pharmaceutics

661

491

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“…Enhancement of cross-presentation was a specific feature of rhuHsp70 as BSA, a protein with similar molecular weight and solubility (51), was unable to enhance cross-presentation under these conditions. Surface plasmon resonance spectroscopy (Biacore) confirmed that rhuHsp70 but not BSA bound to b-pep70-MART-1 peptide (not shown).…”

Section: Rhuhsp70 Enhances Cross-presentation Of Exogenous Tumor Antimentioning

confidence: 99%

Human Heat Shock Protein 70 Enhances Tumor Antigen Presentation through Complex Formation and Intracellular Antigen Delivery without Innate Immune Signaling

Bendz

Ruhland

Pandya

et al. 2007

Journal of Biological Chemistry

120

105

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Heat shock proteins (HSPs) have shown promise for the optimization of protein-based vaccines because they can transfer exogenous antigens to dendritic cells and at the same time induce their maturation. Great care must be exercised in interpretating HSP-driven studies, as by-products linked to the recombinant generation of these proteins have been shown to mediate immunological effects. We generated highly purified human recombinant Hsp70 and demonstrated that it strongly enhances the cross-presentation of exogenous antigens resulting in better antigen-specific T cell stimulation. Augmentation of T cell stimulation was a direct function of the degree of complex formation between Hsp70 and peptides and correlated with improved antigen delivery to endosomal compartments. The Hsp70 activity was independent of TAP proteins and was not inhibited by exotoxin A or endosomal acidification. Consequently, Hsp70 enhanced cross-presentation of various antigenic sequences, even when they required different post-uptake processing and trafficking, as exemplified by the tumor antigens tyrosinase and Melan-A/MART-1. Furthermore, Hsp70 enhanced cross-presentation by different antigen-presenting cells (APCs), including dendritic cells and B cells. Importantly, enhanced cross-presentation and antigen-specific T cell activation were observed in the absence of innate signals transmitted by Hsp70. As Hsp70 supports the cross-presentation of different antigens and APCs and is inert to APC function, it may show efficacy in various settings of immune modulation, including induction of antigen-specific immunity or tolerance.Cytotoxic CD8 T cells have an essential role in cellular immunity in that they destroy infected or malignantly transformed cells. They are activated by the recognition of complexes of major histocompatibility complex (MHC) 4 class I and antigenic peptides present on the surface of antigen-presenting cells (APC). Conventionally, the antigenic peptides presented by MHC class I are derived from endogenous cytosolic antigens. In specialized situations, MHC class I molecules additionally present peptides derived from exogenous antigens. This noncanonical MHC class I presentation, which is referred to as cross-presentation, requires that the exogenous antigen is internalized by APCs, subsequently enzymatically processed into peptides, and channeled into the MHC class I loading pathway (1, 2). Cross-presentation is crucial for the generation of CD8 T cell responses against antigens that are not endogenously produced by APCs, such as tumor antigens and pathogen-derived proteins. In an applied setting, cross-presentation is the required pathway for the generation of protein-based vaccines that are intended to stimulate antigen-specific CD8 responses. Critical parameters that define the efficacy of a vaccine are the amount of delivered antigen and the context in which the antigen is presented to the T cells. As the physiological capacity of APCs to cross-present antigen is generally low (3), there is significant interest to de...

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“…Correlations between independent spectral data (elements, C 1s peak components) were used to validate peak decomposition and component assignment, and to identify useful markers for the determination of surface molecular composition. Therefore reference data were deduced from the amino acid sequence of BSA (Hirayama et al, 1990) and are presented in Supporting Material. They concern the elemental composition as well as the chemical functions associated with the components of the C 1s and O 1s peaks and their concentrations.…”

Section: Surface Compositionmentioning

confidence: 99%

Conditioning materials with biomacromolecules: Composition of the adlayer and influence on cleanability

Toure

Genet

Dupont‐Gillain

et al. 2014

Journal of Colloid and Interface Science

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AbbreviationsBSA: bovine serum albumin RFC: radial flow cell XPS: X-ray photoelectron spectroscopy 2 ABSTRACTThe influence of substrate hydrophobicity and biomacromolecules (dextran, bovine serum albumin -BSA) adsorption on the cleanability of surfaces soiled by spraying aqueous suspensions of quartz particles (10 to 30 µm size), then dried, was investigated using glass and polystyrene as substrates. The cleanability was evaluated using radial flow cell (RFC).The surface composition was determined by X-ray photoelectron spectroscopy (XPS). The interpretation of XPS data allowed the complexity due to the ubiquitous presence of organic contaminants to be coped with, and the surface composition to be expressed in terms of both the amount of adlayer and the mass concentration of adlayer constituents.When soiled with a suspension of particles in water, glass was much less cleanable than polystyrene, which was attributed to its much lower water contact angle, in agreement with previous observations on starch soil. Dextran was easily desorbed and did not affect the cleanability. The presence of BSA at the interface strongly improved the cleanability of glass while the contact angle did not change appreciably. In contrast, soiling polystyrene with quartz particles suspended in a BSA solution instead of water did not change markedly the cleanability, while the contact angle was much lower and the aggregates of soiling particles were more flat. These observations are explained by the major role of capillary forces developed upon drying, which influence the closeness of the contact between the soiling particles and the substrate and, thereby, the adherence of particles. The capillary forces are proportional to the liquid surface tension and depend in a more complex way on contact angles of the particles and of the substrate. The dependence of cleanability on capillary forces, and in particular on the liquid surface tension, is predominant as compared with its dependence on the size and shape of the soiling aggregates, which influence the efficiency of shear forces exerted by the flowing water upon cleaning.

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Rapid confirmation and revision of the primary structure of bovine serum albumin by ESIMS and frit-FAB LC/MS

Cited by 523 publications

References 19 publications

Optimization of the preparation process for human serum albumin (HSA) nanoparticles

Optimization of the preparation process for human serum albumin (HSA) nanoparticles

Human Heat Shock Protein 70 Enhances Tumor Antigen Presentation through Complex Formation and Intracellular Antigen Delivery without Innate Immune Signaling

Conditioning materials with biomacromolecules: Composition of the adlayer and influence on cleanability

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