Biomedical subjects
Publications and source records attributed to F Gossé.
Recurrent post-traumatic dislocation of the hip joint without an accompanying fracture is very rare. Delayed reduction and a too short immobilization periods seems to favor redislocation. One case is presented together with a discussion of the operative therapy and the intraoperative pathological-anatomical findings with respect to the literature.
Laminaribiose and gentiobiose, two O-beta-linked disaccharides deriving from plant beta-glucans, were found to be hydrolyzed in the rat small intestine by an enzyme anchored into the brush border membrane of the enterocytes. Immunological and biochemical data, together with the developmental pattern of expression, support that this activity is carried out by the bifunctional enzyme involved in the hydrolysis of lactose and glycosylceramides: the lactase-phlorizin hydrolase complex.
During the degradation of intestinal sucrase-isomaltase by pancreatic proteinases, degradation of sucrase-active site precedes that of the isomaltase-active site in rats. In the present paper, we demonstrate that the extent of degradation of sucrase-isomaltase is altered by dietary manipulation in vivo. Adult rats were starved for 24 h and received either a standard diet (20 cal% protein, 55% carbohydrate) or an isocaloric high-protein, low-carbohydrate diet (70 cal% protein, 5% carbohydrate). Animals were killed 15 h after the refeeding. In rats fed a high-protein, low-carbohydrate diet, luminal trypsin activity was three times higher than controls, and sucrase activity in proximal ileum was significantly lower (P less than 0.001) than controls, whereas isomaltase activity was similar in both groups. In proximal jejunum, luminal trypsin activity was remarkably lower (P less than 0.01) than in proximal ileum in both groups; sucrase and isomaltase activity was similar in both groups. Crossed immunoelectrophoresis demonstrated that a degradation product of sucrase-isomaltase, i.e., isomaltase monomer, was present in a larger amount in rats fed a high-protein, low-carbohydrate diet. In rats with bypassed pancreatic ducts, the amount of this degradation product was decreased and effect of a high-protein, low-carbohydrate diet was abolished. Experiments with a sequential isolation of epithelial cells of proximal ileum revealed that sucrase activity was decreased along the entire height of the villus in animals fed a high-protein, low-carbohydrate diet.(ABSTRACT TRUNCATED AT 250 WORDS)
The short-term effects of high-protein/low-carbohydrate diet on aminopeptidase N activity were studied in the brush-border membranes of proximal jejunum and proximal ileum of adult rats. The animals were starved overnight and re-fed for 15 h either with a standard diet (20% protein, 55% carbohydrate, in terms of energy content) or with a high-protein/low-carbohydrate diet of equal energy content (70% protein, 5% carbohydrate). All rats consumed similar amounts of diet, and measurements were made 15 h after initiation of re-feeding. In the proximal jejunum a slight increase in aminopeptidase activity was observed after the high-protein intake. In contrast, considerable stimulation (52%) of the enzyme specific activity was obtained in the proximal ileum. This increase in ileal aminopeptidase activity was more prominent in the mature cells of the upper villus. To determine if the increase of aminopeptidase activity was due to an increased amount of enzyme protein, rocket immunoelectrophoresis was performed with detergent-solubilized brush-border protein from ileum on agarose gels containing anti-(rat brush-border) antiserum. When the same amount of enzyme activity was loaded on the gels, the peaks of immunoprecipitate for aminopeptidase were similar for animals fed on a standard or a high-protein diet. When the same amount of protein was loaded, the peak of immunoprecipitate for aminopeptidase was higher (81%) after a high-protein diet. These results showed that the high protein intake evoked an increase in aminopeptidase activity, with a concomitant increase in the amount of immunoreactive protein.