Search results for "Collagen metabolism"
showing 3 items of 3 documents
Collagens in the injured porcine intervertebral disc
1994
Spinal pain often is thought to be due to degeneration and mechanical failure of the intervertebral disc. Since the mechanical strength of the tissue depends on collagen fibers, the present study was designed to investigate the reactions in collagen metabolism after an experimentally induced disc injury. Five domestic pigs underwent an incision in the anterior part of the annulus fibrosus of disc L4-L5 through a retroperitoneal approach. The animals were killed 3 months postoperatively, and the injured discs and intact discs (controls) from different animals were removed for chemical analysis. Slices were cut from seven different parts across the disc. The concentration of total collagen (h…
Enhanced prolylhydroxylase activity in the posterior annulus fibrosus of canine intervertebral discs following long-term running exercise
2010
The effect of long-term excercise on the intervertebral disc collagen concentration (hydroxyproline), collagen-synthesizing enzymes (prolyl-4-hydroxylase, PH, and galactosyl-hydroxylysyl glucosyltransferase, GGT) and hydroxypyridinium crosslinks was studied in ten female beagle dogs. The dogs were run on a treadmill for 1 year starting at the age of 15 weeks. The daily running distance was gradually increased to 40km, which distance the dogs ran for the final 15 weeks. Ten untrained dogs from the same breeding colony served as controls. The nucleus pulposus and anterior and posterior halves of the annulus fibrosus of C2-3, T10-12, L4-5 disc segments were analysed. Crosslinks were measured f…
Biochemical, morphological and immunological findings in a patient with a cutis laxa-associated inborn disorder (De Barsy syndrome).
1986
Clinical symptoms of a male infant are described and compared with cases now classified as the De Barsy syndrome, a distinct disorder related to cutis laxa. Morphologically, clastic fibres in skin were frayed and reduced in number and density. The collagen fibril network was normal. Biochemical studies on collagen metabolism in a skin specimen and in cultured skin fibroblasts showed a normal amino acid content and a normal electrophoretic pattern of collagen constituents. The chemotactic migration of cultured fibroblasts was diminished when compared with fibroblasts from donors of different age groups. Immunological investigations revealed an impaired granulocyte function.