Proteomic and peptidomic analysis of human sweat with emphasis on proteolysis

Journal of Proteomics

Volumn 155, Issue , 2017, Pages 40-48

  Yu, Yijing ^a,b   Prassas, Ioannis ^b   Muytjens, Carla M J ^a,b   Diamandis, Eleftherios P ^a,b,c  

^a UNIVERSITY OF TORONTO   (Canada)

^b MOUNT SINAI HOSPITAL   (Canada)

^c UNIVERSITY HEALTH NETWORK   (Canada)

Author keywords

Endogenous peptides; Mass spectrometry; Peptidomics; Protease; Proteomics; Sweat

Indexed keywords

BIOLOGICAL MARKER; PEPTIDE; PEPTIDOME; POLYPEPTIDE ANTIBIOTIC AGENT; PROTEINASE; PROTEINASE INHIBITOR; PROTEOME; UNCLASSIFIED DRUG; ANTIMICROBIAL CATIONIC PEPTIDE;

ADULT; AMINO ACID SEQUENCE; ANTIMICROBIAL ACTIVITY; APOCRINE GLAND; ARTICLE; BIOINFORMATICS; CATALYSIS; ECCRINE GLAND; EXERCISE; FEMALE; HUMAN; INNATE IMMUNITY; ION EXCHANGE CHROMATOGRAPHY; MALE; MASS SPECTROMETRY; NORMAL HUMAN; PEPTIDOMICS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEOMICS; SKIN; SWEAT; THERMOREGULATION; METABOLISM; MIDDLE AGED;

ADULT; ANTIMICROBIAL CATIONIC PEPTIDES; FEMALE; HUMANS; MALE; MIDDLE AGED; PROTEOLYSIS; PROTEOME; PROTEOMICS; SWEAT;

EID: 85010443325     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2017.01.005     Document Type: Article

References (52)

1. [1] Murota, H., Matsui, S., Ono, E., Kijima, A., Kikuta, J., Ishii, M., Katayama, I., Sweat, the driving force behind normal skin: an emerging perspective on functional biology and regulatory mechanisms. J. Dermatol. Sci. 77:1 (2015), 3–10.
2. [2] Burian, M., Velic, A., Matic, K., Gunther, S., Kraft, B., Gonser, L., Forchhammer, S., Tiffert, Y., Naumer, C., Krohn, M., Berneburg, M., Yazdi, A.S., Macek, B., Schittek, B., Quantitative proteomics of the human skin secretome reveal a reduction in immune defense mediators in ectodermal dysplasia patients. J. Investig. Dermatol. 135:3 (2015), 759–767.
3. [3] Raiszadeh, M.M., Ross, M.M., Russo, P.S., Schaepper, M.A., Zhou, W., Deng, J., Ng, D., Dickson, A., Dickson, C., Strom, M., Osorio, C., Soeprono, T., Wulfkuhle, J.D., Petricoin, E.F., Liotta, L.A., Kirsch, W.M., Proteomic analysis of eccrine sweat: implications for the discovery of schizophrenia biomarker proteins. J. Proteome Res. 11:4 (2012), 2127–2139.
4. [4] Mark, H., Harding, C.R., Amino acid composition, including key derivatives of eccrine sweat: potential biomarkers of certain atopic skin conditions. Int. J. Cosmet. Sci. 35:2 (2013), 163–168.
5. [5] Wagener, J.S., Zemanick, E.T., Sontag, M.K., Newborn screening for cystic fibrosis. Curr. Opin. Pediatr. 24:3 (2012), 329–335.
6. [6] Calderon-Santiago, M., Priego-Capote, F., Turck, N., Robin, X., Jurado-Gamez, B., Sanchez, J.C., Luque de Castro, M.D., Human sweat metabolomics for lung cancer screening. Anal. Bioanal. Chem. 407:18 (2015), 5381–5392.
7. [7] De Giovanni, N., Fucci, N., The current status of sweat testing for drugs of abuse: a review. Curr. Med. Chem. 20:4 (2013), 545–561.
8. [8] Park, J.H., Park, G.T., Cho, I.H., Sim, S.M., Yang, J.M., Lee, D.Y., An antimicrobial protein, lactoferrin exists in the sweat: proteomic analysis of sweat. Exp. Dermatol. 20:4 (2011), 369–371.
9. [9] Csosz, E., Emri, G., Kallo, G., Tsaprailis, G., Tozser, J., Highly abundant defense proteins in human sweat as revealed by targeted proteomics and label-free quantification mass spectrometry. J. Eur. Acad. Dermatol. Venereol. 29:10 (2015), 2024–2031.
10. [10] Adewole, O.O., Erhabor, G.E., Adewole, T.O., Ojo, A.O., Oshokoya, H., Wolfe, L.M., Prenni, J.E., Proteomic profiling of eccrine sweat reveals its potential as a diagnostic biofluid for active tuberculosis. Proteomics Clin. Appl. 10:5 (2016), 547–553.
11. [11] Dallas, D.C., Guerrero, A., Parker, E.A., Robinson, R.C., Gan, J., German, J.B., Barile, D., Lebrilla, C.B., Current peptidomics: applications, purification, identification, quantification, and functional analysis. Proteomics 15:5–6 (2015), 1026–1038.
12. [12] Dai, X., Okazaki, H., Hanakawa, Y., Murakami, M., Tohyama, M., Shirakata, Y., Sayama, K., Eccrine sweat contains IL-1alpha, IL-1beta and IL-31 and activates epidermal keratinocytes as a danger signal. PLoS One, 8(7), 2013, e67666.
13. [13] Bauca, J.M., Martinez-Morillo, E., Diamandis, E.P., Peptidomics of urine and other biofluids for cancer diagnostics. Clin. Chem. 60:8 (2014), 1052–1061.
14. [14] Bery, A., Leung, F., Smith, C.R., Diamandis, E.P., Kulasingam, V., Deciphering the ovarian cancer ascites fluid peptidome. Clin. Proteomics, 11(1), 2014, 13.
15. [15] Yu, Y., Prassas, I., Dimitromanolakis, A., Diamandis, E.P., Novel biological substrates of human kallikrein 7 identified through degradomics. J. Biol. Chem. 290:29 (2015), 17762–17775.
16. [16] Cretu, D., Prassas, I., Saraon, P., Batruch, I., Gandhi, R., Diamandis, E.P., Chandran, V., Identification of psoriatic arthritis mediators in synovial fluid by quantitative mass spectrometry. Clin. Proteomics, 11(1), 2014, 27.
17. [17] Waghu, F.H., Gopi, L., Barai, R.S., Ramteke, P., Nizami, B., Idicula-Thomas, S., CAMP: collection of sequences and structures of antimicrobial peptides. Nucleic Acids Res. 42:Database issue (2014), D1154–D1158.
18. [18] de Veer, S.J., Furio, L., Harris, J.M., Hovnanian, A., Proteases and proteomics: cutting to the core of human skin pathologies. Proteomics Clin. Appl. 8:5–6 (2014), 389–402.
19. [19] Prassas, I., Eissa, A., Poda, G., Diamandis, E.P., Unleashing the therapeutic potential of human kallikrein-related serine proteases. Nat. Rev. Drug Discov. 14:3 (2015), 183–202.
20. [20] Goettig, P., Magdolen, V., Brandstetter, H., Natural and synthetic inhibitors of kallikrein-related peptidases (KLKs). Biochimie 92:11 (2010), 1546–1567.
21. [21] Prassas, I., Chrystoja, C.C., Makawita, S., Diamandis, E.P., Bioinformatic identification of proteins with tissue-specific expression for biomarker discovery. BMC. Med., 10, 2012, 39.
22. [22] Edqvist, P.H., Fagerberg, L., Hallstrom, B.M., Danielsson, A., Edlund, K., Uhlen, M., Ponten, F., Expression of human skin-specific genes defined by transcriptomics and antibody-based profiling. J. Histochem. Cytochem. 63:2 (2015), 129–141.
23. [23] Sanford, J.A., Gallo, R.L., Functions of the skin microbiota in health and disease. Semin. Immunol. 25:5 (2013), 370–377.
24. [24] Rieg, S., Steffen, H., Seeber, S., Humeny, A., Kalbacher, H., Dietz, K., Garbe, C., Schittek, B., Deficiency of dermcidin-derived antimicrobial peptides in sweat of patients with atopic dermatitis correlates with an impaired innate defense of human skin in vivo. J. Immunol. 174:12 (2005), 8003–8010.
25. [25] Rieg, S., Seeber, S., Steffen, H., Humeny, A., Kalbacher, H., Stevanovic, S., Kimura, A., Garbe, C., Schittek, B., Generation of multiple stable dermcidin-derived antimicrobial peptides in sweat of different body sites. J. Investig. Dermatol. 126:2 (2006), 354–365.
26. [26] Koomen, J.M., Li, D., Xiao, L.C., Liu, T.C., Coombes, K.R., Abbruzzese, J., Kobayashi, R., Direct tandem mass spectrometry reveals limitations in protein profiling experiments for plasma biomarker discovery. J. Proteome Res. 4:3 (2005), 972–981.
27. [27] Mikhaylova, M., Schumacher, A., Borutzki, C., Neumann, J.R., Macharadze, T., El-Mousleh, T., Wahle, P., Zenclussen, A.C., Kreutz, M.R., Analysis of Y-P30/Dermcidin expression and properties of the Y-P30 peptide. BMC Res. Notes, 7, 2014, 400.
28. [28] Gkegkes, I.D., Aroni, K., Agrogiannis, G., Patsouris, E.S., Konstantinidou, A.E., Expression of caspase-14 and keratin-19 in the human epidermis and appendages during fetal skin development. Arch. Dermatol. Res. 305:5 (2013), 379–387.
29. [29] Baechle, D., Flad, T., Cansier, A., Steffen, H., Schittek, B., Tolson, J., Herrmann, T., Dihazi, H., Beck, A., Mueller, G.A., Mueller, M., Stevanovic, S., Garbe, C., Mueller, C.A., Kalbacher, H., Cathepsin D is present in human eccrine sweat and involved in the postsecretory processing of the antimicrobial peptide DCD-1L. J. Biol. Chem. 281:9 (2006), 5406–5415.
30. [30] Eissa, A., Amodeo, V., Smith, C.R., Diamandis, E.P., Kallikrein-related peptidase-8 (KLK8) is an active serine protease in human epidermis and sweat and is involved in a skin barrier proteolytic cascade. J. Biol. Chem. 286:1 (2011), 687–706.
31. [31] Bennett, K., Heywood, W., Di, W.L., Harper, J., Clayman, G.L., Jayakumar, A., Callard, R., Mills, K., The identification of a new role for LEKTI in the skin: the use of protein ‘bait’ arrays to detect defective trafficking of dermcidin in the skin of patients with Netherton syndrome. J. Proteome 75:13 (2012), 3925–3937.
32. [32] Borgono, C.A., Michael, I.P., Komatsu, N., Jayakumar, A., Kapadia, R., Clayman, G.L., Sotiropoulou, G., Diamandis, E.P., A potential role for multiple tissue kallikrein serine proteases in epidermal desquamation. J. Biol. Chem. 282:6 (2007), 3640–3652.
33. [33] Emami, N., Diamandis, E.P., Human tissue kallikreins: a road under construction. Clin. Chim. Acta 381:1 (2007), 78–84.
34. [34] Brattsand, M., Stefansson, K., Lundh, C., Haasum, Y., Egelrud, T., A proteolytic cascade of kallikreins in the stratum corneum. J. Investig. Dermatol. 124:1 (2005), 198–203.
35. [35] Caubet, C., Jonca, N., Brattsand, M., Guerrin, M., Bernard, D., Schmidt, R., Egelrud, T., Simon, M., Serre, G., Degradation of corneodesmosome proteins by two serine proteases of the kallikrein family, SCTE/KLK5/hK5 and SCCE/KLK7/hK7. J. Investig. Dermatol. 122:5 (2004), 1235–1244.
36. [36] Brattsand, M., Egelrud, T., Purification, molecular cloning, and expression of a human stratum corneum trypsin-like serine protease with possible function in desquamation. J. Biol. Chem. 274:42 (1999), 30033–30040.
37. [37] Eissa, A., Diamandis, E.P., Human tissue kallikreins as promiscuous modulators of homeostatic skin barrier functions. Biol. Chem. 389:6 (2008), 669–680.
38. [38] Ishida-Yamamoto, A., Igawa, S., Kishibe, M., Order and disorder in corneocyte adhesion. J. Dermatol. 38:7 (2011), 645–654.
39. [39] Peitsch, W.K., Doerflinger, Y., Fischer-Colbrie, R., Huck, V., Bauer, A.T., Utikal, J., Goerdt, S., Schneider, S.W., Desmoglein 2 depletion leads to increased migration and upregulation of the chemoattractant secretoneurin in melanoma cells. PLoS One, 9(2), 2014, e89491.
40. [40] Yang, T., Liang, D., Koch, P.J., Hohl, D., Kheradmand, F., Overbeek, P.A., Epidermal detachment, desmosomal dissociation, and destabilization of corneodesmosin in Spink5 −/− mice. Genes Dev. 18:19 (2004), 2354–2358.
41. [41] Komatsu, N., Takata, M., Otsuki, N., Toyama, T., Ohka, R., Takehara, K., Saijoh, K., Expression and localization of tissue kallikrein mRNAs in human epidermis and appendages. J. Investig. Dermatol. 121:3 (2003), 542–549.
42. [42] Chavanas, S., Bodemer, C., Rochat, A., Hamel-Teillac, D., Ali, M., Irvine, A.D., Bonafe, J.L., Wilkinson, J., Taieb, A., Barrandon, Y., Harper, J.I., de Prost, Y., Hovnanian, A., Mutations in SPINK5, encoding a serine protease inhibitor, cause Netherton syndrome. Nat. Genet. 25:2 (2000), 141–142.
43. [43] Komatsu, N., Saijoh, K., Jayakumar, A., Clayman, G.L., Tohyama, M., Suga, Y., Mizuno, Y., Tsukamoto, K., Taniuchi, K., Takehara, K., Diamandis, E.P., Correlation between SPINK5 gene mutations and clinical manifestations in Netherton syndrome patients. J. Investig. Dermatol. 128:5 (2008), 1148–1159.
44. [44] Brannstrom, K., Ohman, A., von Pawel Rammingen, U., Olofsson, A., Brattsand, M., Characterization of SPINK9, a KLK5-specific inhibitor expressed in palmo-plantar epidermis. Biol. Chem. 393:5 (2012), 369–377.
45. [45] Redelfs, L., Fischer, J., Weber, C., Wu, Z., Meyer-Hoffert, U., The serine protease inhibitor of Kazal-type 9 (SPINK9) is expressed in lichen simplex chronicus, actinic keratosis and squamous cell carcinoma. Arch. Dermatol. Res. 308:2 (2016), 133–137.
46. [46] Magister, S., Kos, J., Cystatins in immune system. J. Cancer 4:1 (2013), 45–56.
47. [47] Mukherjee, S., Ukil, A., Das, P.K., Immunomodulatory peptide from cystatin, a natural cysteine protease inhibitor, against leishmaniasis as a model macrophage disease. Antimicrob. Agents Chemother. 51:5 (2007), 1700–1707.
48. [48] Blankenvoorde, M.F., van't Hof, W., Walgreen-Weterings, E., van Steenbergen, T.J., Brand, H.S., Veerman, E.C., Nieuw Amerongen, A.V., Cystatin and cystatin-derived peptides have antibacterial activity against the pathogen Porphyromonas gingivalis. Biol. Chem. 379:11 (1998), 1371–1375.
49. [49] Jasir, A., Kasprzykowski, F., Kasprzykowska, R., Lindstrom, V., Schalen, C., Grubb, A., New antimicrobial cystatin C-based peptide active against gram-positive bacterial pathogens, including methicillin-resistant Staphylococcus aureus and multiresistant coagulase-negative staphylococci. APMIS 111:11 (2003), 1004–1010.
50. [50] Schauber, J., Gallo, R.L., Expanding the roles of antimicrobial peptides in skin: alarming and arming keratinocytes. J. Investig. Dermatol. 127:3 (2007), 510–512.
51. [51] Meyer-Hoffert, U., Wichmann, N., Schwichtenberg, L., White, P.C., Wiedow, O., Supernatants of Pseudomonas aeruginosa induce the Pseudomonas-specific antibiotic elafin in human keratinocytes. Exp. Dermatol. 12:4 (2003), 418–425.
52. [52] Yamasaki, K., Schauber, J., Coda, A., Lin, H., Dorschner, R.A., Schechter, N.M., Bonnart, C., Descargues, P., Hovnanian, A., Gallo, R.L., Kallikrein-mediated proteolysis regulates the antimicrobial effects of cathelicidins in skin. FASEB J. 20:12 (2006), 2068–2080.