Quantitative Proteomics of the Human Skin Secretome Reveal a Reduction in Immune Defense Mediators in Ectodermal Dysplasia Patients

Burian, Marc; Velić, Ana; Matic, Katarina; Günther, Stephanie; Kraft, Beatrice; Gonser, Lena; Forchhammer, Stephan; Tiffert, Yvonne; Naumer, Christian; Krohn, Michael; Berneburg, Mark; Yazdi, Amir S.; Maček, Boris; Schittek, Birgit

doi:10.1038/jid.2014.462

Cited by 27 publications

(25 citation statements)

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“…Sweat also contains several complex biomolecules such as proteolytic enzymes and antimicrobial peptides (Calderó n-Santiago et al, 2014). Effector molecules in sweat play an essential role in crosstalk between skin cells and commensal microbiota and are involved in local immune homeostasis (Burian et al, 2015;Naik et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

Proteomic Profiling of Sweat Exosome Suggests its Involvement in Skin Immunity

Liu

2018

Journal of Investigative Dermatology

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Healthy human skin sustains an effective immune defense mechanism, formed by a complex physical and chemical epidermal barrier that coordinates with different cellular components of the skin immune system. However, the mechanism by which skin cells regulate local immune homeostasis in health and disease contexts is not well known. To investigate whether exosomes exist in sweat, sweat samples from healthy individuals were collected after aerobic exercise. Sweat exosome was isolated via differential ultracentrifugation, observed under transmission electron microscopy, measured by dynamic light scattering, and confirmed by immunoblot. Further, shotgun liquid chromatography (LC)-mass spectrometry (MS)/MS analysis was conducted to investigate the proteomic profiling of sweat exosome. Secreted exosome was detected in human sweat. A total of 1,062 proteins were identified in sweat exosome, including 997 different proteins compared with sweat proteomics and 896 unique proteins compared with urine, saliva, and plasma exosomes. Diverse antimicrobial peptides and immunological factors were found in sweat exosome, suggesting the involvement of exosome in skin immunity. This study provides direct evidence that secreted exosomes exist in human sweat. The proteomic profiling of sweat exosome provides insight into sweat features and the potential physiological significance of exosomes in immune homeostasis.

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Section: Introductionmentioning

confidence: 99%

Proteomic Profiling of Sweat Exosome Suggests its Involvement in Skin Immunity

Liu

2018

Journal of Investigative Dermatology

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“…Currently, intense research efforts are being carried out to discover new diagnostic, prognostic and predictive biomarkers in samples which are easily obtainable from patients using non‐invasive methods. Recent advances in analytical techniques now allow thorough analysis of human sweat proteins, hence, facilitating sweat biomarker studies …”

Section: Introductionmentioning

confidence: 99%

“…Recent advances in analytical techniques now allow thorough analysis of human sweat proteins, hence, facilitating sweat biomarker studies. 13,14 Label-free quantification of proteins with mass spectrometry is a powerful and sensitive method for protein identification and relative quantification. The protein digests are introduced into high precision mass spectrometers where MS/MS spectra are recorded.…”

Section: Introductionmentioning

confidence: 99%

Highly abundant defense proteins in human sweat as revealed by targeted proteomics and label‐free quantification mass spectrometry

Csősz

Emri

Kalló

et al. 2015

Acad Dermatol Venereol

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BACKGROUND The healthy human skin with its effective antimicrobial defense system forms an efficient barrier against invading pathogens. There is evidence suggesting that the composition of this chemical barrier varies between diseases, making the easily-collected sweat an ideal candidate for biomarker discoveries. OBJECTIVE Our aim was to provide information about the normal composition of the sweat, and to study the chemical barrier found at the surface of skin. METHODS Sweat samples from healthy individuals were collected during sauna bathing, and the global protein panel was analyzed by label-free mass spectrometry. SRM-based targeted proteomic methods were designed and stable isotope labeled reference peptides were used for method validation. RESULTS 95 sweat proteins were identified, 20 of them were novel proteins. It was shown that dermcidin is the most abundant sweat protein, and along with apolipoprotein D, clusterin, prolactin inducible protein and serum albumin, they make up 91% of secreted sweat proteins. The roles of these highly abundant proteins were reviewed; all of which have protective functions, highlighting the importance of sweat glands in composing the first line of innate immune defense system, and maintaining the epidermal barrier integrity. CONCLUSION Our findings in regards to the proteins forming the chemical barrier of the skin as determined by label free quantification and targeted proteomics methods are in accordance with previous studies, and can be further used as a starting point for non-invasive sweat biomarker research.

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“…20 μg of total protein extracts were run in a 12% pre-cast acrylamide gel at 100V for 20 min, and total protein bands were excised from the gel. Gel slices were digested as described previously 71 . Peptide mixtures were then separated on an EasyLC nano-HPLC (Proxeon Biosystems) coupled to an LTQ Orbitrap Elite mass spectrometer (Thermo Fisher Scientific) as described elsewhere 72 with the following modifications: peptides were eluted with an 130-min segmented gradient of 5–33-90% HPLC solvent B (80% acetonitrile in 0.5% acetic acid).…”

Section: Methodsmentioning

confidence: 99%

A temperature-dependent translational switch controls biofilm development inVibrio cholerae

Santos

Blake

Sit

et al. 2020

Preprint

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16The gastrointestinal pathogen Vibrio cholerae frequently forms biofilms during its life 17 cycle. Biofilm formation is vital for protection against environmental stresses and is 18 thought to facilitate intestinal colonization. Adaptation to temperature is crucial for V. 19 cholerae survival, as the pathogen is exposed to seasonal temperature variations in 20 the aquatic environment, and temperature fluctuations during host-environment 21 transitions. Here, we show that V. cholerae strains naturally lacking the master biofilm 22 transcriptional regulator HapR are unable to develop colony rugosity at low 23 temperatures. We find that BipA, a ribosome-associated GTPase, accounts for this 24 temperature-dependent control of biofilm formation by repressing translation of the 25 primary biofilm transcriptional activators VpsR and VpsT at low temperatures. In vitro 26 studies demonstrate that low temperatures influence BipA structural conformation and 27 decrease its sensitivity to proteolysis. Proteomic analyses reveal that BipA exerts 28 temperature-dependent control over >200 proteins in V. cholerae involved in a 29 multitude of cell processes, including biofilm assembly. Our study reveals a 30 remarkable new facet of the complex V. cholerae biofilm regulatory cascade and 31suggests that combined transcriptional-translational control could be a common 32 mechanism by which bacteria adapt to environmental flux.A common strategy of bacteria for adaptation and survival to changing environmental 35 conditions is the formation of biofilms: bacterial communities enclosed in an 36 extracellular matrix. Vibrio cholerae, the causative agent of the severe diarrhoeal 37 disease cholera, forms biofilms both in biotic and abiotic surfaces in the aquatic 38 environment that inhabits 1-3 and also in the intestine of the human host 4,5 . The 39 formation of biofilms enhances persistence of V. cholerae, since it provides protection 40 against environmental insults, predators and stress conditions and allows a better 41 access to nutrients 3 . There is some evidence indicating that biofilm-formation capacity 42 is critical for intestinal colonization 5 and biofilms have also been linked to a 43 hyperinfectious phenotype 6 . 44V. cholerae's biofilm is primarily composed of VPS (Vibrio polysaccharide), matrix 45 proteins (RbmA, RbmC and Bap1) and extracellular DNA 7-13 . The genes encoding the 46 activities for the production of VPS, grouped in the vpsI and vpsII clusters, and the 47 genes encoding the RbmA and RbmC matrix proteins, located in the rbm cluster 48 between vpsI and vpsII clusters, form the so-called V. cholerae biofilm-matrix cluster 49 (VcBMC) 7-10 . 50 Biofilm formation inVibrio cholerae is a highly regulated process, controlled by the 51 transcriptional activators VpsR, VpsT and AphA, the transcriptional repressors HapR 52 and H-NS, small regulatory RNAs, alternative sigma factors (RpoS, RpoN and RpoE), 53 and small nucleotide signalling (c-di-GMP, cAMP, ppGpp). Specific environmental 54 signals such as changes...

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Quantitative Proteomics of the Human Skin Secretome Reveal a Reduction in Immune Defense Mediators in Ectodermal Dysplasia Patients

Cited by 27 publications

References 40 publications

Proteomic Profiling of Sweat Exosome Suggests its Involvement in Skin Immunity

Proteomic Profiling of Sweat Exosome Suggests its Involvement in Skin Immunity

Highly abundant defense proteins in human sweat as revealed by targeted proteomics and label‐free quantification mass spectrometry

A temperature-dependent translational switch controls biofilm development inVibrio cholerae

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