RESUMO
Twenty-six samples of human skin from three non-weight-bearing and 27 samples from three weight-bearing sites were obtained at autopsy from 11 subjects varying in age from 4 to 91 years. The dermis was idssected free of other tissues and after proteolytic digestion, the glycosaminoglycans were isolated quantitatively by ion-exchange chromatography. Analysis of the preparations showed that there was significantly more glycosaminoglycan in the dermis from weight-bearing sites (p less than 0.001). The major glycosaminoglycans were hyaluronic acid and dermatan sulfate with chondroitin sulfate as a minor component, but the relative proportions of these components were not significantly different in the two sets of samples (p greater than 0.1). It is suggested that the quantity of glycosaminoglycan in the dermis is influenced by the functional requirements of the dermis at that site.
Assuntos
Pé/análise , Glicosaminoglicanos/análise , Pele/análise , Adolescente , Adulto , Idoso , Criança , Pré-Escolar , Sulfatos de Condroitina/análise , Dermatan Sulfato/análise , Feminino , Calcanhar/análise , Ácidos Hexurônicos/análise , Humanos , Ácido Hialurônico/análise , Queratinas/análise , Masculino , Pessoa de Meia-Idade , Pressão , Pele/ultraestrutura , Dedos do Pé/análiseRESUMO
The glycosaminoglycan content and the axial periodicity of collagen was determined in various regions of the rabbit flexor digitorum profundus tendon. This tendon, which passes from the calf to the toes round the inner side of the ankle, contains a thickened sesamoid-like pad where it is subjected to friction and pressure. Other regions of the tendon are subject only to longitudinal tension. In tensional areas the axial periodicity of collagen was of the order of 62 nm and the tissue contained less than 0.2% proteoglycan on a dry weight basis. In the sesamoid-like region, however, the axial periodicity was a significant 13-15% less, and the proteoglycan constituted about 3.5% of the dry weight. Also, in the tensional areas the predominant glycosaminoglycan was dermatan sulphate, whereas in the sesamoid the predominant glycosaminoglycan was chondroitin sulphate. The possible interrelationships between collagen axial peroidicity and proteoglycan content in this tissue are discussed.
