THE STRUCTURE OF HUMAN SKIN COLLAGEN AS STUDIED WITH THE ELECTRON MICROSCOPE

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Abstract
1. The structure of the collagen fibrils of normal human skin corium has been investigated with the electron microscope. 2. Under the conditions of observation the fibrils ranged in width from about 700 to 1,400 A with 1,000 A as the value occurring most frequently. They showed little tendency to fray longitudinally as is characteristic of tendon fibrils; when fracture of fibrils occurred it was usually in planes transverse to the axis. 3. The axial repeating periods observed in fibrils stained with phosphotungstic acid or shadowed with chromium or platinum range from about 500 to 800 A, the maximum occurring between 620 and 660 A. The average period in fibrils from infant skin does not differ significantly from that of adult and aged skin. 4. Depending on conditions of preparation, intraperiod fine structure, in the form of cross-bands, was observed in varying detail. The most detailed pattern commonly observed contains six bands of characteristic density and position. 5. Shadowed plastic replicas of dried collagen fibrils reproduce much of the structure commonly seen in shadowed fibrils. Replicas of moist fibrils show considerably less surface contouring than do dried fibrils. Replicas from smears of connective tissue fragments on glass show detailed structure, indicating the feasibility of applying this technique to biopsy material. 6. Infant skin differs from adult skin in having considerably greater amounts of amorphous material, little of which is strongly adherent to the collagen fibrils.