Reference : Basement membrane components and galactosylhydroxylysyl glucosyltransferase in suction b...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/83792
Basement membrane components and galactosylhydroxylysyl glucosyltransferase in suction blisters of human skin.
English
Oikarinen, A. [ > > ]
Savolainen, E. R. [ > > ]
Tryggvason, K. [ > > ]
Foidart, Jean-Michel mailto [Université de Liège - ULg > Département des sciences cliniques > Gynécologie - Obstétrique - Labo de biologie des tumeurs et du développement >]
Klistala, U. [ > > ]
1982
British Journal of Dermatology
Blackwell Publishing
106
3
257-66
Yes (verified by ORBi)
International
0007-0963
1365-2133
Oxford
United Kingdom
[en] Basement membrane components and collagen biosynthesis were studied in suction blisters in human skin. The basement membrane components were characterized by immunofluorescence using specific antibodies to type IV collagen, laminin and fibronectin, and collagen biosynthesis was studied by assaying galactosylhydroxylysyl glucosylatransferase. In suction blisters, the separation of epidermis and dermis occurred above the lamina lucida, indicating that the basement membrane, composed of lamina lucida and lamina densa, forms a mechanically strong entity. During the regeneration phase of blisters, type Iv collagen and laminin were not observed in the old epidermal blister roof. This indicates that keratinocytes when separated from the underlying basement membrane or connective tissue do not synthesize laminin or type IV collagen. Galactosylhydroxylysyl glucosyltransferase activity could be demonstrated in blister fluid and was about the same as in serum when expressed on the basis of protein in fresh blisters. It increased by 2-3 fold during the repair of blisters, indicating that there was local production of this enzyme. Further studies revealed that pure epidermis contained galactosylyhdroxylysyl glucosyltransferase and hydroxyprolineand this suggests that epidermis may synthesize some collagen type which, according to these studies, is not type IV (basement memebrane) collagen.
http://hdl.handle.net/2268/83792

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