THE OXYTALAN FIBER: A PREVIOUSLY UNDESCRIBED CONNECTIVE TISSUE FIBER

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Abstract
Oxidation of formalin-fixed deparaffinized sections of complete outopsies of mice, and tendons and jaws of man with peracetic acid resulted in the staining of certain connective tissue fibers of periodontal membranes, tendons, ligaments and the perineurium with aldehyde fuchsin. These fibers were not found in connective tissues such as in skin and parenchymatous organ stroma, but were located principally in areas subjected to stress. These fibers were found to differ significantly from previously described connective tissue fibers and are named oxytalan fibers. After peracetic acid oxidation oxytalan fibers were found to stain with aldehyde fuchsin, some with orcein, or resorcin fuchsin, but none with orcinol-new fuchsin or Verhoeff s stain for elastic fibers. The stainable component of oxytalan fibers is removed by hyaluronidase or lysozyme if they are previously oxidized with peracetic acid. They are also digested by elastase if they are previously oxidized with peracetic acid; peracetic acid was not required for digestion of elastic fibers. Fresh jaws extracted with 2% NaOH for 72 hours and subsequently embedded and sectioned, were unreactive for oxytalan fibers with the peracetic-aldehyde fuchsin stain. The aldehyde fuchsin staining reaction was not prevented by acetylation, deamination or by aldehyde blockade after peracetic acid oxidation. A 16 hour methylation in 0.1N HC1 at 60[degree] C interposed wither before or after peracetic acid oxidation prevented the reaction. The reaction of aldehyde fuchsin with a sulfonic acid, sulfate, disulfide or sulfhydryl in oxytalan fibers was ruled out. On the basis of the above observations, the stainable component of oxytalan fibers is considered to be a mucopolysaccharide or mucoprotein-like substance. The peracetic-aldehyde fuchsin stain does not react with reticular fibers, and stains for reticulin do not demonstrate these fibers.