scholarly journals Effect of glucose on polyphosphoinositide metabolism in isolated rat islets of Langerhans

1985 ◽  
Vol 227 (2) ◽  
pp. 483-489 ◽  
Author(s):  
W Montague ◽  
N G Morgan ◽  
G M Rumford ◽  
C A Prince
Keyword(s):  
B Cell ◽  
Islets Of Langerhans ◽  
Sugar Metabolism ◽  
Receptor Occupancy ◽  
Early Event ◽  
Coupling Mechanism ◽  
Rat Islets ◽  
Plasma Membrane Receptor ◽  
Rat Islets Of Langerhans ◽  
Phosphatidylinositol 4

The metabolism of inositol-containing phospholipids during insulin secretion was studied in rat islets of Langerhans preincubated with [3H]inositol to label their phospholipids. Glucose (20 mM) caused a rapid breakdown of phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 4-phosphate and an accumulation of inositol trisphosphate and inositol bisphosphate. This effect was maximal at 60s, did not require the presence of extracellular Ca2+, and was abolished by mannoheptulose (15 mM), but not by noradrenaline (1 microM). Mannose (20 mM) and DL-glyceraldehyde (10 mM) produced similar effects to those of glucose, but galactose (20 mM) and KCl (30 mM) were without effect. These results are compatible with the hypothesis that an early event in the stimulus-secretion coupling mechanism in the pancreatic B-cell is the rapid breakdown of polyphosphoinositides catalysed by phospholipase C. Moreover, they suggest that the breakdown of polyphosphoinositides is linked to sugar metabolism in the B-cell. This observation is important, since it demonstrates that events in a cell other than plasma-membrane receptor occupancy can promote polyphosphoinositide hydrolysis.

Opioid peptides in rat islets of Langerhans. Immunoreactive met- and leu-enkephalins and BAM-22P

Diabetes ◽  
1986 ◽  
Vol 35 (1) ◽  
pp. 52-57 ◽  
Author(s):  
K. I. Timmers ◽  
N. R. Voyles ◽  
C. King ◽  
M. Wells ◽  
R. Fairtile ◽  
...  
Keyword(s):  
Islets Of Langerhans ◽  
Opioid Peptides ◽  
Rat Islets ◽  
Rat Islets Of Langerhans

Effects of epicatechin on rat islets of Langerhans

Diabetes ◽  
1984 ◽  
Vol 33 (3) ◽  
pp. 291-296 ◽  
Author(s):  
C. S. Hii ◽  
S. L. Howell
Keyword(s):  
Islets Of Langerhans ◽  
Rat Islets ◽  
Rat Islets Of Langerhans

scholarly journals CYTOCHEMICAL LOCALIZATION OF ADENYL CYCLASE ACTIVITY IN RAT ISLETS OF LANGERHANS

1972 ◽  
Vol 20 (11) ◽  
pp. 873-879 ◽  
Author(s):  
S. L. HOWELL ◽  
MARGARET WHITFIELD
Keyword(s):  
B Cells ◽  
Islets Of Langerhans ◽  
Adenosine Triphosphate ◽  
Adenyl Cyclase ◽  
Cyclase Activity ◽  
Cytochemical Localization ◽  
Adenyl Cyclase Activity ◽  
Rat Islets ◽  
Rat Islets Of Langerhans ◽  
A And B Cells

A cytochemical method has been used to investigate the localization of adenyl cyclase activity in A and B cells of isolated rat islets of Langerhans. Adenosine triphosphate was initially utilized as substrate, the pyrophosphate liberated being precipitated by lead ions at its site of production. The specificity of the method was increased by the use of adenylyl-imidodiphosphate as an alternative substrate; this adenosine triphosphate analogue was not hydrolyzed by adenosine triphosphatase but provided an effective substrate for adenyl cyclase. Adenyl cyclase activity, which was found to retain its glucagon and fluoride sensitivity in glutaraldehyde-fixed tissue, was found exclusively and almost uniformly in the plasma membranes of A and B cells. Storage granule membrane, incorporated into the plasma membrane during secretion of the granule content by exocytosis, appeared to be devoid of adenyl cyclase activity.

scholarly journals Stimulation of Adenylate Cyclase by Ca2+ and Calmodulin in Rat Islets of Langerhans: Explanation for the Glucose-induced Increase in Cyclic AMP Levels

Diabetes ◽  
1980 ◽  
Vol 29 (1) ◽  
pp. 74-77 ◽  
Author(s):  
G. W. G. Sharp ◽  
D. E. Wiedenkeller ◽  
D. Kaelin ◽  
E. G. Siegel ◽  
C. B. Wollheim
Keyword(s):  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Islets Of Langerhans ◽  
Rat Islets ◽  
Rat Islets Of Langerhans ◽  
Stimulation Of

Immunological characterization of the guanine-nucleotide binding proteins Gi and Go in rat islets of Langerhans

1992 ◽  
Vol 8 (2) ◽  
pp. 103-108 ◽  
Author(s):  
N. S. Berrow ◽  
G. Milligan ◽  
N. G. Morgan
Keyword(s):  
G Proteins ◽  
Islets Of Langerhans ◽  
Pertussis Toxin ◽  
Nucleotide Binding ◽  
Molecular Forms ◽  
Antigenic Determinants ◽  
Guanine Nucleotide ◽  
Rat Islets ◽  
Guanine Nucleotide Binding ◽  
Rat Islets Of Langerhans

ABSTRACT Inhibition of insulin secretion from rat islets of Langerhans is known to involve at least one pertussis toxin-sensitive guanine-nucleotide binding (G) protein. We have used antisera raised against unique antigenic determinants of different members of the family of pertussis toxin-sensitive G proteins to identify these proteins in rat islets. Antiserum SG1, which recognizes both Gi1 and Gi2, reacted with an islet protein having an approximate Mr of 40 000. Antiserum IlC (Gi1 specific) failed to recognize any islet proteins, suggesting that Gi2 is present in much greater amounts than Gi1. Indeed, Gi1 levels were below the detection limit of a sensitive immunogold/silver-staining method, indicating that it may be absent from the cells of rat islets. Two different antisera were used to identify Go-like G proteins in rat islet homogenates. Both antisera reacted with a protein band which, under appropriate conditions, could be resolved to reveal two separate proteins of Mr 39–40 000. Thus, at least two molecular forms of Go are present in rat islets. Subcellular fractionation indicated that all three G proteins identified in this study (Gi2 and two forms of Go) are localized to islet membranes. No immunoreactivity could be detected in the cytosolic fraction.

Immunoprecipitation of a pertussis toxin substrate of the Go family from rat islets of Langerhans

1992 ◽  
Vol 12 (2) ◽  
pp. 95-100 ◽  
Author(s):  
Nicholas S. Berrow ◽  
Roger D. Hurst ◽  
Susan L. F. Chan ◽  
Noel G. Morgan
Keyword(s):  
Molecular Weight ◽  
Insulin Secretion ◽  
Adenylate Cyclase ◽  
G Protein ◽  
G Proteins ◽  
Islets Of Langerhans ◽  
Pertussis Toxin ◽  
Inhibitory Receptors ◽  
Rat Islets ◽  
Rat Islets Of Langerhans

Rat islets express a pertussis toxin sensitive G-protein involved in receptor-mediated inhibition of insulin secretion. This has been assumed previously to represent “Gi” which couples inhibitory receptors to adenylate cyclase. Incubation of islet G-proteins with32P-NAD and pertussis toxin resulted in the labelling of a band of molecular weight 40,000. This band was very broad and did not allow resolution of individual components. Incubation of the radiolabelled proteins with an anti-Go antiserum resulted in specific immunoprecipitation of a32P-labelled band. These results demonstrate that the complement of pertussis toxin sensitive G-proteins in rat islets includes Go.

Cryogenic preservation of isolated rat islets of Langerhans

Cryobiology ◽  
1976 ◽  
Vol 13 (6) ◽  
pp. 646-647
Author(s):  
Harvey Bank ◽  
Richard Davis ◽  
James Scoggin ◽  
Richard Weiss ◽  
Dorothy Noe
Keyword(s):  
Islets Of Langerhans ◽  
Rat Islets ◽  
Isolated Rat Islets ◽  
Rat Islets Of Langerhans ◽  
Isolated Rat

Kinetics of 65Zinc Uptake and Distribution in Fractions from Cultured Rat Islets of Langerhans

Diabetes ◽  
1980 ◽  
Vol 29 (10) ◽  
pp. 767-773 ◽  
Author(s):  
D. P. Figlewicz ◽  
B. Formby ◽  
A. T. Hodgson ◽  
F. G. Schmid ◽  
G. M. Grodsky
Keyword(s):  
Islets Of Langerhans ◽  
Rat Islets ◽  
Rat Islets Of Langerhans ◽  
Kinetics Of

Calcium distribution in islets of Langerhans: a study of calcium concentrations and of calcium accumulation in B cell organelles

1975 ◽  
Vol 19 (2) ◽  
pp. 395-409
Author(s):  
S.L. Howell ◽  
W. Montague ◽  
M. Tyhurst
Keyword(s):  
Endoplasmic Reticulum ◽  
Cyclic Amp ◽  
B Cell ◽  
Islets Of Langerhans ◽  
Cyclic Gmp ◽  
Cell Organelles ◽  
Calcium Accumulation ◽  
Labile Pool ◽  
Storage Granules ◽  
Rat Islets Of Langerhans

Calcium concentrations of various pancreatic B cell organelles have been determined by X-ray microanalysis of areas of frozen sections of unfixed rat islets of Langerhans. Highest concentrations were detected in storage granules and in mitochondria, although calcium was also present in nuclei, in areas of endoplasmic reticulum and of cytoplasm. Accumulation of 45Ca by isolated organelles has been studied in homogenates and isolated subcellular fractions of rat islets of Langerhans. In the presence of a permeant anion (oxalate or phosphate), accumulation of 45Ca into mitochondria and microsomes was strongly stimulated by ATP. This net uptake was diminished during incubation of homogenates or of a mitochondria plus storage granule-rich fraction in the presence of cyclic AMP, dibutyryl cyclic GMP; 2:4-dinitrophenol or of ruthenium red. Investigations of the characteristics of 45Ca accumulation by homogenates prepared from storage granule-depleted islets showed no differences from those of normal islets, suggesting that the granules do not represent an important labile pool of calcium. With the exception of cyclic AMP and cyclic GMP none of the insulin secretagogues tested (glucose, leucine, arginine, adrenalin, noradrenalin, theophylline, glibenclamide) altered calcium accumulation by islet homogenates. On the basis of absolute calcium levels and of 45Ca uptake studies it is concluded that islet B cells contain a readily exchangeable mitochondrial calcium pool, and an endoplasmic reticulum pool containing a lower concentration of calcium which is also readily exchangeable. The storage granules, despite their high calcium content, do not appear to constitute a labile pool. It seems likely that the labile mitochondria and endoplasmic reticulum pools play a predominant role in the regulation of cytoplasmic free calcium levels, which may in turn be important in the regulation of rates of insulin secretion.

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