Sweat protein components tested by SDS-polyacrylamide gel electrophoresis followed by immunoblotting.

Nakayashiki, Nori

doi:10.1620/tjem.161.25

Cited by 27 publications

(18 citation statements)

References 15 publications

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“…We identified human serum albumin (band at 65 kDa) and the antimicrobial peptide DCD-1L (bands at 4 kDa), which both have already been described in sweat (18,12 (21) showed that the prolactin-inducible protein (15 kDa) is present in sweat glands. Psoriasin has been recently identified in keratinocytes (5).…”

Section: Identification Of Dominant Proteins In Human Eccrinementioning

confidence: 65%

“…Beside these antimicrobial peptides and proteins, the surface of human skin provides other proteins such as human serum albumin (18), cytokeratin I (19), Zn-␣2-glycoprotein (20), prolactin-inducible protein (21), and cystatin A (22,23). Additionally certain proteases have been described in human sweat such as gelatinolytic and caseinolytic proteases (24), cathepsin B-and H-like cysteine proteases (25), human stratum corneum chymotryptic enzyme (26), and tissue kallikrein and kininase II (27).…”

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confidence: 99%

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Cathepsin D Is Present in Human Eccrine Sweat and Involved in the Postsecretory Processing of the Antimicrobial Peptide DCD-1L

Baechle

Flad

Cansier

et al. 2006

Journal of Biological Chemistry

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The protein pattern of healthy human eccrine sweat was investigated and 10 major proteins were detected from which apolipoprotein D, lipophilin B, and cathepsin D (CatD) were identified for the first time in human eccrine sweat. We focused our studies on the function of the aspartate protease CatD in sweat. In vitro digestion experiments using a specific fluorescent CatD substrate showed that CatD is enzymatically active in human sweat. To identify potential substrates of CatD in human eccrine sweat LL-37 and DCD-1L, two antimicrobial peptides present in sweat, were digested in vitro with purified CatD. LL-37 was not significantly digested by CatD, whereas DCD-1L was cleaved between Leu 44 and Asp 45 and between Leu 29 and Glu 30 almost completely. The DCD-1L-derived peptides generated in vitro by CatD were also found in vivo in human sweat as determined by surface-enhanced laser desorption/ionization (SELDI) mass spectrometry. Furthermore, besides the CatD-processed peptides we identified additionally DCD-1L-derived peptides that are generated upon cleavage with a 1,10-phenanthroline-sensitive carboxypeptidase and an endoprotease. Taken together, proteolytic processing generates 12 DCD-1L-derived peptides. To elucidate the functional significance of postsecretory processing the antimicrobial activity of three CatDprocessed DCD-1L peptides was tested. Whereas two of these peptides showed no activity against Gram-positive and Gram-negative bacteria, one DCD-1L-derived peptide showed an even higher activity against Escherichia coli than DCD-1L. Functional analysis indicated that proteolytic processing of DCD-1L by CatD in human sweat modulates the innate immune defense of human skin.

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Section: Identification Of Dominant Proteins In Human Eccrinementioning

confidence: 65%

mentioning

confidence: 99%

Cathepsin D Is Present in Human Eccrine Sweat and Involved in the Postsecretory Processing of the Antimicrobial Peptide DCD-1L

Baechle

Flad

Cansier

et al. 2006

Journal of Biological Chemistry

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“…ZAG has been identified as a biomarker associated with multiple diseases, including prostate, bladder, and breast cancer (3,6,7 ). Therefore, ZAG concentrations by themselves are unlikely to be a specific screening test for any targeted disease, such as PCa.…”

Section: Discussionmentioning

confidence: 99%

“…Biochemically, ZAG stimulates lipid degeneration in adipocytes and appears to be involved in cachexia, a wasting syndrome that can affect people with cancer, AIDS, and other terminal illnesses (3,4 ). ZAG appears naturally in most body fluids, such as blood (5 ), sweat (6 ), seminal fluid (7 ), breast cyst fluid (8 ), cerebrospinal fluid (9 ), and urine (10 ) and is also found in secretory epithelial cells of the liver and the gastrointestinal tract (11 ).…”

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confidence: 99%

LC-MS/MS Quantification of Zn-α2 Glycoprotein: A Potential Serum Biomarker for Prostate Cancer

et al. 2007

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Background: Zn-␣2 glycoprotein (ZAG) is a relatively abundant glycoprotein that has potential as a biomarker for prostate cancer. We present a high-flow liquid chromatography-tandem mass spectrometry (LC-MS/MS) method for measuring serum ZAG concentrations by proteolytic cleavage of the protein and quantification of a unique peptide. Methods: We selected the ZAG tryptic peptide 147 EI-PAWVPEDPAAQITK 162 as the intact protein for quantification and used a stable isotope-labeled synthetic peptide with this sequence as an internal standard. Standards using recombinant ZAG in bovine serum albumin, 50 g/L, and a pilot series of patient sera were denatured, reduced, alkylated, and digested with trypsin. The concentration of ZAG was calculated from a dose-response curve of the ratio of the relative abundance of the ZAG tryptic peptide to internal standard.

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“…Approximately 40% of the body's extravasal HSA content is located within the skin, which is 2-fold more concentrated per weight than in muscle. Both, the presence of HSA in sweat (14,51) and the changes in human skin during hydration, indicate its bidirectional trafficking through the epidermal basement membrane (19).…”

Section: Discussionmentioning

confidence: 99%

Metal-Protein Complex-Mediated Transport and Delivery of Ni2+ to TCR/MHC Contact Sites in Nickel-Specific Human T Cell Activation

Thierse

Moulon

Allespach

et al. 2004

The Journal of Immunology

100

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Nickel allergy clearly involves the activation of HLA-restricted, skin-homing, Ni-specific T cells by professional APCs. Nevertheless, knowledge concerning the molecular details of metal-protein interactions underlying the transport and delivery of metal ions to APC during the early sensitization phase and their interactions with HLA and TCRs is still fragmentary. This study investigates the role of human serum albumin (HSA), a known shuttling molecule for Ni2+ and an often-disregarded, major component of skin, in these processes. We show that Ni-saturated HSA complexes (HSA-Ni) induce and activate Ni-specific human T cells as potently as Ni salt solutions when present at equimolar concentrations classically used for in vitro T cell stimulation. However, neither HSA itself nor its Ni-binding N-terminal peptide are involved in determining the specificity of antigenic determinants. In fact, HSA could be replaced by xenogeneic albumins exhibiting sufficient affinity for Ni2+ as determined by surface plasmon resonance (Biacore technology) or atomic absorption spectroscopy. Moreover, despite rapid internalization of HSA-Ni by APC, it was not processed into HLA-associated epitopes recognizable by Ni-specific T cells. In contrast, the presence of HSA-Ni in the vicinity of transient contacts between TCR and APC-exposed HLA molecules appeared to facilitate a specific transfer of Ni2+ from HSA to high-affinity coordination sites created at the TCR/HLA-interface.

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Sweat protein components tested by SDS-polyacrylamide gel electrophoresis followed by immunoblotting.

Cited by 27 publications

References 15 publications

Cathepsin D Is Present in Human Eccrine Sweat and Involved in the Postsecretory Processing of the Antimicrobial Peptide DCD-1L

Cathepsin D Is Present in Human Eccrine Sweat and Involved in the Postsecretory Processing of the Antimicrobial Peptide DCD-1L

LC-MS/MS Quantification of Zn-α2 Glycoprotein: A Potential Serum Biomarker for Prostate Cancer

Metal-Protein Complex-Mediated Transport and Delivery of Ni2+ to TCR/MHC Contact Sites in Nickel-Specific Human T Cell Activation

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