Molecular determination of laminin-5 degradation: A biomarker for mustard gas exposure diagnosis and its mechanism of action

Experimental Dermatology

Volumn 17, Issue 1, 2008, Pages 49-56

  Jin, Xiannu ^a   Ray, Radharaman ^b   Leng, Yan ^c   Ray, Prabhati ^a  

^a WALTER REED ARMY INSTITUTE OF RESEARCH   (United States)

^b US ARMY MEDICAL RESEARCH INSTITUTE OF CHEMICAL DEFENSE   (United States)

^c NATIONAL INSTITUTE OF MENTAL HEALTH   (United States)

Author keywords

Adhesion molecule; Keratinocyte; Laminin 5; Protease inhibitor; Skin blistering; Ssulphur mustard

Indexed keywords

1,10 PHENANTHROLINE; ALKYLATING AGENT; GLYCOPROTEIN; KALININ; LAMININ ALPHA3 PROTEIN; LAMININ BETA3 PROTEIN; LAMININ GAMMA2 PROTEIN; MUSTARD GAS; PROTEIN SUBUNIT; PROTEINASE; SERINE PROTEINASE INHIBITOR; UNCLASSIFIED DRUG;

ARTICLE; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; DIAGNOSTIC VALUE; DISEASE MARKER; EPIDERMIS CELL; EXPOSURE; HUMAN; HUMAN CELL; KERATINOCYTE; PATHOPHYSIOLOGY; PROTEIN DEGRADATION; PROTEIN DETERMINATION; SKIN TOXICITY;

BIOLOGICAL MARKERS; CELL ADHESION MOLECULES; CELLS, CULTURED; CYSTEINE PROTEINASE INHIBITORS; DERMATOLOGIC AGENTS; ENVIRONMENTAL EXPOSURE; HUMANS; KERATINOCYTES; LAMININ; LEUCINE; MUSTARD GAS; PHENANTHROLINES; PROTEASE INHIBITORS; SERINE PROTEINASE INHIBITORS;

EID: 37249071278     PISSN: 09066705     EISSN: 16000625     Source Type: Journal    
DOI: 10.1111/j.1600-0625.2007.00632.x     Document Type: Article

References (34)

1. Dacre J C, Goldman M. Toxicology and pharmacology of the chemical warfare agent sulfur mustard. Pharm Rev 1996: 48: 289-326.
2. Sidell F R, Urbanetti J S, Smith W J, Hurst C G. Vesicants. In: Zajtchuk R, Bellamy RF, eds. Textbook of Military Medicine: Medical Aspects of Chemical and Biologic Warfare. Washington, DC: Office of the Surgeon General at TMM Publications, Borden Institute, Walter Reed Army Medical Center, 1997: 197-228.
3. Meier H L, Millard C, Moser J. Poly (ADP-ribose) polymerase inhibitors regulates the mechanism of sulfur mustard-initiated cell death in human lymphocytes. J Appl Toxicol 2001: 20: S93-S100.
4. Smith K J, Smith W J, Hamilton T et al. Histopathologic and immunohistochemical features in human skin after exposure to nitrogen and sulfur mustard. Am J Dermatopathol 1998: 20: 22-28.
5. Nishiyama T, Amano S, Tsunenaga M et al. The importance of laminin 5 in the dermal-epidermal basement membrane. J Dermatol Sci 2000: 24: S51-S59.
6. Rousselle P, Lunstrum G P, Keene D R, Burgeson R E. Kalinin: An epithelium-specific basement membrane adhesion molecule that is a component of anchoring filaments. J Cell Biol 1991: 114: 567-576.
7. Green K J, Jones J C R. Desmosomes and hemidesmosomes: Structure and function of molecular components. FASEB J 1996: 10: 871-881.
8. Marinkovich M P, Lunstrum G P, Burgeson R E. The anchoring filament protein kalinin is synthesized and secreted as a high molecular weight precursor. J Biol Chem 1992: 267: 17900-17906.
9. Goldfinger L E, Stack M S, Jones J C. Processing of laminin-5 and its functional consequences: Role of plasmin and tissue-type plasminogen activator. J Cell Biol 1998: 141: 255-265.
10. Miyazaki K, Kikkawa Y, Umeda M. A large cell-adhesive scatter factor secreted by human gastric carcinoma cells. Pro Natl Acad Sci USA 1993: 90: 11767-11771.
11. Rousselle P, Aumailley M. Kalinin is more efficient than laminin in promoting adhesion of primary keratinocytes and some other epithelial cells and has a different requirement for integrin receptors. J Cell Biol 1994: 125: 205-214.
12. Pulkkinen L, Christiano A M, Airenne T, Haakana H, Tryggvason K, Uitto J. Mutations in the gamma 2 chain gene (LAMC2) of kalinin/laminin 5 in junctional forms of epidermolysis bullosa. Nat Genet 1994: 6: 293-298.
13. Aberdam D, Galliano M F, Vailly J et al. Herlitz's junctional epidermolysis bullosa is linked to mutations in the gene (LAMC2) for the gamma2 subunit of nicein/kalinin (laminin-5). Nat Genet 1994: 6: 299-304.
14. Smith K J, Hurst C G, Moeller R B, Skelton H G, Sidell F R. Sulfur mustard: Its continuing threat as a chemical warfare agent, the cutaneous lesions induced, progress in understanding its mechanism of action, its long-term health effects, and new developments for protection and therapy. J Am Acad Dermatol 1995: 32: 765-776.
15. Broomfield C A, Gross C L. Stability of sulfur mustard in a two phase storage configuration. In: Broomfield C A, Gross C L, eds. Proceedings 1989 Medical Defense Bioscience Review, AD B139 55. US: Army Medical Research Institute of Chemical Defense, Aberdeen Proving Ground, MD, 1989: 433-435.
16. Leng Y, Chase T N, Bennett C. Muscarinic receptor stimulation induces translation of an α-synuclein oligomer from plasma membrane to a light vesicle fraction in cytoplasm. J Biol Chem 2001: 276: 28212-28218.
17. Ishida H, Zhang X, Ericson K, Ray P. Botulinum toxin type A targets RhoB to inhibit lysophosphatidic acid-stimulated actin reorganization and acetylcholine release in nerve growth factor-treated PC12. J Pharm Exp Ther 2004: 310: 881-889.
18. Wang Z Y, Sosne G, Kurpakus-Wheater M. Plasminogen activator inhibitor-1 (PAI-1) stimulates human corneal epithelial cell adhesion and migration in vitro. Exp Eye Res 2005: 80: 1-8.
19. Ray P, Chakrabarti A K, Broomfield C A, Ray R. Sulfur mustard-stimulated protease: A target for antivesicant drugs. J Appl Toxicol 2002: 22: 139-140.
20. Matsui C, Wang C K, Nelson C F, Bauer E A, Hoeffler W K. The assembly of laminin-5 subunits. J Biol Chem 1995: 270: 23496-23503.
21. Aumailley M, Smyth N. The role of laminins in basement membrane function. J Anat 1998: 193: 1-21.
22. Fassihi H, Wong T, Wessagowit V, McGrath J A, Mellerio J E. Target proteins in inherited and acquired blistering skin disorders. Clin Exp Dermatol 2006: 31: 252-259.
23. Lazarova Z, Hsu R, Yee C, Yancey K B. Human anti-laminin-5 autoantibodies induce subepidermal blister in an experimental human skin graft model. J Invest Dermatol 2000: 114: 178-184.
24. Grando S A. Cholinergic control of epidermal cohesion. Exp Dermatol 2006: 15: 265-282.
25. Giannelli G, Falk-Marzillier J, Schiraldi O, Stetler-Stevenson W G, Guaranta V. Induction of cell migration by matrix metalloprotease-2 cleavage of laminin-5. Science 1997: 277: 225-228.
26. Werrlein R J, Madren-Whalley J S. Multiphoton microscopy: An optical approach to understanding and resolving sulfur mustard lesions. J Biomed Opt 2003: 8: 396-409.
27. Papirmeister B, Gross C L, Meier H L, Petrali J P, Johnson J B. Molecular basis for mustard-induced vesication. Fundamen Appl Toxicol 1985: 5: S134-S149.
28. Vonderheid E C, Tan E T, Kantor A F, Sharger L, Micaily B, VanScott E J. Long term efficacy, curative potential and carcinogenicity of topical mechlorethamine chemotherapy in cutaneous T cell lymphoma. J Am Acad Dermatol 1989: 20: 416-428.
29. Adams V R, Bence A K. Guide for the administration and use of cancer chemotherapeutic agents. McMahonMed: Oncol Spe Edn 2004: 7: 147-163.
30. Zhang Z, Peters B P, Montriro-Riviere N A. Sulfur mustard alkylates laminin by cross linking. Toxicologist 1994: 14: 428.
31. Byrne M P, Broomfield C A, Stites W E. Mustard gas crosslinking of protein through preferential alkylation of cysteines. J Prot Chem 1996: 15: 131-136.
32. Lindsay C D, Rice P. Assessment of the biochemical effects of percutaneous exposure of sulphur mustard in an in vitro human skin system. Hum Exp Toxicol 1996: 15: 237-244.
33. Lindsay C D, Rice P. Changes in connective tissue macromolecular components of Yucatan mini-pig skin following application of sulphur mustard vapour. Hum Exp Toxicol 1995: 14: 341-348.
34. Lindsay C D, Hambrook J L, Brown R F R, Platt J C, Knight R, Rice P. Examination of changes in connective tissue macromolecular components of large white pig skin following application of lewisite vapour. J Appl Toxicol 2004: 24: 37-46.