Elastic fiber during development and aging
| Autor: | M. Baccarani-Contri, I. Pasquali-Ronchetti |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
Histology
integumentary system biology Biglycan Papillary dermis macromolecular substances Anatomy Matrix (biology) Desmosine Medical Laboratory Technology chemistry.chemical_compound medicine.anatomical_structure chemistry Dermis Biophysics biology.protein medicine Instrumentation Elastin Fibrillin Elastic fiber |
| Zdroj: | Microscopy Research and Technique. 38:428-435 |
| ISSN: | 1097-0029 1059-910X |
| DOI: | 10.1002/(sici)1097-0029(19970815)38:4<428::aid-jemt10>3.0.co;2-l |
| Popis: | Elastin molecules aggregate in the extracellular space where they are crosslinked by stable desmosine bridges. The resulting polymer is structurally organized as branched fibers and lamellae, which, in skin, are wider (a few microns) in the deep dermis and become progressively thinner (fraction of a micron) towards the papillary dermis. Several general and local factors seem to regulate elastin gene expression, deposition and degradation. In skin, the volume density of the elastin network increases from birth up to maturity, when it accounts for about 3-4% of the tissue. However, its amount and distribution depend on dermis areas, which are different among subjects and change with age. Several matrix molecules (glycosaminoglycans, decorin, biglycan, osteopontin) have been found to be associated with elastin into the normal fiber, and several others have been recognized within pathologic elastic fiber (osteonectin, vitronectin, alkaline phosphatase in PXE). With age, and in some pathologic conditions, skin elastin may undergo irreversible structural and compositional changes, which seem to progress from localized deposition of osmiophilic materials to the substitution of the great majority of the amorphous elastin with interwoven filaments negative for elastin specific antibodies. |
| Databáze: | OpenAIRE |
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