Genomic organization and localization of the gene encoding human preprogalanin

Evans, Helen F.; Baumgartner, Martina; Shine, John; Herzog, Herbert

doi:10.1016/s0888-7543(11)80002-9

Cited by 47 publications

(29 citation statements)

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“…It is a product of post-translational process of 121AA long prepro-galanin and consists of 30 amino acids in humans (Evans et al 1993). The N-terminal part of galanin, which includes residues 1-14, is highly conserved between species and is therefore considered to play a crucial role in its biological activity and receptor interaction (Branchek et al 2000).…”

Section: Introductionmentioning

confidence: 99%

Ligand binding properties of human galanin receptors

Jurkowski

Elofsson

2012

Molecular Membrane Biology

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This is an accepted version of a paper published in Molecular membrane biology. This paper has been peer-reviewed but does not include the final publisher proof-corrections or journal pagination.Citation for the published paper: Jurkowski, W., Yazdi, S., Elofsson, A. (2013) AbstractThe galanin receptor family comprises of three members, GalR1, GalR2 and GalR3, all belonging to the G-protein-couple receptor superfamily. All three receptors bind the peptide hormone galanin, but show distinctly di erent binding properties to other molecules and e ects on intracellular signaling. To gain insight on the molecular basis of receptor subtype speci ficity, we have generated a three-dimensional model for each of the galanin receptors based on its homologs in the same family. We found significant di erences in the organization of the binding pockets among the three types of receptors, which might be the key for specific molecular recognition o igands. Through docking o ragments of the galanin peptide and a number o igands, we investigated the involvement of transmembrane and loop residues in ligand interaction.

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Section: Introductionmentioning

confidence: 99%

Ligand binding properties of human galanin receptors

Jurkowski

Elofsson

2012

Molecular Membrane Biology

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“…The PCR product was run using 1.5% (wt/vol) agarose gel electrophoresis with 40 mM Tris-acetate buffer (pH 8.0) containing 1 mM EDTA and visualized with the use of ethidium bromide (0.5 g/ml). Gene-specific oligonucleotide primers for amplification of turtle galanin cDNAs were designed on the basis of the conserved regions of human (5,14), chicken (27), quail (27), rat (25), and mouse (26) galanin. Accordingly, the forward and reverse primers for the 3Ј-RACE system were 5Ј-CCACATGCAGTA-GAGATAACCAC-3Ј and 5Ј-CTAATACGACTCACTATAGGGC-AAGCAGTGGTATCAACGCAGAGT-3Ј (the so-called universal primer mix A by SMART RACE kit), respectively.…”

Section: Methodsmentioning

confidence: 99%

“…Although its mechanism of action in these reptilian physiological processes remains unknown, galanin in mammals reportedly operates via G i /G 0 -proteincoupled receptors involving effector systems such as K ϩ channels, Ca 2ϩ channels, and adenylate cyclase (3). In mice and humans, the galanin gene contains six exons and five introns (14,26), and its mRNA consists of 398 -989 base pairs (bp), depending on the species (5, 8, 13, 14, 25-27, 35, 41, 42, 50). The open-reading frame encodes a mouse (124 aa) (26) and human (125 aa) (5,14) preprogalanin protein.…”

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confidence: 99%

“…In mice and humans, the galanin gene contains six exons and five introns (14,26), and its mRNA consists of 398 -989 base pairs (bp), depending on the species (5, 8, 13, 14, 25-27, 35, 41, 42, 50). The open-reading frame encodes a mouse (124 aa) (26) and human (125 aa) (5,14) preprogalanin protein. In vertebrates, mature galanin derived from the preprogalanin COOH terminus contains 29 aa and amidates with glycine at the final residue (threonine or alanine) (2, 5, 8, 13, 14, 18, 25-27, 35, 41, 42, 50, 52, 56 -59).…”

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confidence: 99%

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A preprogalanin cDNA from the turtle pituitary and regulation of its gene expression

Yu¹,

Pon²,

Ku³

et al. 2007

American Journal of Physiology-Regulatory, Integrative and Comp

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Galanin is a hormone 29 or 30 amino acids (aa) long that is widely distributed within the body and exerts numerous biological effects in vertebrates. To fully understand its physiological roles in reptiles, we analyzed preprogalanin cDNA structure and expression in the turtle pituitary. Using the Chinese soft-shell turtle (Pelodiscus sinensis order Testudines), we obtained a 672-base pair (bp) cDNA containing a 99-bp 5Ј-untranslated region, a 324-bp preprogalanin coding region, and a 249-bp 3Ј-untranslated region. The open-reading frame encoded a 108-aa preprogalanin protein with a putative 23-aa signal sequence at the NH 2 terminus. Based on the location of putative Lys-Arg dibasic cleavage sites and an amidation signal of Gly-Lys-Arg, we propose that turtle preprogalanin is processed to yield a 29-aa galanin peptide with Gly 1 and Thr 29 substitutions and a COOH-terminal amidation. Sequence comparison revealed that turtle preprogalanin and galanin-29 had 48 -81% and 76 -96% aa identities with those of other vertebrates, respectively, suggesting their conservative nature. Expression of the turtle galanin gene was detected in the pituitary, brain, hypothalamus, stomach, liver, pancreas, testes, ovaries, and intestines, but not in the adipose or muscle tissues, suggesting tissue-dependent differences. An in vitro study that used pituitary tissue culture indicated that treatment with 17␤-estradiol, testosterone, or gonadotropin-releasing hormone resulted in increased galanin mRNA expression with dose-or time-dependent differences, whereas leptin and neuropeptide Y reduced galanin mRNA levels. These results suggest a hormone-dependent effect on hypophyseal galanin mRNA expression.estrogen; androgen; gonadotropin-releasing hormone; neuropeptide Y; leptin GALANIN, a 29-amino acid (aa) hormone, was first isolated from porcine intestine and used to stimulate contractions of rat smooth muscle and to cause hyperglycemia in dogs (52). Since its discovery, galanin has also been found to exhibit numerous actions in vertebrates. For example, it induces feeding and the release of pituitary hormones [i.e., luteinizing hormone (LH) and growth hormone (GH)], decreases circulating levels of oxytocin, plays an antinociceptive role in the spinal cord, is involved in gastrointestinal motility and autonomic function, inhibits memory and learning, and promotes smooth muscle contractions (12). Moreover, clinical investigations have shown that galanin levels and galanin receptors are related to human disorders, such as Alzheimer disease and obesity (12). In reptiles, galanin can control gastrointestinal blood flow (24) and female oviposition (29). Although its mechanism of action in these reptilian physiological processes remains unknown, galanin in mammals reportedly operates via G i /G 0 -proteincoupled receptors involving effector systems such as K ϩ channels, Ca 2ϩ channels, and adenylate cyclase (3). In mice and humans, the galanin gene contains six exons and five introns (14, 26), and its mRNA consists of 398 -989 base pairs (bp),...

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“…They named the new molecule GALP because of its shared partial sequence identity with galanin and its binding in vitro to two of the known galanin receptors [26]. Despite the partially shared sequence, GALP and galanin are encoded by different genes [27,28]. Fulllength GALP is cleaved from a larger precursor and comprises 60 amino acids.…”

Section: Galp and Its Binding To Galanin Receptorsmentioning

confidence: 99%

Galanin-like peptide as a link in the integration of metabolism and reproduction

Gottsch

Clifton

Steiner

2004

Trends in Endocrinology & Metabolism

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The arcuate nucleus is a hypothalamic center that couples energetics and reproduction. Peptide-releasing neurons in the arcuate nucleus receive and process humoral signals from the periphery and relay this information to other nuclei in the hypothalamus and preoptic area. Galanin-like peptide (GALP) is expressed in the arcuate nucleus, and GALP-containing neurons are targets for the action of leptin. GALP-containing neurons are closely apposed to gonadotropin-releasing hormone (GnRH) neurons in the preoptic area, and CNS injections of GALP stimulate GnRH-mediated secretion of luteinizing hormone. These observations indicate that GALP is a molecular signal that couples circulating indices of metabolism to the neuroendocrine reproductive system and, thus, regulates reproductive activity as a function of the energy state. In this article, we describe the involvement of GALP in metabolism and reproduction, and in the coupling between these two processes.The brain has a remarkable ability to sense the status of metabolic fuel reserves and defend their adequacy by adjusting appetite and metabolism to maintain an appropriate body weight. Moreover, the brain governs the activity of the reproductive system as a function of these metabolic reserves and enables activation of the hypothalamic -pituitary -gonadal axis only when fuel stores are deemed adequate to support the energetic requirements of reproduction. The arcuate nucleus (Arc) in the hypothalamus is a node for this physiological integration. Recently, a newly identified peptide in the Arc has been shown to modulate both feeding behavior and reproduction, which unveils a new link in the integration of metabolism and reproduction. In this review, we discuss the emerging role of this peptide, known as galanin-like peptide (GALP), in the physiological integration of metabolism and reproduction. The Arc integrates metabolism and reproductionThe Arc comprises the neuronal circuitry required for the neuroendocrine integration of metabolism and reproduction [1]. Two populations of neurons in the Arc play key roles in the regulation of these physiological processes. One population produces neuropeptide Y (NPY) and agouti-related peptide (AgRP), whereas the other produces a-melanocyte-stimulating hormone (a-MSH) and b-endorphin from a common precursor, proopiomelanocortin (POMC), and cocaine-and amphetamine-regulated transcript (CART). These two cell groups (NPY/AgRP and POMC/CART) are regulated differentially by metabolic hormones such as leptin and insulin, and act in opposition to control appetite, body weight and metabolic rate [1][2][3][4]. NPY/AgRP and POMC/CART neurons send axonal projections to the paraventricular nucleus (PVN), lateral hypothalamus, and areas in the midbrain and hindbrain to regulate the circuitry that controls complex behaviors, such as feeding, and adjust the metabolic rate to maintain body weight homeostasis [3,[5][6][7]. Disruption of these networks leads to the dysregulation of body weight and disturbances in metabolism [8]. The Arc is also a...

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Genomic organization and localization of the gene encoding human preprogalanin

Cited by 47 publications

References 12 publications

Ligand binding properties of human galanin receptors

Ligand binding properties of human galanin receptors

A preprogalanin cDNA from the turtle pituitary and regulation of its gene expression

Galanin-like peptide as a link in the integration of metabolism and reproduction

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