Biomedical subjects

J Grizard

Publications and source records attributed to J Grizard.

76 records · Page 5Linked to original sources

PubMedDate not supplied

Metabolic clearance of insulin from the cerebrospinal fluid in the anesthetized rat.

Infusion of 125I-(Tyr A14)-insulin at tracer doses into the cerebrospinal fluid (CSF) resulted in a slow rate of increase in the CSF-labeled insulin during the first 2 hours with a plateau thereafter. Labeled insulin was cleared from the CSF at a higher rate than 3H-inulin, a marker of CSF bulk flow. The labeled insulin was mainly distributed in all the ventricular and periventricular brain regions. Small amounts of degraded insulin appeared in the CSF. Coinfusion with an excess of unlabeled insulin impaired the clearance and degradation of labeled insulin. It also inhibited the labeling in medial hypothalamus, olfactory bulbs and brain stem. In contrast, coinfusion of ribonuclease B (used to test the specificity of uptake) was without any effect. It was concluded that there is an active insulin intake from CSF into brain specific compartments that is presumably essential for the effects of insulin on brain function.

Anesthesia↗

PubMedDate not supplied

Insulin action on skeletal muscle protein metabolism during catabolic states.

Insulin plays a major role in the regulation of skeletal muscle protein turnover but its mechanism of action is not fully understood, especially in vivo during catabolic states. These aspects are presently reviewed. Insulin inhibits the ATP-ubiquitin proteasome proteolytic pathway which is presumably the predominant pathway involved in the breakdown of muscle protein. Evidence of the ability of insulin to stimulate muscle protein synthesis in vivo was also presented. Many catabolic states in rats, e.g. streptozotocin diabetes, glucocorticoid excess or sepsis-induced cytokines, resulted in a decrease in insulin action on protein synthesis or degradation. The effect of catabolic factors would therefore be facilitated. In contrast, the antiproteolytic action of insulin was improved during hyperthyroidism in man and early lactation in goats. Excessive muscle protein breakdown should therefore be prevented. In other words, the anabolic hormone insulin partly controlled the 'catabolic drive'. Advances in the understanding of insulin signalling pathways and targets should provide information on the interactions between insulin action, muscle protein turnover and catabolic factors.

Animals↗

PubMedDate not supplied

Effect of short-term starvation on Leydig cell function in adult rats.

An experiment was carried out to analyze the effect of 3 days of starvation on the Leydig cell function in adult rats. Starvation markedly decreased plasma insulin and testosterone levels (p < .05). The weight of testes was maintained, whereas the testicular interstitial fluid volume decreased (p < .05). The level of testosterone decreased in this fluid (60%), whereas insulin levels showed no significant change. Purified Leydig cells showed normal LH/hCG binding in fasted rats but low insulin binding. The ability of these cells to produce testosterone in vitro was normal under both basal conditions and hCG stimulation in the absence and presence of insulin in the incubation medium. These data suggest that there is no gross impediment in the Leydig cell capacity to produce testosterone that might explain the starvation-associated decrease in plasma testosterone.

Animals↗

PubMedDate not supplied

Insulin binding sites in solubilized membranes from rat testis. Effect of age.

The effect of aging on the binding of insulin to testicular solubilized microsomal membranes was studied in rats. The insulin receptor was solubilized in triton x-100 and its properties compared with those of solubilized membranes of rat liver. At the three life stages studied (21, 38-40 and 75-80 days) binding specificity in testicular solubilized membranes showed the following order of competition relative to porcine insulin (100): proinsulin (7), guinea-pig insulin and IGF-I (less than 1). Scatchard analysis of the binding data always gave curvilinear plots with a high affinity of about 0.9 10(9) M-1. With aging, high affinity binding expressed as fmol per mg protein did not vary in the testis whereas it decreased in the liver. Where expressed as fmol bound per testis, the binding of insulin increased 14-fold between the age of 21 days and adult age. It is concluded that the characteristics of solubilized membranes receptors for insulin are roughly similar in the testis and liver but the effect of age on the number of high affinity binding sites is quite different in the two tissues.

Aging↗