Premium
Increased deposition of fibulin‐2 in solar elastosis and its colocalization with elastic fibres
Author(s) -
Hunzelmann N.,
Nischt R.,
Brenneisen P.,
Eickert A.,
Krieg T.
Publication year - 2001
Publication title -
british journal of dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.304
H-Index - 179
eISSN - 1365-2133
pISSN - 0007-0963
DOI - 10.1046/j.1365-2133.2001.04337.x
Subject(s) - colocalization , fibulin , deposition (geology) , elastin , biophysics , elastic fiber , materials science , pathology , chemistry , medicine , microbiology and biotechnology , biology , extracellular matrix , paleontology , sediment
Background Fibulin‐2 is a 195‐kDa protein belonging to a novel family of extracellular matrix proteins that might be involved in microfibril and elastic fibre organization. Objectives To determine the localization of fibulin‐2 in relation to elastic fibres in normal skin and in solar elastosis characterized by increased elastotic material in the papillary dermis. Methods The expression and synthesis of fibulin‐2 was investigated by means of in situ hybridization, immunohistochemistry and Western blot analysis in normal and photoaged skin. Results Immunohistochemistry and elastic tissue staining revealed that fibulin‐2 deposition mainly colocalized with microfibrils and elastin fibres, with a marked staining of elastotic material in solar elastosis. Western blot analysis demonstrated that in photoaged skin fibulin‐2 showed the same electrophoretic mobility as in sun‐protected skin. However, in actinic elastosis the amount of fibulin‐2 was significantly higher. In addition, smaller degradation products were detectable, presumably reflecting increased proteinase activity in photodamaged skin. Conclusions This study shows that deposition of fibulin‐2 and elastin is highly co‐ordinated, indicating that this protein plays an important role in elastic fibre and microfibril formation in normal and actinically damaged skin.