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C Susini

Publications and source records attributed to C Susini.

At least 73 records · Page 4Linked to original sources
PubMed1986

Studies on human pancreatic acini: action of secretagogues on amylase release and cellular cyclic AMP accumulation.

A technique for preparing a suspension of dispersed functional acini from human pancreas has been developed. The changes in pancreatic enzyme secretion and accumulation of cellular cyclic AMP caused by various secretagogues have been studied. Ca2+-mobilizing agents stimulated amylase release from human pancreatic acini. The relative potencies with which secretagogues increased amylase release were as follows: gastrin-releasing peptide's potency (Ec50, 0.1 +/- 0.01 nM) was greater than bombesin 14's (Ec50, 0.2 +/- 0.01 nM), which was greater than litorin's (Ec50, 0.6 +/- 0.18 nM), which was greater than bombesin 9's (Ec50, 6 +/- 0.1 nM). For CCK-peptides, the relative potencies were as follows: CCK-39's potency (Ec50, 0.28 +/- 0.15 microM) was equal to cerulein's (Ec50, 0.3 +/- 0.07 microM). Both of these potencies were greater than CCK-8's (Ec50, 1.6 +/- 0.1 microM), which was greater than that of CCK-4. Carbamyl choline was poorly potent (Ec50 greater than 1 mM). The 12-O-tetradecanoylphorbol-13-acetate (TPA) was active from 0.1 nM to 0.1 microM. Neither secretin nor VIP increased amylase release from human pancreatic acini but they did cause an accumulation of cellular cyclic AMP, secretin (Ec50, 0.5 +/- 0.2 nM) being more potent than VIP.

Amylases↗
PubMed1985

Tumor promoter inhibition of cellular binding of somatostatin.

Tumor promoting phorbol esters inhibited the binding of 125I-[Tyr11] somatostatin to isolated acinar cells from guinea-pig pancreas. Maximal inhibition reached 69.7 +/- 5% at 1 microM TPA. Receptor affinity was decreased by 2.5-fold without change in binding capacity. The ability of TPA in inhibiting somatostatin binding was decreased in 30 nM Ca2+ medium, abolished at 4 degrees C or in a membrane preparation. The effect of caerulein, a secretagogue which also caused loss of binding, and that of TPA were not additive. We concluded that TPA inhibits somatostatin binding not by binding directly at the active site of somatostatin receptor. TPA may act at a later point than caerulein via a similar pathway to modulate somatostatin receptor affinity.

Amylases↗
PubMed1984

125I-(Thr34, Nle37)- CCK31-39 a non oxidizable tracer for the characterization of CCK receptor on pancreatic acini and radio-immunoassay of C-terminal CCK peptides.

A derivative of the C-terminal nonapeptide of CCK, namely (Thr34, Nle37) - CCK31-39 was radio-iodinated by conjugation with 125I-Bolton-Hunter reagent. The labelled peptide was purified by RP-HPLC on a C-18 column. Validation of the iodinated peptide was performed by measuring its biological integrity and by studying its binding characteristics on pancreatic acini. 125I-(Thr, Nle)-CCK-9 present the same ability to stimulates amylase release than (Thr, Nle)- CCK-9 and CCK-8. Binding of the radio-ligand to CCK receptors is specific, reversible, saturable. Inhibition of the binding by CCK-related peptides correlates well their biological potencies. 125I-(Thr, Nle)-CCK-9 is able to interact with high affinity CCK receptors. Furthermore, 125I-(Thr, Nle)-CCK-9 is recognized by C-terminal CCK directed antibodies. This reliable tracer could be used as a replacement of CCK-8 since it is protected from risks of oxidation.

Amylases↗
PubMed1984

Binding of somatostatin to pancreatic acinar cells.

The binding of 125I-[Tyr11]somatostatin to guinea pig pancreatic acini was saturable and temperature, protein, and radioligand concentration dependent. Dissociation rate was very slow (t1/2 = 193 +/- 24 min). Scatchard analysis revealed a single class of binding sites with a Kd of 0.28 +/- 0.02 nM and a maximal binding capacity of 72 +/- 10.6 fmol/mg prot. There was a strong correlation between binding capacity and extracellular calcium concentration. Incubating acini in EGTA-containing medium with no added Ca2+ caused a 50% decrease in maximal binding capacity with a decrease in receptor affinity. Furthermore, in the absence of calcium, bound somatostatin was rapidly released (t1/2 = 14 +/- 1 min). Subcellular fractionation studies and acid treatment of acini incubated with the tracer showed that most of the somatostatin binding sites were located on the cell surface. Agents that altered cellular calcium in pancreatic acini, such as analogues of cholecystokinin and cholinergic agents, also inhibited the binding of 125I-[Tyr11]somatostatin by a calcium-dependent process. We conclude that somatostatin binds to specific plasma membrane receptors to form a slowly reversible complex that is highly reactive with calcium. Cell calcium-mobilizing agents decrease the affinity of acinar somatostatin receptors for somatostatin.

Animals↗
PubMed1983

Binding of somatostatin to guinea-pig pancreatic membranes: regulation by ions.

Somatostatin receptors were characterized on guinea-pig pancreatic acini membranes using 125I-[Tyr11] somatostatin 14 as a radioligand. In 0.1 mM Ca2+ buffer the binding was saturable and slowly reversible, exhibiting a single class of high affinity binding sites (KD = 0.15 +/- 0.03 nM) with a maximal binding capacity (B max) of 178 +/- 18 fmol/mg protein. In 30 nM) free Ca2+ buffer, the binding was highly reversible. Affinity and B max were decreased by about 2-fold. Ca2+ exhibited an EC50 of 2.4 +/- 0.9 microM to potentiate the binding of somatostatin. Na+, but not K+, inhibited the binding: Bmax was decreased with no change in affinity. Somatostatin analogs inhibited the binding of 125I-[Tyr11] somatostatin 14. The relative potencies were: somatostatin 14 greater than somatostatin 28 = [Nle8]somatostatin 28 greater than [D Tryp8, D Cys14]somatostatin 14.

Animals↗
PubMed1983

Bimodal regulation of pancreatic exocrine function in vitro by somatostatin-28.

The action of natural and synthetic somatostatin-(1--28), [Nle8]somatostatin-(1--28), somatostatin-(15--28), and somatostatin-(1--14) was examined in dispersed acini from guinea pig pancreas. At high concentrations, the 28-amino acid form of somatostatin increased amylase release, outflux of 45Ca, cellular cGMP, and to a lesser extent cellular cAMP. The increase in amylase release was suppressed by dibutyryl cGMP but was not modified by theophylline or atropine. Binding of 125I-labeled [Thr28, Nle31] cholecystokinin-(25--33) was inhibited by [Nle8]somatostatin-(1--28). These effects required the entire 28-amino acid peptide and appeared to result from occupation of cholecystokinin receptors. It is postulated that they involve interactions between the C-terminal and the N-terminal sequences of the molecule with the participation of the amino acid in position 8. At low concentrations, natural and synthetic forms of somatostatin-(1--28) and somatostatin-(15--28) inhibited secretin- and vasoactive intestinal peptide (VIP)-stimulated increases in cellular cAMP concentration. No difference was found between the potency of somatostatin peptides, indicating that the tetradecapeptide somatostatin-(15--28) is sufficient to exert an inhibitory action on secretin- and VIP-stimulated cellular cAMP concentration. By contrast, the somatostatin fragment S-(1--14) was inactive on pancreatic cellular function.

Amylases↗
PubMed1981

Effects of somatostatin-14 and somatostatin-28 on bombesin-stimulated release of gastrin, insulin, and glucagon in the dog.

The effects of somatostatin-14 (S14) and somatostatin-28 (S28), a novel intestinal peptide containing somatostatin tetradecapeptide in its C-terminal position, on the bombesin-stimulated release of gastrin, insulin, and glucagon were tested. On iv infusion of bombesin, the increase in the level of glucagon was seen to be twice that of gastrin, and the insulin increase was 8 times that of gastrin. Plasma concentrations of somatostatin were not modified. S14 and S28 inhibited the release of gastrin, insulin, and glucagon; insulin release was inhibited most effectively, with glucagon release next, and gastrin release least inhibited. Based on the exogenous dose needed to produce equal effects, S28 was more potent than S14 on a molar basis, but based on the plasma concentrations needed to produce equal effects, S14 and S28 were equipotent.

Animals↗
PubMed1980

Somatostatin 28: effects on exocrine pancreatic secretion in conscious dogs.

The effect of somatostatin 28, a noval intestinal peptide containing somatostatin in its C-terminal portion, was tested on basal exocrine pancreatic secretion on conscious dogs and after stimulation by secretin (1 CU x kg-1 x hr-1), caerulein (37.5 ng x kg-1 x hr-1) or secretin (2 CU x kg-1 x hr-1) caerulein (37.5 ng x kg-1 x hr-1). We found differences in the inhibitory effect of somatostatin 28 on these three forms of stimulation. Bicarbonate secretion stimulated by secretin was inhibited only slightly by large doses of somatostatin 28, whereas small doses markedly inhibited stimulation by caerulein. Protein concentrations were inhibited only when secretin was the stimulant. Protein outputs to all forms of stimulation were inhibited. When compared with synthetic somatostatin 14, lower doses of somatostatin 28 were required to produce the same inhibitory effect on protein outputs stimulated by secretin alone and on volumes stimulated by caerulein alone.

Animals↗
PubMed1979

Adrenaline responsiveness of glucose metabolism in insulin-resistant adipose tissue of rats fed a high-fat diet.

The effects of adrenaline (0.5 microM) and the combination of adrenaline and insulin (1.7nM) on [6-14C]glucose metabolism were assessed in epididymal fat-pads from rats fed either a low- or high-fat diet. The response of lipolysis to adrenaline was clearly diminished in fat-fed rats. Insulin added to adrenaline inhibited the lipolysis by 50% regardless of the diet. Glucose utilization in adipose tissue of fat-fed rats was markedly stimulated by adrenaline (glucose uptake was increased 3-fold and the production of CO2 and the glycerol moiety of acylglycerol was increased 4-fold). However, adipose tissue from fat-fed rats was resistant to the effect of insulin to produce a further increase in adrenaline-stimulated glucose uptake. The intracellular capacity of lipogenesis on the one hand, and the production of CO2 and the glycerol moiety of acylglycerol on the other, are of prime importance in the action of insulin and adrenaline on glucose utilization in this model.

Adipose Tissue↗
PubMed1979

A new delay technique with application to ultrasound phased-array imaging systems.

In ultrasound phased-array imaging systems the receiver directivity pattern is steered by controlling the delay of echoes from the array elements. A new processing technique is introduced that provides the required delay first by properly phasing the echo carrier, and successively by delaying the echo envelope. This latter operation is based on a new analogue sampled-data delay-line. Independent control of phase delay offers a simple means of compensating for random phase errors due to non-uniformity of the array elements response.

Ultrasonics↗
PubMed1979

Mechanism of insulin resistance in adipocytes of rats fed a high-fat diet.

Insulin's ability to stimulate glucose metabolism is severely diminished in the adipose tissue of rats fed a high-fat diet as compared to that of rats fed a low-fat diet. To elucidate the mechanism for this effect we have measured the binding of insulin, the hormone effect on 2-deoxyglucose uptake and the major pathways of [1-(14)C]glucose metabolism, and the activity of lipogenesis-related enzymes in adipocytes of rats fed a low- or high-fat diet for 7 days. Rats fed high- or low-fat diets bound equal amounts of insulin per adipocyte at all insulin concentrations tested. Basal and maximally insulin-stimulated 2-deoxyglucose uptake per fat cell were reduced in high-fat-fed rats. However, the insulin stimulation over basal was the same in both groups (230%). Submaximal doses of insulin produced equivalent increments of 2-deoxyglucose uptake in both groups, as would be predicted by the binding studies. The effect of both submaximal and maximal insulin concentration on the labeling of CO(2) and fatty acids was markedly decreased by high-fat feeding. The insulin response of the glyceride-glycerol pathway was less severely, though significantly, reduced. Acetyl CoA carboxylase and malic enzyme in adipocytes of high-fat-fed rats were reduced to 13% of the activity in the low-fat-fed rats. Glucose-6-phosphate and 6-phosphogluconate dehydrogenases were decreased to 20% and 34% of their activities in low-fat-fed rats, respectively. These reductions paralleled the changes in insulin-stimulated glucose oxidation and fatty acid synthesis. The data therefore strongly suggest that the blunted response of glucose metabolism to insulin in adipocytes of high-fat-fed rats is a result of a decreased intracellular capacity to utilize glucose for lipogenesis.

Adipose Tissue↗
PubMed1978

Inhibition of exocrine pancreatic secretion by somatostatin in dogs.

The effect of somatostatin on the pancreatic exocrine response to different doses of exogenous stimuli and the somatostatin dose-response relationships on pancreatic secretion were studied in conscious dogs. Somatostatin caused a strong inhibition of basal or slightly stimulated pancreatic secretion but failed to inhibit the maximal responses, suggesting that somatostatin interacts with secretin or caerulein by a competitive mechanism. A higher maximal percentage of inhibition and a dose-response relationship was observed with protein outputs and enzyme concentrations. Volumes and bicarbonate outputs were also inhibited but the maximal percentage of inhibition was lower.

Animals↗