ABSTRACT
Treatment of full-thickness wounds with A. vera, on rats resulted in increased biosynthesis of collagen and its degradation. A corresponding increase in the urinary excretion of hydroxyproline was also observed. Elevated levels of lysyl oxidase also indicated increased crosslinking of newly synthesised collagen. The results suggest that A. vera influences the wound healing process by enhancing collagen turnover in the wound tissue.
Subject(s)
Aloe , Animals , Collagen/biosynthesis , Collagenases/metabolism , Hydroxyproline/urine , Male , Plants, Medicinal , Protein-Lysine 6-Oxidase/metabolism , Rats , Rats, Wistar , Skin/injuries , Wound HealingABSTRACT
Effects of oral and topical administration of an alcoholic extract of C. asiatica on rat dermal wound healing was studied. The extract increased cellular proliferation and collagen synthesis at the wound site, as evidenced by increase in DNA, protein and collagen content of granulation tissues. Quicker and better maturation and crosslinking of collagen was observed in the extract-treated rats, as indicated by the high stability of acid-soluble collagen and increase in aldehyde content and tensile strength. The extract treated wounds were found to epithelialise faster and the rate of wound contraction was higher, as compared to control wounds. The results show that C. asiatica produced different actions on the various phases of wound repair.
Subject(s)
Animals , Male , Plant Extracts/pharmacology , Plant Leaves/chemistry , Plants, Medicinal/chemistry , Rats , Rats, Wistar , Skin/injuries , Wound Healing/drug effectsABSTRACT
Non-enzymatic glycosylation of rat tail tendon collagen was examined by incubation with D-glucose in vitro. The changes in molecular parameters such as viscosity, thermal stability, electrophoretic mobility and solubility were determined on nonenzymatically glycosylated collagen in vitro. Tendons incubated with 8 and 24 mg glucose/ml showed an increase in dissolution temperature and a l·6-3-fold increase in thermal isometric tension respectively when compared to tendons incubated in the absence of glucose, indicating the formation of new intermolecular bonds. This conclusion was further supported by the decreased solubility of glycosylated collagen in 0·5 Ν acetic acid and the change in sub-unit composition as measured from the sodium dodecyl sulphate Polyacrylamide gel electrophoresis pattern. Glycosylated collagen gave a characteristic absorption spectra (λmax 248 nm) as distinct from that of control (λmax 242 nm). Denaturation temperature of glycosylated collagen, as determined from temperature dependent viscosity measurements, was reduced. These studies indicate that glycosylation affects the molecular interactions as well as the crosslinking of collagen.