Galanin—10 years with a neuroendocrine peptide

Bedecs, Katarina; Berthold, Malin; Bartfai, Tamás

doi:10.1016/1357-2725(95)00008-d

Cited by 122 publications

(86 citation statements)

References 92 publications

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“…Galanin is a 29-amino acid (30 in men) polypeptide which is abundantly expressed in brain as well as in peripheral tissues. The regulation of a variety of physiological processes like stimulation of food intake, nociception, memory, depression, and control of neuroendocrine hypothalamic-pituitary circuits has been correlated with galanin and its receptors (Bartfai et al, 1993;Bedecs et al, 1995;Kask et al, 1995;Wang and Gustafson, 1998). In pituitary GH 3 cells and in the pancreatic b-cell model RINm5F, galanin interferes with hormone release by inhibition of voltage-gated Ca 2+ channels (Kalkbrenner et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

The galanin receptor type 2 initiates multiple signaling pathways in small cell lung cancer cells by coupling to Gq, Gi and G12 proteins

et al. 2000

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Neuropeptides like galanin produced and released by small cell lung cancer (SCLC) cells are considered principal mitogens in these tumors. We identi®ed the galanin receptor type 2 (GALR2) as the only galanin receptor expressed in H69 and H510 cells. Photoa nity labeling of G proteins in H69 cell membranes revealed that GALR2 activates G proteins of three subfamilies: G q , G i , and G 12 . In H69 cells, galanin-induced Ca 2+ mobilization was pertussis toxin-insensitive. While phorbol ester-induced extracellular signal-regulated kinase (ERK) activation required protein kinase C (PKC) activity, preincubation of H69 cells with the PKCinhibitor GF109203X had no e ect on galanin-dependent ERK activity. A rise of the intracellular calcium concentration was necessary and su cient to mediate galanin-induced ERK activation. In support of G i coupling, stimulation of GALR2 expressed in HEK293 cells inhibited isoproterenol-induced cAMP accumulation and raised cAMP levels in COS-7 cells when coexpressed with a chimeric Ga S -Ga i protein. In H69 cells, galanin activated the monomeric GTPase RhoA and induced stress ®ber formation in Swiss 3T3 cells expressing GALR2. Thus, we provide the ®rst direct evidence that in SCLC the mitogenic neuropeptide galanin, interacting with GALR2, simultaneously activates multiple classes of G proteins and signals through the G q phospholipase C/calcium sequence and a G 12 /Rho pathway. Oncogene (2000) 19, 4199 ± 4209.

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Section: Introductionmentioning

confidence: 99%

The galanin receptor type 2 initiates multiple signaling pathways in small cell lung cancer cells by coupling to Gq, Gi and G12 proteins

et al. 2000

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“…The mature Galanin peptide, a well known neurotransmitter, consists of 29 amino acids, which are highly conserved throughout the vertebrates. Initial translation of the murine Gal mRNA results in a 124 amino acid pre-pro-peptide, which is proteolytically cleaved both in the ER and after secretion to give rise to the active 29 amino acid peptide (Bedecs et al, 1995). Gal expression was analyzed by whole-mount in situ hybridization (WMISH) from E7.5 to E13.5 using an antisense probe synthezised from a 450-bp cDNA clone (cf.…”

Section: Left Asymmetric Expression Of Gal In the Linear Heart Tube Pmentioning

confidence: 99%

Left‐asymmetric expression of Galanin in the linear heart tube of the mouse embryo is independent of the nodal co‐receptor gene cryptic

Schweickert

Deißler

Britsch

et al. 2008

Developmental Dynamics

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Only very few left/right asymmetrically expressed genes are known in the mammalian embryo. In a screen for novel factors we identified the gene encoding the neuropeptide Galanin in mouse. At embryonic day (E) 8.5 asymmetric mRNA transcription was found in the left half of the linear heart tube. During heart looping and morphogenesis expression became restricted to the atrio-ventricular (AV) canal, followed by specific staining of the AV-node and AV-rings in the four-chambered heart. Expression was inverted in inv/inv and randomized in homozygous iv mutant embryos. Left-sided heart-specific transcription of mouse Gal thus should be controlled by the left-right pathway. The asymmetric pattern was retained in cryptic mutant embryos, in which the Nodal signaling cascade is disrupted. Surprisingly, Pitx2c was found to be expressed in 50% of cryptic mutant hearts as well, suggesting that some aspects of asymmetric gene expression in the heart are independent of cryptic. Developmental Dynamics 237:3557-3564, 2008.

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“…Galanin is a widely distributed peptide with a broad spectrum of biological effects Bedecs et al, 1995). Galanin was originally isolated from pig intestine in 1983 during a search for C-terminally amidated peptides (Tatemoto et a!., 1983) and in subsequent years has been found in the CNS and the PNS of numerous species.…”

Section: Introductionmentioning

confidence: 99%

Molecular Characterization and Expression of Cloned Human Galanin Receptors GALR2 and GALR3

Kolakowski

O’Neill

Howard

et al. 1998

Journal of Neurochemistry

168

129

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Abstract:Galanin is a 29-or 30-amino acid peptide with wide-ranging effects on hormone release, feeding behavior, smooth muscle contractility, and somatosensory neuronal function. Three distinct galanin receptor (GALR) subtypes, designated GALR1, 2, and 3, have been cloned from the rat. We report here the cloning of the human GALR2 and GALR3 genes, an initial characterization of their pharmacology with respect to radioligand binding and signal transduction pathways, and a profile of their expression in brain and peripheral tissues. Human GALR2 and GALR3 show, respectively, 92 and 89% amino acid sequence identity with their rat homologues. Radioligand binding studies with 125l-galanin show that recombinant human GALR2 binds with high affinity to human galanin (K 0 = 0.3 nM). Human GALR3 binds galanin with less affinity (IC50 of 12 nM for porcine galanin and 75 nM for human galanin). Human GALR2 was shown to couple to phospholipase C and elevation of intracellular calcium levels as assessed by aequorin luminescence in HEK-293 cells and by Xenopus melanophore pigment aggregation and dispersion assays, in contrast to human GALR1 and human GALR3, which signal predominantly through inhibition of adenylate cyclase. GALR2 mRNA shows a wide distribution in the brain (mammillary nuclei, dentate gyrus, cingulate gyrus, and posterior hypothalamic, supraoptic, and arcuate nuclei), and restricted peripheral tissue distritution with highest mRNA levels detected in human small intestine. In comparison, whereas GALR3 mRNA was expressed in many areas of the rat brain, there was abundant expression in the primary 01-factory cortex, olfactory tubercie, the islands of Calleja, the hippocampal CA regions of Ammon's horn, and the dentate gyrus. GALR3 mRNA was highly expressed in human testis and was detectable in adrenal gland and pancreas. The genes for human GALR2 and 3 were localized to chromosomes 17q25 and 22q12.2-13.1, respectively. Key Words: Galanin receptor-G protein-coupled receptor-Cloning.

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Galanin—10 years with a neuroendocrine peptide

Cited by 122 publications

References 92 publications

The galanin receptor type 2 initiates multiple signaling pathways in small cell lung cancer cells by coupling to Gq, Gi and G12 proteins

The galanin receptor type 2 initiates multiple signaling pathways in small cell lung cancer cells by coupling to Gq, Gi and G12 proteins

Left‐asymmetric expression of Galanin in the linear heart tube of the mouse embryo is independent of the nodal co‐receptor gene cryptic

Molecular Characterization and Expression of Cloned Human Galanin Receptors GALR2 and GALR3

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