Characterization of Galanin Receptors in the Insulin- Secreting Cell Line Rin m 5F: Evidence for Coupling with a Pertussis Toxin-Sensitive Guanosine Triphosphate Regulatory Protein*

Endocrinology ◽  
1989 ◽  
Vol 124 (5) ◽  
pp. 2635-2641 ◽  
Author(s):  
I. LAGNY-POURMIR ◽  
B AMIRANOFF ◽  
A. M. LORINET ◽  
K. TATEMOTO ◽  
M. LABURTHE
Keyword(s):  
Cell Line ◽  
Pertussis Toxin ◽  
Regulatory Protein ◽  
Guanosine Triphosphate ◽  
Secreting Cell ◽  
Galanin Receptors

Characterization of a Novel Glucose-Responsive Insulin-Secreting Cell Line, BRIN-BD11, Produced by Electrofusion

Diabetes ◽  
1996 ◽  
Vol 45 (8) ◽  
pp. 1132-1140 ◽  
Author(s):  
N. H. McClenaghan ◽  
C. R. Barnett ◽  
E. Ah-Sing ◽  
Y. H. A. Abdel-Wahab ◽  
F. P. M. O'Harte ◽  
...  
Keyword(s):  
Cell Line ◽  
Secreting Cell

Morphological and functional characterization of beta TC-6 cells--an insulin-secreting cell line derived from transgenic mice

Diabetes ◽  
1995 ◽  
Vol 44 (3) ◽  
pp. 306-313 ◽  
Author(s):  
V. Poitout ◽  
L. E. Stout ◽  
M. B. Armstrong ◽  
T. F. Walseth ◽  
R. L. Sorenson ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Cell Line ◽  
Functional Characterization ◽  
Secreting Cell

scholarly journals Functional Expression and Characterization of a Voltage-Gated CaV1.3 (α1D) Calcium Channel Subunit from an Insulin-Secreting Cell Line

2001 ◽  
Vol 15 (7) ◽  
pp. 1211-1221 ◽  
Author(s):  
Alexandra Scholze ◽  
Tim D. Plant ◽  
Annette C. Dolphin ◽  
Bernd Nürnberg
Keyword(s):  
Calcium Channel ◽  
Cell Line ◽  
Functional Expression ◽  
Secreting Cell ◽  
Voltage Gated

Characterization of binding sites for oxyntomodulin on a somatostatin-secreting cell line (RIN T3).

Endocrinology ◽  
1992 ◽  
Vol 130 (3) ◽  
pp. 1263-1270
Author(s):  
L Gros ◽  
E Demirpence ◽  
C Jarrousse ◽  
A Kervran ◽  
D Bataille
Keyword(s):  
Cell Line ◽  
Binding Sites ◽  
Secreting Cell

Morphological and Functional Characterization of  TC-6 Cells--an Insulin-Secreting Cell Line Derived From Transgenic Mice

Diabetes ◽  
1995 ◽  
Vol 44 (3) ◽  
pp. 306-313 ◽  
Author(s):  
V. Poitout ◽  
L. E. Stout ◽  
M. B. Armstrong ◽  
T. F. Walseth ◽  
R. L. Sorenson ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Cell Line ◽  
Functional Characterization ◽  
Secreting Cell

Immunochemical and electrophoretic characterization of the major pertussis toxin substrate of the RAW264 macrophage cell line

Biochemistry ◽  
1988 ◽  
Vol 27 (6) ◽  
pp. 2040-2046 ◽  
Author(s):  
Peter S. Backlund ◽  
Robert R. Aksamit ◽  
Cecilia G. Unson ◽  
Paul Goldsmith ◽  
Allen M. Spiegel ◽  
...  
Keyword(s):  
Cell Line ◽  
Pertussis Toxin ◽  
Macrophage Cell Line ◽  
Macrophage Cell

scholarly journals Characterization of a complement-fragment-C5a-stimulated calcium-influx mechanism in U937 monocytic cells

1993 ◽  
Vol 295 (3) ◽  
pp. 679-684 ◽  
Author(s):  
P N Monk ◽  
L J Partridge
Keyword(s):  
Cell Line ◽  
Pertussis Toxin ◽  
Inositol Phosphates ◽  
Calcium Influx ◽  
Cell Types ◽  
U937 Cells ◽  
Monocytic Cell ◽  
Monocytic Cell Line ◽  
Monocytic Cells

The mechanism by which complement fragment C5a elevates intracellular Ca2+ ([Ca2+]i) levels in two cell types, a monocytic cell line, U937, and neutrophils, has been investigated by the use of fluorometric and radiometric techniques. In U937 cells the influx of extracellular Ca2+ can be distinguished from the release of intracellular Ca2+ stores in terms of dose-responsiveness to C5a and sensitivity to pertussis-toxin poisoning. This suggests that the mechanism of Ca2+ influx in these cells is at least partially independent of both the production of inositol phosphates and elevation of internal Ca2+ concentration. The C5a-stimulated influx of 45Ca2+ into U937 cells is inhibited by a series of metal ions (Zn2+ > Co2+ > Mn2+ > Sr2+ approximately equal to Ni2+ > La3+). The stimulated influx of Ca2+ into neutrophils is inhibited differently (Ni2 >> Co2+ > Zn2+ approximately equal to La3+ > Mn2+ approximately equal to Sr2+), is less sensitive to C5a and both the influx of extracellular Ca2+ and the release of intracellular stores are equally sensitive to pertussis toxin treatment. Taken together these results indicate that [Ca2+]i is controlled in U937 monocytes by mechanisms distinct from those which appear to operate in other myeloid cells, such as neutrophils, stimulated with C5a and formylpeptide.

Characterization of α2-adrenoceptors in a plasma membrane enriched fraction from the insulin-secreting cell line RINm5F

1989 ◽  
Vol 121 (4) ◽  
pp. 525-532 ◽  
Author(s):  
Susanne Ullrich ◽  
Claes B. Wollheim
Keyword(s):  
Plasma Membrane ◽  
Cell Line ◽  
Membrane Fraction ◽  
Specific Activity ◽  
Secretory Granules ◽  
Rinm5f Cells ◽  
Secreting Cell ◽  
High Affinity Binding Site ◽  
Receptor Number

Abstract. A plasma membrane enriched fraction from the insulin-secreting cell line RINm5F was used to characterize [3H]clonidine binding. After a single self-generating Percoll gradient, the specific activity of 5'-nucleotidase (a plasma membrane marker) of the membrane fraction was enriched about 8-fold over that of the homogenate and nearly 30% of the total amount was recovered. The fraction was essentially free of mitochondria and secretory granules. [3H]clonidine binding to this membrane fraction revealed a single, high affinity binding site with a Kd of 2.3 nmol/l. The binding was competitively inhibited by adrenergic agonists in the following order of potency: clonidine > epinephrine > phenylephrine > isoproterenol, and by antagonists in the order of potency: idazoxan > yohimbine > propranolol > prazosin. Pertussis toxin pretreatment of the cells did not alter the inhibition of [3H]clonidine binding by epinephrine and clonidine nor the estimated receptor number for [3H]clonidine. In conclusion, the pharmacologic characteristics of [3H]clonidine binding sites on a plasma membrane enriched fraction from insulin-secreting RINm5F cells demonstrate that the receptor is of the α2-adrenergic subtype.

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