Summary
Monoclonal antibodies recognizing the antiproteolytic compound α2-macroglobulin (MG) were used for immunohistological studies on normal human skin. MG-specific immunoreactivity was found to be localized to the papillary dermis and to be concentrated in the region of the epidermodermal junction. In view of these findings and the possible involvement of proteolytic enzymes and their inhibitors in blister formation, we asked whether MG occurs in the fluid of experimentally induced blisters. MG was identified (by western-blotting) and quantified (by a monoclonal antibody based enzyme immunoassay) in the fluid of experimentally induced suction blisters. Taken together, MG is present in such blister fluid in concentrations 6 times lower than in serum, but still in an antiproteolytic range. These findings allow suggestion of a possible role for the antiproteolytic compound MG in blister formation.
Similar content being viewed by others
References
Barrett AJ, Starkey PM (1973) The interaction of α2 macroglobulin with proteinases. Biochem J 133:709–724
Eisen AZ (1969) Human skin collagenase: relationship to pathogenesis of epidermolysis bullosa dystrophica. J Invest Dermatol 52:449–453
Fräki JE, Schechter NM, Lazarus GS (1983) Human skin proteinases as inflammatory mediators. Br J Dermatol [Suppl 25] 109:72–76
Justus C, Müller S, Kramer MD (1988) Monoclonal antibodies recognizing human α2 macroglobulin their use for one step affinity purification, quantification and immunohistological localisation of the proteinase inhibitor. Enzyme and Microbial Technology (in press)
Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–682
Oikarinen AI, Zone JJ, Razzaque AA, Kiistala U, Uitto J (1983) Demonstration of collagenase and elastase activity in the blister fluids from bullous skin diseases. Comparison between dermatitis herpetiformis and bullous pemphigoid. J Invest Dermatol 81:261–266
Saksela O (1985) Plasminogen activation and regulation of pericellular proteolysis. Biochim Biophys Acta 823:35–65
Towbin H, Staehelin T, Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 77:9837–9842
Van Leuven F (1982) Human α2 macroglobulin: structure and function. Trends Biochem Sci 7:185–187
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Kramer, M.D., Justus, C. The antiproteolytic compound α 2 in human skin. Arch Dermatol Res 280, 93–96 (1988). https://doi.org/10.1007/BF00417711
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00417711