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Inhibition of glucose stimulated insulin secretion by neuropeptide Y is mediated via the Y1 receptor and inhibition of adenylyl cyclase in RIN 5AH rat insulinoma cells (1998)

Morgan, D. G. ; Kulkarni, R. N. ; Hurley, J. D. ; [et al.]

Springer

Diabetologia 41 (1998), S. 1482-1491

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ISSN: 1432-0428

Keywords: Keywords Neuropeptide Y ; Y1 receptor ; insulin secretion ; insulinoma cells.

Source: Springer Online Journal Archives 1860-2000

Topics: Medicine

Notes: Summary Neuropeptide Y (NPY) has been shown to inhibit insulin secretion from the islets of Langerhans. We show that insulin secretion in the insulinoma cell line RIN 5AH is inhibited by NPY. 125I-Peptide YY (PYY) saturation and competition-binding studies using NPY fragments and analogues on membranes prepared from this cell line show the presence of a single class of NPY receptor with a Y1 receptor subtype-like profile. Inhibition of insulin secretion in this cell line by NPY fragments and analogues also shows a Y1 receptor-like profile. Both receptor binding and inhibition of insulin secretion showed the same orders of potency with NPY 〉 [Pro34]-NPY 〉 NPY 3–36 〉 〉 NPY 13–36. The Y1 receptor antagonist, BIBP 3226, blocks NPY inhibition of insulin secretion from, and inhibits 125I-PYY binding to, RIN 5AH cells. Northern blot analysis using a Y1-receptor specific probe shows that NPY Y1 receptors are expressed by RIN 5AH cells. Y5 receptors are not expressed in this cell line. Neuropeptide Y inhibition of insulin secretion is blocked by incubation with pertussis toxin, implying that the effect is via a G-protein (Gi or Go) coupled receptor. Neuropeptide Y inhibits the activation of adenylyl cyclase by isoprenaline in RIN 5AH cell lysates, and the stimulation of cAMP by glucagon-like peptide-1 (7–36) amide (GLP-1). It also blocks insulin secretion stimulated by GLP-1, but not by dibutyryl cyclic AMP. Hence, we suggest that NPY inhibits insulin secretion from RIN 5AH cells via a Y1 receptor linked through Gi to the inhibition of adenylyl cyclase. [Diabetologia (1998) 41: 1482–1491]

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/s001250051095

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Reflection high resolution analytical electron microscopy: A technique for studying crystal surfaces (1988)

Wang, Z. L.

New York, NY : Wiley-Blackwell

Journal of Electron Microscopy Technique 10 (1988), S. 35-43

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ISSN: 0741-0581

Keywords: REM ; RHEED ; TRHEED ; REELS ; EDX ; RHEED theory ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Natural Sciences in General

Notes: Reflection electron microscopy (REM), reflection high energy electron diffraction (RHEED), reflection electron energy-loss spectroscopy (REELS), and energy dispersion x-ray spectroscopy (EDX) have been comprehensively used as a technique, termed reflection high resolution analytical electron microscopy (RHRAEM), for studying the structures of the bulk crystal GaAs (110) surfaces by transmission electron microscopy (TEM). The simultaneous observations of surface topography imaging, the surface diffraction mechanism with RHEED, surface atomic inner-shell excitations with REELS, and surface chemical compositions with EDX provide a systematic description of the atomic structure and chemical structure of the surface. The surface channelling effect has been observed in GaAs (110) with REELS, which may provide a basis for localizing surface foreign atoms with ALCHEMI. The theoretically predicted surface-resonance wave has been observed directly in the RHEED pattern; the surface-captured Bragg reflection wave have been identified. It is shown that surface chemical compositions can be determined by analyzing the EDX spectra obtained in the REM case. Finally, the surface monolayer resonance characteristic of the RHRAEM has been confirmed by calculations with dynamical RHEED theory.

Additional Material: 9 Ill.