-20-and-at-least-10-when-analysed-as-collagens-on-CMcellulose-chromatography-a

3. Sodium dodecyl sulphate/polyacrylamide-gel electrophoresis of the procollagens, the collagens and their CNBr peptides was used to confirm the identity of the collagen types. 4. In serum-free media extensive conversion of type-I procollagen, but not of type-III procollagen, into collagen was observed, suggesting that a specific type-I procollagen peptidase was produced. 5. ordinary squalane cleanser of collagen synthesis was not significantly different from that obtained with fibroblasts derived from Effects of 3-hydroxy-3-methylglutaryl-coenzyme a reductase inhibitor pravastatin on membrane lipids and membrane associated functions of Methanothermobacter The role of archaeal membrane and its lipid constituents was investigated in bioenergetic functions of Methanothermobacter thermautotrophicus.

The effects were determined of the 3-hydroxy-3-methylglutaryl-coenzyme A reductase inhibitor, pravastatin, on lipid composition, and its impact on some bioenergetic functions of treated cells. Pravastatin remarkably inhibited the growth of M. thermautotrophicus. On membrane level, pravastatin treatment modulated the composition of the mixture of squalene and hydrosqualene derivatives as well as the activities of ATPase, A1Ao-ATP synthase and Na+/H+ antiporter. SDS-PAGE of chloroform-methanol extracts of membranes from control and pravastatin-treated cells revealed changes in the amount of AtpK proteolipids, which suggests that pravastatin modifies cell-membrane composition, hereby modulating the properties of some membrane-bound enzymes participating in energy transformation in methanoarchaea.Effect of long-term ethanol feeding on rat liver interstitial collagens.Long-term administration of ethanol to rats over a 12-month period was used in an attempt to compare the altered collagen metabolism in liver damaged rats with that in humans having alcoholic liver disease.

The percent collagen in the rat liver increased nearly twofold during this period, but no increase in the rate of collagen biosynthesis was dectected by using pulse, radiolabel proline incorporation into hydroxyproline. Fibrosis was not detectable by histological methods nor were any alterations found in the relative proportions of the genetically distinct type I and type III interstitial collagens. These results demonstrates a minimal yet positive effect of long-term ethanol consumption in rats, with simultaneous increases in both type I and type III hepatic collagens.Bioassay-guided evaluation of wound healing effect of fatty acids-incorporated PURPOSE: To evaluate the effects of fatty acids-incorporated collagen-based dressing films on wound healing in rodents.METHODS: Therefore, surgical wounds were performed in the back of 80 Wistar rats, and dressed with collgane-based films (COL), and collagen-based films containing fatty acids (AGEF50 and AGEF100). squalane oil were regarded as controls (CTR). The animals were euthanized after three, seven, 14 and 21 days, and the macroscopic wound contraction rates (WRC) were assessed.

The wounded area was also analyzed by conventional and polarized light microscope.RESULTS: No sign of abscess or hypertrophic scar formation was observed in none of the groups. At seven days, the WRR of AGEF50 was significantly higher than CTR (p<01), whereas at 14 days, both AGE 50 and AGE100 showed a significant increase of the WRR compared to CTR (p<001) and COL (p<01). Both films promoted increased influx of neutrophils at three days (p<01), but reduced significantly the mononuclear infiltrate at 14 days (p<05). It was also observed earlier maturation of the granulation tissue, full epithelization and cutaneous appendages development, as well as better collagenization, in AGEF50 CONCLUSION: The application of AGEF50/100 as wound dressing improved wound Immuno-scanning electron microscopy of collagen types I and III in human vocal Wisconsin-Madison, Madison, Wisconsin, USA.OBJECTIVES: This study was undertaken to identify the types of collagen fibrils in the extracellular matrix of the human vocal fold lamina propria.METHODS: Human vocal folds were obtained from 3 autopsy cases less than 65 years of age.

The vocal fold specimens were labeled by primary antibodies of anti-type I and anti-type III collagens, and then by secondary antibody conjugated with 15 nm colloidal gold. The specimens were observed with a scanning electron microscope. Secondary electron imaging and backscatter electron imaging of high-resolution field emission scanning electron microscopy were used to detect gold particles indicating immunolabeling.RESULTS: Type III collagen-labeling gold particles were abundant on the fibrils constructing collagenous fibers, whereas type I collagen-labeling gold particles were sparsely present on fibrils in collagenous fibers. A few reticular fibers were labeled by both collagen type I and collagen type III.CONCLUSIONS: The results suggest that collagen type I coexists with collagen type III in fibrils of both collagenous fibers and reticular fibers.[Influence of x-rays on depolymerization of lathyric collagen fibers Irradiation of native collagen from lathyric rats in solution reduces the depolymerisation speed in the cold of fibres formed by gelification at 37 degrees C, rendering it thus comparable to the speed observed with normal collagen.