Biophysical approach to studying protein interactions in skin wound healing

سال انتشار: 1404
نوع سند: مقاله ژورنالی
زبان: انگلیسی
مشاهده: 182

فایل این مقاله در 15 صفحه با فرمت PDF قابل دریافت می باشد

استخراج به نرم افزارهای پژوهشی:

لینک ثابت به این مقاله:

شناسه ملی سند علمی:

JR_IRANJB-1-2_008

تاریخ نمایه سازی: 26 مرداد 1404

چکیده مقاله:

Cutaneous wounds are a significant health problem worldwide. That is why wound healing and biological factors, including proteins, are substantial. This complicated and dynamic process consists of five overlapping phases: Hemostasis, Inflammation, Granulation tissue formation, Re-epithelialization, and Remodeling. Cells and proteins shared in these phases can trigger myriad activities that eventually complement each other. This paper aims to provide an understanding of the key proteins' functions and signaling involved in the wound healing process, based on data available on bioinformatics websites. These proteins include the interleukin-۱ family, tight junction proteins (occludin and claudin), platelet-derived growth factor (PDGF), and extracellular matrix components such as matrix metalloproteinases (MMPs), fibronectin, and laminins. In addition, by examining the significant role of inflammatory cytokines, proteases, and members of the large family of metalloproteinases, we can take novel measures to accelerate the healing of chronic wounds that are stuck in the inflammatory phase. Additionally, it is notable that mediator proteins are vital, as they exhibit co-expression and share molecular interactions with key proteins. Therefore, their absence or impaired functioning can disrupt the normal healing process of skin wounds.Cutaneous wounds are a significant health problem worldwide. That is why wound healing and biological factors, including proteins, are substantial. This complicated and dynamic process consists of five overlapping phases: Hemostasis, Inflammation, Granulation tissue formation, Re-epithelialization, and Remodeling. Cells and proteins shared in these phases can trigger myriad activities that eventually complement each other. This paper aims to provide an understanding of the key proteins' functions and signaling involved in the wound healing process, based on data available on bioinformatics websites. These proteins include the interleukin-۱ family, tight junction proteins (occludin and claudin), platelet-derived growth factor (PDGF), and extracellular matrix components such as matrix metalloproteinases (MMPs), fibronectin, and laminins. In addition, by examining the significant role of inflammatory cytokines, proteases, and members of the large family of metalloproteinases, we can take novel measures to accelerate the healing of chronic wounds that are stuck in the inflammatory phase. Additionally, it is notable that mediator proteins are vital, as they exhibit co-expression and share molecular interactions with key proteins. Therefore, their absence or impaired functioning can disrupt the normal healing process of skin wounds.

نویسندگان

Samin Khosravi

Department of Biology, NT.C., Islamic Azad University, Tehran, Iran

Hosna Basiri kheradmand Tehrani

Department of Biology, NT.C., Islamic Azad University, Tehran, Iran

Mina Sadat Naderi

Department of Biology, NT.C., Islamic Azad University, Tehran, Iran

Seyed Mehdi Tabaie

Department of Medical Laser, Medical Laser Research Center, Yara Institute, Academic Center for Education Culture and Research (ACECR), Tehran, Iran

Shima Hatamzadeh

Department of Biology, Faculty of Sciences, University of Guilan, Rasht, Iran

مراجع و منابع این مقاله:

لیست زیر مراجع و منابع استفاده شده در این مقاله را نمایش می دهد. این مراجع به صورت کاملا ماشینی و بر اساس هوش مصنوعی استخراج شده اند و لذا ممکن است دارای اشکالاتی باشند که به مرور زمان دقت استخراج این محتوا افزایش می یابد. مراجعی که مقالات مربوط به آنها در سیویلیکا نمایه شده و پیدا شده اند، به خود مقاله لینک شده اند :
  • [1] Nussbaum SR, Carter MJ, Fife CE, DaVanzo J, Haught ...
  • DOI: 10.1016/j.jval.2017.07.007 PMID: 29304937 ...
  • [2] Sen CK. Human Wounds and Its Burden: An Updated ...
  • PMID: 30809421 ...
  • [3] Sen CK. Human Wound and Its Burden: Updated 2020 ...
  • PMID: 33733885 ...
  • [4] Rogers LC, Armstrong DG, Capotorto J, Fife CE, Garcia ...
  • [5] Nejati R, Kovacic D, Slominski A. Neuro-immune-endocrine functions of ...
  • [6] Tottoli EM, Dorati R, Genta I, Chiesa E, Pisani ...
  • PMID: 32764269 ...
  • [7] Yousef H, Miao JH, Alhajj M, Badri T. Histology, ...
  • [8] Marcos-Garcés V, Molina Aguilar P, Bea Serrano C, García ...
  • [9] Rippa AL, Kalabusheva EP, Vorotelyak EA. Regeneration of Dermis: ...
  • DOI: 10.3390/cells8060607 PMID: 31216669 ...
  • [10] Lansdown AB. Calcium: a potential central regulator in wound ...
  • [11] Gao FL, Jin R, Zhang L, Zhang YG. The ...
  • [12] Roh JS, Sohn DH. Damage-Associated Molecular Patterns in Inflammatory ...
  • DOI: 10.4110/in.2018.18.e27 PMID: 30181915 ...
  • [13] van der Vliet A, Janssen-Heininger YM. Hydrogen peroxide as ...
  • [14] Ozgok Kangal MK, Regan JP. Wound Healing. In: StatPearls. ...
  • URL: https://www.ncbi.nlm.nih.gov/books/NBK535406 ...
  • [15] Cañedo-Dorantes L, Cañedo-Ayala M. Skin Acute Wound Healing: A ...
  • PMID: 31275545 ...
  • [16] Wilkinson HN, Hardman MJ. Wound healing: cellular mechanisms and ...
  • PMID: 32993416 ...
  • [17] Schultz GS, Chin GA, Moldawer L, Diegelmann RF. Principles ...
  • [18] Sorrentino S, Studt JD, Medalia O, Tanuj Sapra K. ...
  • DOI: 10.1016/j.ejcb.2015.01.001 PMID: 25655000 ...
  • [19] Litvinov RI, Pieters M, de Lange-Loots Z, Weisel JW. ...
  • DOI: 10.1007/978-3-030-58971-4_15 PMID: 33252741 ...
  • [20] Wallace HA, Basehore BM, Zito PM. Wound Healing Phases. ...
  • [21] Davies PF. Hemodynamic shear stress and the endothelium in ...
  • [22] Toriseva M, Kähäri VM. Proteinases in cutaneous wound healing. ...
  • [23] Cognasse F, Hamzeh H, Chavarin P, Acquart S, Genin ...
  • [24] Gantwerker EA, Hom DB. Skin: histology and physiology of ...
  • PMID: 21856533 ...
  • [25] Shah D, Mital K. The Role of Trypsin:Chymotrypsin in ...
  • [26] Shah JM, Omar E, Pai DR, Sood S. Cellular ...
  • PMID: 23162220 ...
  • [27] Reinke JM, Sorg H. Wound repair and regeneration. Eur ...
  • PMID: 22797712 ...
  • [28] Sorg H, Tilkorn DJ, Hager S, Hauser J, Mirastschijski ...
  • DOI: 10.1159/000454919 PMID: 27974711 ...
  • [29] Lenselink EA. Role of fibronectin in normal wound healing. ...
  • PMID: 23742140 ...
  • [30] Dvorak AM. Mast cell-derived mediators of enhanced microvascular permeability, ...
  • DOI: 10.1159/000086517 PMID: 15970658 ...
  • [31] Weller K, Foitzik K, Paus R, Syska W, Maurer ...
  • PMID: 16966487 ...
  • [32] Zhao R, Liang H, Clarke E, Jackson C, Xue ...
  • DOI: 10.3390/ijms17122085 PMID: 27973441 ...
  • [33] Bowers S, Franco E. Chronic Wounds: Evaluation and Management. ...
  • PMID: 32003952 ...
  • [34] Alhajj M, Goyal A. Physiology, Granulation Tissue. 2022. In: ...
  • [35] Jiang D, Scharffetter-Kochanek K. Mesenchymal Stem Cells Adaptively Respond ...
  • PMID: 32850818 ...
  • [36] Goto T, Yanaga F, Ohtsuki I. Studies on the ...
  • [37] Gu S, Dai H, Zhao X, Gui C, Gui ...
  • [38] Wang J, Wu H, Peng Y, Zhao Y, Qin ...
  • [39] Shaw TJ, Martin P. Wound repair: a showcase for ...
  • DOI: 10.1016/j.ceb.2016.04.001 PMID: 27085790 ...
  • [40] Pasparakis M, Haase I, Nestle FO. Mechanisms regulating skin ...
  • [41] Wager L, Leavesley D. MicroRNA regulation of epithelial-to-mesenchymal transition ...
  • [42] Li J, Chen J, Kirsner R. Pathophysiology of acute ...
  • DOI: 10.1016/j.clindermatol.2006.09.007 PMID: 17276196 ...
  • [43] Rousselle P, Braye F, Dayan G. Re-epithelialization of adult ...
  • DOI: 10.1016/j.addr.2018.06.019 PMID: 29981800 ...
  • [44] Shi J, Ma X, Su Y, Song Y, Tian ...
  • [45] Masson-Meyers DS, Andrade TAM, Caetano GF, Guimaraes FR, Leite ...
  • [46] Díaz-Coránguez M, Liu X, Antonetti DA. Tight Junctions in ...
  • DOI: 10.3390/ijms20235972 PMID: 31783547 ...
  • [47] Higashi T, Arnold TR, Stephenson RE, Dinshaw KM, Miller ...
  • [48] Witte MB, Barbul A. General principles of wound healing. ...
  • [49] Darby IA, Laverdet B, Bonté F, Desmoulière A. Fibroblasts ...
  • [50] Ozsvar J, Yang C, Cain SA, Baldock C, Tarakanova ...
  • PMID: 33718344 ...
  • [51] Duca L, Floquet N, Alix AJ, Haye B, Debelle ...
  • DOI: 10.1016/j.critrevonc.2003.09.007 PMID: 15036263 ...
  • [52] Almine JF, Wise SG, Weiss AS. Elastin signaling in ...
  • [53] Krzyszczyk P, Schloss R, Palmer A, Berthiaume F. The ...
  • PMID: 29765329 ...
  • [54] Li B, Wang JH. Fibroblasts and myofibroblasts in wound ...
  • PMID: 19995679 ...
  • [55] Minor AJ, Coulombe KLK. Engineering a collagen matrix for ...
  • DOI: 10.1002/jbm.b.34573 PMID: 31984665 ...
  • [56] Miekus N, Luise C, Sippl W, Baczek T, Schmelzer ...
  • PMID: 31278967 ...
  • [57] Demidova-Rice TN, Hamblin MR, Herman IM. Acute and impaired ...
  • DOI: 10.1097/01.ASW.0000416006.55218.d0 PMID: 22713781 ...
  • [58] Mathew-Steiner SS, Roy S, Sen CK. Collagen in Wound ...
  • DOI: 10.3390/bioengineering8050063 PMID: 34064689 ...
  • [59] Mofazzal Jahromi MA, Sahandi Zangabad P, Moosavi Basri SM, ...
  • PMID: 28782570 ...
  • [60] Heldin CH. Targeting the PDGF signaling pathway in tumor ...
  • DOI: 10.1186/1478-811X-11-97 PMID: 24359404 ...
  • [61] Yang Y, Yuzawa S, Schlessinger J. Contacts between membrane ...
  • DOI: 10.1073/pnas.0802896105 PMID: 18505839 ...
  • [62] Yu J, Ustach C, Kim HR. Platelet-derived growth factor ...
  • DOI: 10.5483/bmbrep.2003.36.1.049 PMID: 12542975 ...
  • [63] Pierce GF, Mustoe TA, Altrock BW, Deuel TF, Thomason ...
  • [64] Senzel L, Gnatenko DV, Bahou WF. The platelet proteome. ...
  • DOI: 10.1097/MOH.0b013e32832e9dc6 PMID: 19550320 ...
  • [65] Dalton CJ, Lemmon CA. Fibronectin: Molecular Structure, Fibrillar Structure ...
  • [66] To WS, Midwood KS. Plasma and cellular fibronectin: distinct ...
  • PMID: 21923916 ...
  • [67] Singh P, Carraher C, Schwarzbauer JE. Assembly of fibronectin ...
  • [68] Patten J, Wang K. Fibronectin in development and wound ...
  • DOI: 10.1016/j.addr.2020.09.005 PMID: 32961203 ...
  • [69] Wang Y, Reheman A, Spring CM, Kalantari J, Marshall ...
  • DOI: 10.1172/JCI74630 PMID: 25180602 ...
  • [70] Gale AJ. Continuing education course #2: current understanding of ...
  • DOI: 10.1177/0192623310389474 PMID: 21119054 ...
  • [71] Trial J, Rossen RD, Rubio J, Knowlton AA. Inflammation ...
  • DOI: 10.1177/153537020422900612 PMID: 15169973 ...
  • [72] Speziale P, Arciola CR, Pietrocola G. Fibronectin and Its ...
  • DOI: 10.3390/cells8121516 PMID: 31779172 ...
  • [73] Purohit T, Qin Z, Quan C, Lin Z, Quan ...
  • DOI: 10.1371/journal.pone.0173191 PMID: 28267785 ...
  • [74] Shimizu M, Minakuchi K, Moon M, Koga J. Difference ...
  • DOI: 10.1016/s0167-4838(96)00214-2 PMID: 9165099 ...
  • [75] Kudo A, Kii I. Periostin function in communication with ...
  • [76] Calabro NE, Kristofik NJ, Kyriakides TR. Thrombospondin-2 and extracellular ...
  • [77] Benito-Jardón M, Strohmeyer N, Ortega-Sanchís S, Bharadwaj M, Moser ...
  • DOI: 10.1083/jcb.202004198 PMID: 33141174 ...
  • [78] Bax DV, Rodgers UR, Bilek MM, Weiss AS. Cell ...
  • [79] Ishihara J, Ishihara A, Fukunaga K, Sasaki K, White ...
  • [80] Theocharis AD, Skandalis SS, Gialeli C, Karamanos NK. Extracellular ...
  • [81] Couchman JR. Syndecans: proteoglycan regulators of cell-surface microdomains? Nat ...
  • DOI: 10.1038/nrm1257 PMID: 14685171 ...
  • [82] Cui C, Wang S, Myneni VD, Hitomi K, Kaartinen ...
  • DOI: 10.1016/j.bone.2013.11.006 PMID: 24246248 ...
  • [83] Bergmann S, von Buenau B, Vidal-Y-Sy S, Haftek M, ...
  • [84] Feldman GJ, Mullin JM, Ryan MP. Occludin: structure, function ...
  • DOI: 10.1016/j.addr.2005.01.009 PMID: 15820558 ...
  • [85] Cummins PM. Occludin: one protein, many forms. Mol Cell ...
  • PMID: 22083955 ...
  • [86] González-Mariscal L, Betanzos A, Nava P, Jaramillo BE. Tight ...
  • DOI: 10.1016/s0079-6107(02)00037-8 PMID: 12475568 ...
  • [87] National Center for Biotechnology Information. OCLN occludin [Homo sapiens ...
  • [88] Furuse M, Fujita K, Hiiragi T, Fujimoto K, Tsukita ...
  • PMID: 9647647 ...
  • [89] Nishi H, Hashimoto K, Panchenko AR. Phosphorylation in protein-protein ...
  • [90] Van Itallie CM, Anderson JM. Phosphorylation of tight junction ...
  • [91] Murakami T, Frey T, Lin C, Antonetti DA. Protein ...
  • PMID: 22438576 ...
  • [92] Shi J, Barakat M, Chen D, Chen L. Bicellular ...
  • DOI: 10.3390/ijms19123862 PMID: 30518037 ...
  • [93] Tsukita S, Tanaka H, Tamura A. The Claudins: From ...
  • PMID: 30665499 ...
  • [94] Bhat AA, Syed N, Therachiyil L, Nisar S, Hashem ...
  • [95] National Center for Biotechnology Information. CLDN1 claudin 1 [Homo ...
  • [96] Hamazaki Y, Itoh M, Sasaki H, Furuse M, Tsukita ...
  • DOI: 10.1074/jbc.M109005200 PMID: 11689568 ...
  • [97] Gondelaud F, Ricard-Blum S. Structures and interactions of syndecans. ...
  • DOI: 10.1111/febs.14828 PMID: 30932318 ...
  • [98] Shimada T, Yasuda S, Sugiura H, Yamagata K. Syntenin: ...
  • [99] Liu X, Shepherd TR, Murray AM, Xu Z, Fuentes ...
  • [100] Palomo J, Dietrich D, Martin P, Palmer G, Gabay ...
  • [101] Kwak A, Lee Y, Kim H, Kim S. Intracellular ...
  • [102] Xu D, Mu R, Wei X. The Roles of ...
  • PMID: 31572353 ...
  • [103] Momeni HR. Role of calpain in apoptosis. Cell J. ...
  • [104] Lefrançais E, Roga S, Gautier V, Gonzalez-de-Peredo A, Monsarrat ...
  • DOI: 10.1073/pnas.1115884109 PMID: 22307629 ...
  • [105] Broz P, Dixit VM. Inflammasomes: mechanism of assembly, regulation ...
  • [106] Kolaczkowska E, Kubes P. Neutrophil recruitment and function in ...
  • [107] Namikawa K, Okamoto T, Suzuki A, Konishi H, Kiyama ...
  • [108] Kruger GM, Mosher JT, Bixby S, Joseph N, Iwashita ...
  • DOI: 10.1016/s0896-6273(02)00827-9 PMID: 12194866 ...
  • [109] McCarty SM, Percival SL. Proteases and Delayed Wound Healing. ...
  • [110] James GA, Swogger E, Wolcott R, Pulcini Ed, Secor ...
  • [111] Malinda KM, Kleinman HK. The laminins. Int J Biochem ...
  • [112] Mukherjee C, Saleem S, DAS S, Biswas SC, Bhattacharyya ...
  • PMID: 32713856 ...
  • [113] Min SK, Lee SC, Hong SD, Chung CP, Park ...
  • DOI: 10.1016/j.biomaterials.2010.02.045 PMID: 20303583 ...
  • [114] Zhu Y, Cankova Z, Iwanaszko M, Lichtor S, Mrksich ...
  • DOI: 10.1073/pnas.1804262115 PMID: 29891655 ...
  • [115] Malinda KM, Wysocki AB, Koblinski JE, Kleinman HK, Ponce ...
  • DOI: 10.1016/j.biocel.2008.05.025 PMID: 18603014 ...
  • [116] Longmate WM, Lyons SP, DeFreest L, Van De Water ...
  • PMID: 28923241 ...
  • [117] Chang YC, Wang JD, Chang HY, Zhou P, Hahn ...
  • DOI: 10.1002/ar.24405 PMID: 32421930 ...
  • [118] Michopoulou A, Montmasson M, Garnier C, Lambert E, Dayan ...
  • DOI: 10.1016/j.matbio.2020.06.004 PMID: 32621878 ...
  • [119] Mithieux SM, Weiss AS. Elastin. Adv Protein Chem. 2005;70:437-61. ...
  • PMID: 15837523 ...
  • [120] Heinz A, Schräder CU, Baud S, Keeley FW, Mithieux ...
  • [121] Antonicelli F, Bellon G, Debelle L, Hornebeck W. Elastin-elastases ...
  • [122] Almeida-González FR, González-Vázquez A, Mithieux SM, O'Brien FJ, Weiss ...
  • [123] Wang K, Meng X, Guo Z. Elastin Structure, Synthesis, ...
  • DOI: 10.3389/fcell.2021.596702 PMID: 34917605 ...
  • [124] Rodgers UR, Weiss AS. Cellular interactions with elastin. Pathol ...
  • DOI: 10.1016/j.patbio.2004.12.022 PMID: 16085115 ...
  • [125] de Castro Brás LE, Frangogiannis NG. Extracellular matrix-derived peptides ...
  • PMID: 32438055 ...
  • [126] Wahart A, Hocine T, Albrecht C, Henry A, Sarazin ...
  • PMID: 30946528 ...
  • [127] Scandolera A, Odoul L, Salesse S, Guillot A, Blaise ...
  • PMID: 26973522 ...
  • [128] P01127 PDGFB_HUMAN [Homo sapiens (human)] Gene ID: PDGFB. Updated ...
  • URL: https://www.uniprot.org/uniprotkb/P01127/entry ...
  • [129] PDGF binds to extracellular matrix proteins [Homo sapiens (human)] ...
  • URL: https://reactome.org/PathwayBrowser/#/R-HSA-186797&SEL=R-HSA-382054&PATH=R-HSA-162582,R-HSA-9006934 ...
  • [130] Gao AG, Lindberg FP, Finn MB, Blystone SD, Brown ...
  • [131] Kuznetsova SA, Mahoney DJ, Martin-Manso G, Ali T, Nentwich ...
  • DOI: 10.1016/j.matbio.2007.10.003 PMID: 18042364 ...
  • [132] EBI-2566729 OR EBI-11789924. Updated 6-Jul-2025. ...
  • URL: https://www.ebi.ac.uk/legacy-intact/pages/interactions/interactions.xhtml?query=EBI-2566729%20OR%20EBI-11789924 ...
  • [133] Takino T, Sato H, Shinagawa A, Seiki M. Identification ...
  • PMID: 7559440 ...
  • [134] VEGF-A,C,D bind to VEGFR2 leading to receptor dimerization [Homo ...
  • URL: https://reactome.org/PathwayBrowser/#/R-HSA-194138&SEL=R-HSA-194310&PATH=R-HSA-162582,R-HSA-9006934&FLG=P15692 ...
  • [135] Khayati F, Pérez-Cano L, Maouche K, Sadoux A, Boutalbi ...
  • PMID: 25825981 ...
  • [136] Sang QA, Bodden MK, Windsor LJ. Activation of human ...
  • [137] Morrison CJ, Butler GS, Bigg HF, Roberts CR, Soloway ...
  • [138] Schnapp LM, Hatch N, Ramos DM, Klimanskaya IV, Sheppard ...
  • DOI: 10.1074/jbc.270.39.23196 PMID: 7559467 ...
  • [139] PDGFA. GeneMania. Updated 2025 Jul 6. ...
  • URL: https://genemania.org/search/homo-sapiens/PDGFA/ ...
  • [140] HGF(495-728) [extracellular region] [Homo sapiens (human)] Stable Identifier: R-HSA-141767. ...
  • [141] McElroy CA, Dohm JA, Walsh ST. Structural and biophysical ...
  • PMID: 19141282 ...
  • [142] Futosi K, Fodor S, Mócsai A. Neutrophil cell surface ...
  • DOI: 10.1016/j.intimp.2013.06.034 PMID: 23994464 ...
  • [143] STRING [Internet]. [cited 2022 Jul 1]. URL: https://string-db.org/cgi/network?taskId=bOa9HNe68ZGz&sessionId=bwZkM5lzLdhc. ...
  • [144] cldn5, cldn1, cldn2, cldn3. GeneMania. Updated 2025 Jul 6. ...
  • [145] Crabbe T, O'Connell JP, Smith BJ, Docherty AJ. Reciprocated ...
  • DOI: 10.1021/bi00252a007 PMID: 7981201 ...
  • [146] Strongin AY, Marmer BL, Grant GA, Goldberg GI. Plasma ...
  • [147] Nishida Y, Miyamori H, Thompson EW, Takino T, Endo ...
  • [148] Tam EM, Wu YI, Butler GS, Stack MS, Overall ...
  • DOI: 10.1074/jbc.M206874200 PMID: 12145314 ...
  • [149] Steffensen B, Bigg HF, Overall CM. The involvement of ...
  • PMID: 9685420 ...
  • [150] Latifi-Navid H, Soheili ZS, Samiei S, Sadeghi M, Taghizadeh ...
  • DOI: 10.1111/jcmm.16778 PMID: 34250732 ...
  • [151] Turner CT, Zeglinski MR, Richardson KC, Zhao H, Shen ...
  • DOI: 10.1016/j.jid.2018.09.031 PMID: 30395844 ...
  • نمایش کامل مراجع