IJCRR - 7(12), June, 2015
Pages: 36-43
DELAYED DIABETIC WOUND HEALING: A FOCUS ON BACTERIAL PROTEASES IN CHRONIC WOUND AND FOOT ULCER
Author: Saumya Mary Mathew, Varshaniyah Ravisanker, Tanvi Potluri, Suchithra T.V.
Category: Healthcare
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Abstract:
Background: The infectious bacteria produce proteolytic enzymes which help them to invade, establish infection and to survive the host defence mechanism delaying the wound healing.
Objectives: Protease secreting potential of bacterial flora; specifically the bacterial isolates of diabetic ulcer foot patients are studied here.
Methods: The predominant bacteria in foot ulcer were identified and bacterial enzymes caseinase, gelatinase, alkaline protease, hyaluronidase, proteinase K and collagenase were analysed.
Results: Out of the 78 strains isolated S.aureus was the most predominant organism. Among the bacterial isolates, the presence of different types of proteolytic activities was observed as follows: proteinase K (87.2%), collagenase (80.8%), hyaluronidase (78.2%), caseinase (60.3%), alkaline protease (53.8%) and gelatinase (25.6%).
Conclusions: Bacterial wound flora were found capable to produce and secrete proteolytic enzymes and it can be worsen the proper wound healing
Keywords: Caseinase, Alkaline protease, Hyaluronidase, Proteinase K, Collagenase
Citation:
Saumya Mary Mathew, Varshaniyah Ravisanker, Tanvi Potluri, Suchithra T.V.. DELAYED DIABETIC WOUND HEALING: A FOCUS ON BACTERIAL PROTEASES IN CHRONIC WOUND AND FOOT ULCER International Journal of Current Research and Review. 7(12), June, 36-43
References:
1. Boulton AJ, Vileikyte L, Ragnarson-Tennvall G, Apelqvist J. The global burden of diabetic foot disease.
2. Adler AI, Boyko EJ, Ahroni JH, Smith DG. Lower-extremity amputation in diabetes. The independent effects of peripheral vascular disease, sensory neuropathy, and foot ulcers. Diabetes care. 1999;22(7):1029-35.
3. Percival SL, Cutting KF. Microbiology of wounds. Microbiology of wounds. 2010.
4. Mustoe TA, O’Shaughnessy K, Kloeters O. Chronic wound pathogenesis and current treatment strategies: a unifying hypothesis. Plastic and reconstructive surgery. 2006;117(7S):35S-41S.
5. Hynes WL, Walton SL. Hyaluronidases of Gram-positive bacteria. FEMS microbiology letters. 2000;183(2):201-7.
6. Tran L, Nagano H. Isolation and characteristics of Bacillus subtilis CN2 and its collagenase production. Journal of food science. 2002;67(3):1184-7.
7. Kayaoglu G, Ørstavik D. Virulence factors of Enterococcus faecalis: relationship to endodontic disease. Critical Reviews in Oral Biology and Medicine. 2004;15(5):308-20.
8. Matsumoto K. Proteases in bacterial keratitis. Cornea. 2000;19(6):S160-S4.
9. Hoge R, Pelzer A, Rosenau F, Wilhelm S. Weapons of a pathogen: proteases and their role in virulence of Pseudomonas aeruginosa. Current Research, Technology and Education Topics in Applied Microbiology and Microbial Biotechnology. 2010;2:383-95.
10. Barrett AJ, Woessner JF, Rawlings ND. Handbook of proteolytic enzymes: Elsevier; 2004.
11. Guariguata L, Whiting DR, Hambleton I, Beagley J, Linnenkamp U, Shaw JE. Global estimates of diabetes prevalence for 2013 and projections for 2035 for the IDF Diabetes Atlas. Diabetes Research and Clinical Practice.
12. Cowan ST, Steel KJ, Barrow G, Feltham R. Cowan and Steel’s manual for the identification of medical bacteria: Cambridge university press; 2004.
13. Galloway DR. Role of exotoxins in the pathogenesis of P. aeruginosa infections. Pseudomonas aeruginosa as an Opportunistic Pathogen: Springer; 1993. p. 107-27.
14. Vasil M, Pritchard AE, Ostroff R. Molecular biology of exotoxin A and phospholipase C of Pseudomonas aeruginosa. 1990.
15. Mandl I, MacLennan JD, Howes EL, DeBellis RH, Sohler A. Isolation and characterization of proteinase and collagenase from Cl. histolyticum. Journal of Clinical Investigation. 1953;32(12):1323.
16. Tolksdorf S, McCready M. The turbidimetric assay of hyaluronidase. The Journal of laboratory and clinical medicine. 1949;34(1):74.
17. Kass EH, Seastone C. The role of the mucoid polysaccharide (hyaluronic acid) in the virulence of group A hemolytic streptococci. The Journal of experimental medicine. 1944;79(3):319-30.
18. Meyers S, Ahearn D. Extracellular proteolysis by Candida lipolytica. Mycologia. 1977:646-51.
19. Shah BR, Hux JE. Quantifying the risk of infectious diseases for people with diabetes. Diabetes care. 2003;26(2):510-3.
20. Wheat LJ. Infection and diabetes mellitus. Diabetes care. 1980;3(1):187-97.
21. Sheetz MJ, King GL. Molecular understanding of hyperglycemia’s adverse effects for diabetic complications. Jama. 2002;288(20):2579-88.
22. Wunderlich RP, Peters EJ, Lavery LA. Systemic hyperbaric oxygen therapy: lower-extremity wound healing and the diabetic foot. Diabetes Care. 2000;23(10):1551-5.
23. Falanga V. Wound healing and its impairment in the diabetic foot. The Lancet. 2005;366(9498):1736-43.
24. Miyoshi S-i, Shinoda S. Microbial metalloproteases and pathogenesis. Microbes and infection. 2000;2(1):91-8.
25. Mathew SM, Suchithra TV. A Threatening Approach of Wound Microflora to Diabetic Ulcer Foot Management. Int J Curr Microbiol App Sci. 2014;3(9):640-6.
26. Tentolouris N, Petrikkos G, Vallianou N, Zachos C, Daikos GL, Tsapogas P, et al. Prevalence of methicillin-resistant Staphylococcus aureus in infected and uninfected diabetic foot ulcers. Clin Microbiol Infect. 2006;12(2):186-9.
27. Orji F, Nwachukwu N, Udora E. Bacteriological evaluation of diabetic ulcers in Nigeria. African Journal of Diabetes Medicine. 2009;15(11):19-21.
28. Hena J, Growther L. Studies on bacterial infections of diabetic foot ulcer. African Journal of Clinical and Experimental Microbiology. 2010;11(3).
29. Srivastava S, Srivastava P. Bacteria and Huma30. Diegelmann RF, Evans MC. Wound healing: an overview of acute, fibrotic and delayed healing. Front Biosci. 2004;9(1):283-9.
31. Rahme LG, Ausubel FM, Cao H, Drenkard E, Goumnerov BC, Lau GW, et al. Plants and animals share functionally common bacterial virulence factors. Proceedings of the National Academy of Sciences. 2000;97(16):8815-21.
32. Kastrup CJ, Boedicker JQ, Pomerantsev AP, Moayeri M, Bian Y, Pompano RR, et al. Spatial localization of bacteria controls coagulation of human blood by’quorum acting’. Nature chemical biology. 2008;4(12):742-50.
33. Staats CC, Boldo J, Broetto L, Vainstein M, Schrank A. Comparative genome analysis of proteases, oligopeptide uptake and secretion systems in Mycoplasma spp. Genetics and Molecular Biology. 2007;30(1):225-9
. 34. An S-Y, Ok M, Kim J-Y, Jang M-S, Cho Y-S, Choi Y-L, et al. Cloning, high-level expression and enzymatic properties of an intracellular serine protease from Bacillus sp. WRD-2. Indian Journal of Biochemistry And Biophysics. 2004;41:141-7.
35. Wandersman C. Secretion, processing and activation of bacterial extracellular proteases. Molecular microbiology. 1989;3(12):1825-31.
36. Nam G-W, Lee D-W, Lee H-S, Lee N-J, Kim B-C, Choe E-A, et al. Native-feather degradation by Fervidobacterium islandicum AW-1, a newly isolated keratinase-producing thermophilic anaerobe. Archives of Microbiology. 2002;178(6):538-47.
37. Chung L, Dinakarpandian D, Yoshida N, Lauer-Fields JL, Fields GB, Visse R, et al. Collagenase unwinds triple-helical collagen prior to peptide bond hydrolysis. The EMBO journal. 2004;23(15):3020-30.
38. Toyoshima T, Matsushita O, Minami J, Nishi N, Okabe A, Itano T. Collagen-binding domain of a Clostridium histolyticum collagenase exhibits a broad substrate spectrum both in vitro and in vivo. Connective tissue research. 2001;42(4):281-90.
39. Takeuchi H, Shibano Y, Morihara K, Fukushima J, Inami S, Keil B, et al. Structural gene and complete amino acid sequence of Vibrio alginolyticus collagenase. Biochem J. 1992;281:703-8.
40. Mookhtiar K, Van Wart H. Clostridium histolyticum collagenases: a new look at some old enzymes. Matrix (Stuttgart, Germany) Supplement. 1991;1:116-26.
41. Metzmacher I, Ruth P, Abel M, Friess W. In vitro binding of matrix metalloproteinase-2 (MMP-2), MMP-9, and bacterial collagenase on collagenous wound dressings. Wound repair and regeneration. 2007;15(4):549-55.
42. Starr CR, Engleberg NC. Role of hyaluronidase in subcutaneous spread and growth of group A streptococcus. Infection and immunity. 2006;74(1):40-8.
43. Wessels MR, Bronze MS. Critical role of the group A streptococcal capsule in pharyngeal colonization and infection in mice. Proceedings of the National Academy of Sciences. 1994;91(25):12238-42.
44. Smith NL, Taylor EJ, Lindsay A-M, Charnock SJ, Turkenburg JP, Dodson EJ, et al. Structure of a group A streptococcal phage-encoded virulence factor reveals a catalytically active triple-stranded β-helix. Proceedings of the National Academy of Sciences of the United States of America. 2005;102(49):17652-7.
45. Žukaite V, Biziulevi?ius G. Acceleration of hyaluronidase production in the course of batch cultivation of Clostridium perfringens can be achieved with bacteriolytic enzymes. Letters in applied microbiology. 2000;30(3):203-6.
46. Garcia DdO, Timenetsky J, Martinez MB, Francisco W, Sinto SI, Yanaguita RM. Proteases (caseinase and elastase), hemolysins, adhesion and susceptibility to antimicrobials of Stenotrophomonas maltophilia isolates obtained from clinical specimens. Brazilian Journal of Microbiology. 2002;33(2):157-62.
47. Furumura MT, Figueiredo P, Carbonell GV, Darini ALdC, Yano T. Virulence-associated characteristics of Enterococcus faecalis strains isolated from clinical sources. Brazilian Journal of Microbiology. 2006;37(3):230-6.
48. Sheeran B, Smith P. A second extracellular proteolytic activity associated with the fish pathogen Aeromonas salmonicida. FEMS Microbiology Letters. 1981;11(1):73-6.
49. Percival SL, Cochrane CA. Wounds, Enzymes, and Proteases. Microbiology of Wounds. 2010:249.
50. Schneider LA, Korber A, Grabbe S, Dissemond J. Influence of pH on wound-healing: a new perspective for wound-therapy? Archives of dermatological research. 2007;298(9):413-20.
51. Gethin G. The significance of surface pH in chronic wounds. Wounds uk. 2007;3(3):52.
52. Syed R, Roja Rani S, Masoodi TA, Shafi G, Alharbi K. Functional analysis and structure determination of alkaline protease from Aspergillus flavus. Bioinformation. 2012;8(4):175.
53. Laarman AJ, Bardoel BW, Ruyken M, Fernie J, Milder FJ, van Strijp JA, et al. Pseudomonas aeruginosa alkaline protease blocks complement activation via the classical and lectin pathways. The Journal of Immunology. 2012;188(1):386- 93.
54. Kernacki K, Hobden J, Hazlett L, Fridman R, Berk R. In vivo bacterial protease production during Pseudomonas aeruginosa corneal infection. Investigative ophthalmology and visual science. 1995;36(7):1371-8.
55. Saleem AJ. Relationship Study between the Alkaline Protease Production and the Growth Phases of Pseudomonas aeruginosa Isolated from Patients. Advances in Microbiology. 2012;2(03):354.
56. Upadhyaya PG, Umapathy B, Ravikumar K. Comparative study for the presence of enterococcal virulence factors gelatinase, hemolysin and biofilm among clinical and commensal isolates of Enterococcus faecalis. Journal of laboratory physicians. 2010;2(2):100.
57. Mohan R, Chintala SK, Jung JC, Villar WV, McCabe F, Russo LA, et al. Matrix metalloproteinase gelatinase B (MMP-9) coordinates and effects epithelial regeneration. Journal of Biological Chemistry. 2002;277(3):2065-72.
58. Ladwig GP, Robson MC, Liu RAN, Kuhn M, Muir DF, Schultz GS. Ratios of activated matrix metalloproteinase†9 to tissue inhibitor of matrix metalloproteinase†1 in wound fluids are inversely correlated with healing of pressure ulcers. Wound Repair and Regeneration. 2002;10(1):26-37.
59. Lopes MdFS, Simões AP, Tenreiro R, Marques JJF, Crespo MTB. Activity and expression of a virulence factor, gelatinase, in dairy enterococci. International journal of food microbiology. 2006;112(3):208-14.
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