Proteomic Profiling of Breast Tissue Collagens and Site-specific Characterization of Hydroxyproline Residues of Collagen Alpha-1-(I)

2012 ◽  
Vol 11 (12) ◽  
pp. 5890-5902 ◽  
Author(s):  
Helen Montgomery ◽  
Nitin Rustogi ◽  
Andreas Hadjisavvas ◽  
Koichi Tanaka ◽  
Kyriacos Kyriacou ◽  
...  
Keyword(s):  
Breast Tissue ◽  
Proteomic Profiling ◽  
Site Specific

Gelatin and Glycerine-Based Bioadhesive Vaginal Hydrogel

2020 ◽  
Vol 17 (4) ◽  
pp. 303-311
Author(s):  
Roberta Cassano ◽  
Federica Curcio ◽  
Delia Mandracchia ◽  
Adriana Trapani ◽  
Sonia Trombino
Keyword(s):  
Differential Scanning Calorimetry ◽  
Inflammatory Process ◽  
Vaginal Mucosa ◽  
Vaginal Infection ◽  
Scanning Calorimetry ◽  
Time Intervals ◽  
Site Specific ◽  
Release Studies ◽  
Hiv Seropositive

Aim: The work’s aim was the preparation and characterization of a hydrogel based on gelatin and glycerine, useful for site-specific release of benzydamine, an anti-inflammatory drug, able to attenuate the inflammatory process typical of the vaginal infection. Objective: The obtained hydrogel has been characterized by Electronic Scanning Microscopy (SEM) and Differential Scanning Calorimetry (DSC). In addition, due to the precursor properties, the hydrogel exhibits a relevant mucoadhesive activity. Methods: The swelling degree was evaluated at two different pHs and at defined time intervals. In particular, phosphate buffers were used at pH 6.6, in order to mimic the typical conditions of infectious diseases at the vaginal level, particularly for HIV-seropositive pregnant women, and pH 4.6, to simulate the physiological environment. Results: The obtained results revealed that the hydrogel swells up well at both pHs. Conclusion: Release studies conducted at both pathological and physiological pHs have shown that benzydamine is released at the level of the vaginal mucosa in a slow and gradual manner. These data support the hypothesis of the hydrogel use for the site-specific release of benzydamine in the vaginal mucosa.

scholarly journals Butyrophilin-like 2 regulates site-specific adaptations of intestinal γδ intraepithelial lymphocytes

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Casandra Panea ◽  
Ruoyu Zhang ◽  
Jeffrey VanValkenburgh ◽  
Min Ni ◽  
Christina Adler ◽  
...  
Keyword(s):  
Immune Responses ◽  
Intraepithelial Lymphocytes ◽  
Homeostatic Proliferation ◽  
Intestinal Epithelial ◽  
Intestinal Epithelial Barrier ◽  
Site Specific ◽  
Adaptive Immune ◽  
Intestinal Segments ◽  
Repertoire Diversity

AbstractTissue-resident γδ intraepithelial lymphocytes (IELs) orchestrate innate and adaptive immune responses to maintain intestinal epithelial barrier integrity. Epithelia-specific butyrophilin-like (Btnl) molecules induce perinatal development of distinct Vγ TCR+ IELs, however, the mechanisms that control γδ IEL maintenance within discrete intestinal segments are unclear. Here, we show that Btnl2 suppressed homeostatic proliferation of γδ IELs preferentially in the ileum. High throughput transcriptomic characterization of site-specific Btnl2-KO γδ IELs reveals that Btnl2 regulated the antimicrobial response module of ileal γδ IELs. Btnl2 deficiency shapes the TCR specificities and TCRγ/δ repertoire diversity of ileal γδ IELs. During DSS-induced colitis, Btnl2-KO mice exhibit increased inflammation and delayed mucosal repair in the colon. Collectively, these data suggest that Btnl2 fine-tunes γδ IEL frequencies and TCR specificities in response to site-specific homeostatic and inflammatory cues. Hence, Btnl-mediated targeting of γδ IEL development and maintenance may help dissect their immunological functions in intestinal diseases with segment-specific manifestations.

Proteomic Profiling and Functional Characterization of Multiple Post-Translational Modifications of Tubulin

2015 ◽  
Vol 14 (8) ◽  
pp. 3292-3304 ◽  
Author(s):  
Ningning Liu ◽  
Yun Xiong ◽  
Yiran Ren ◽  
Linlin Zhang ◽  
Xianfei He ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Proteomic Profiling ◽  
Post Translational Modifications

scholarly journals State-of-the-Art Native Mass Spectrometry and Ion Mobility Methods to Monitor Homogeneous Site-Specific Antibody-Drug Conjugates Synthesis

2021 ◽  
Vol 14 (6) ◽  
pp. 498
Author(s):  
Evolène Deslignière ◽  
Anthony Ehkirch ◽  
Bastiaan L. Duivelshof ◽  
Hanna Toftevall ◽  
Jonathan Sjögren ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Gas Phase ◽  
Ion Mobility ◽  
State Of The Art ◽  
Native Mass Spectrometry ◽  
Site Specific ◽  
Drug Conjugates ◽  
Conjugation Process ◽  
Antibody Drug

Antibody-drug conjugates (ADCs) are biotherapeutics consisting of a tumor-targeting monoclonal antibody (mAb) linked covalently to a cytotoxic drug. Early generation ADCs were predominantly obtained through non-selective conjugation methods based on lysine and cysteine residues, resulting in heterogeneous populations with varying drug-to-antibody ratios (DAR). Site-specific conjugation is one of the current challenges in ADC development, allowing for controlled conjugation and production of homogeneous ADCs. We report here the characterization of a site-specific DAR2 ADC generated with the GlyCLICK three-step process, which involves glycan-based enzymatic remodeling and click chemistry, using state-of-the-art native mass spectrometry (nMS) methods. The conjugation process was monitored with size exclusion chromatography coupled to nMS (SEC-nMS), which offered a straightforward identification and quantification of all reaction products, providing a direct snapshot of the ADC homogeneity. Benefits of SEC-nMS were further demonstrated for forced degradation studies, for which fragments generated upon thermal stress were clearly identified, with no deconjugation of the drug linker observed for the T-GlyGLICK-DM1 ADC. Lastly, innovative ion mobility-based collision-induced unfolding (CIU) approaches were used to assess the gas-phase behavior of compounds along the conjugation process, highlighting an increased resistance of the mAb against gas-phase unfolding upon drug conjugation. Altogether, these state-of-the-art nMS methods represent innovative approaches to investigate drug loading and distribution of last generation ADCs, their evolution during the bioconjugation process and their impact on gas-phase stabilities. We envision nMS and CIU methods to improve the conformational characterization of next generation-empowered mAb-derived products such as engineered nanobodies, bispecific ADCs or immunocytokines.

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