Alarin but not its alternative-splicing form, GALP (Galanin-like peptide) has antimicrobial activity

Wada, Akihiro; Wong, Pooi-Fong; Hojo, Hironobu; Hasegawa, Makoto; Ichinose, Akitoyo; Llanes, Rafael; Kubo, Yasuo; Senba, Masachika; Ichinose, Yuki

doi:10.1016/j.bbrc.2013.03.045

Cited by 18 publications

(23 citation statements)

References 28 publications

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“…The discovery that alarin, another member of the galanin family of peptides (see section II), has antimicrobial activity against Escherichia coli (Wada et al, 2013) is also consistent with the idea that the galanin peptide family has important functions and therapeutic potential in the regulation of cutaneous innate immune responses.…”

Section: B Skinsupporting

confidence: 63%

“…Two other members of the galanin family of peptides, GMAP and alarin, have been identified as components of the innate immune system with different spectra and mechanisms of antimicrobial activity. GMAP inhibits the growth of the major human fungal pathogen C. albicans and other Candida species Holub et al, 2011) and interferes with hyphal development, whereas alarin is only effective against the Gramnegative bacteria E. coli, inducing bacterial membrane blebbing (Wada et al, 2013; see section IX.B).…”

Section: Galanin Family Peptides and Receptorsmentioning

confidence: 99%

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Physiology, Signaling, and Pharmacology of Galanin Peptides and Receptors: Three Decades of Emerging Diversity

et al. 2014

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Section: B Skinsupporting

confidence: 63%

Section: Galanin Family Peptides and Receptorsmentioning

confidence: 99%

Physiology, Signaling, and Pharmacology of Galanin Peptides and Receptors: Three Decades of Emerging Diversity

et al. 2014

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“…(Santic et al 2007, Van Der Kolk et al 2010. Alarin shares the same first five amino acids as GALP in the N-terminal end, encoding a splice variant of the Galp gene in exclusion of exon 3, but the following 20 amino acids show no sequence identity to galanin or GALP (Santic et al 2006, Wada et al 2013. Sequence identity of this peptide between macaque and human is 96%, and that between rat and murine is 88% (Santic et al 2006, Fraley et al 2013.…”

Section: Introductionmentioning

confidence: 85%

Central alarin ameliorated insulin resistance of adipocytes in type 2 diabetic rats

Guo¹,

Fang²,

Yu³

et al. 2014

Journal of Endocrinology

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Alarin, a regulatory peptide, belongs to the galanin family and plays the same regulatory roles as galanin in orexigenic activity and energy metabolism. Our previous studies had found that galanin might facilitate insulin sensitivity via activation of its central receptors. To date, little is known about whether central alarin may exert similar effects on insulin sensitivity. In order to investigate this, alarin and its specific antagonist, alarin 6-25Cys, were administered into the cerebral ventricles of type 2 diabetic rats (T2DR) to evaluate the changes in insulin resistance. The results indicated that central treatment with alarin significantly increased the body weight of animals, the 2-(N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino)-2-deoxyglucose uptake, the plasma adiponectin levels, the glucose infusion rates in hyperinsulinemic-euglycemic clamp tests, the vesicle-associated membrane protein 2 as well as glucose transporter 4 (GLUT4 (SLC2A4)) protein and mRNA levels, and the ratios of GLUT4 contents in plasma membranes to total cell membranes in adipocytes, but reduced blood glucose and plasma retinol-binding protein 4 levels. These effects of alarin may be inhibited by pretreatment with alarin 6-25Cys. The above-mentioned results suggest that the central alarin projective system may facilitate insulin sensitivity and glucose uptake via the increase in GLUT4 content and GLUT4 translocation from intracellular pools to plasma membranes in T2DR.

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“…These findings extended host defense peptides to the nervous system [123]. Since then, more antimicrobial neuropeptides have been documented [45,124]. Some of these neuropeptides may become leads for developing new antibiotics.…”

Section: Identification Of Human Antimicrobial Peptidesmentioning

confidence: 99%

Human Antimicrobial Peptides and Proteins

2014

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As the key components of innate immunity, human host defense antimicrobial peptides and proteins (AMPs) play a critical role in warding off invading microbial pathogens. In addition, AMPs can possess other biological functions such as apoptosis, wound healing, and immune modulation. This article provides an overview on the identification, activity, 3D structure, and mechanism of action of human AMPs selected from the antimicrobial peptide database. Over 100 such peptides have been identified from a variety of tissues and epithelial surfaces, including skin, eyes, ears, mouths, gut, immune, nervous and urinary systems. These peptides vary from 10 to 150 amino acids with a net charge between −3 and +20 and a hydrophobic content below 60%. The sequence diversity enables human AMPs to adopt various 3D structures and to attack pathogens by different mechanisms. While α-defensin HD-6 can self-assemble on the bacterial surface into nanonets to entangle bacteria, both HNP-1 and β-defensin hBD-3 are able to block cell wall biosynthesis by binding to lipid II. Lysozyme is well-characterized to cleave bacterial cell wall polysaccharides but can also kill bacteria by a non-catalytic mechanism. The two hydrophobic domains in the long amphipathic α-helix of human cathelicidin LL-37 lays the basis for binding and disrupting the curved anionic bacterial membrane surfaces by forming pores or via the carpet model. Furthermore, dermcidin may serve as ion channel by forming a long helix-bundle structure. In addition, the C-type lectin RegIIIα can initially recognize bacterial peptidoglycans followed by pore formation in the membrane. Finally, histatin 5 and GAPDH(2-32) can enter microbial cells to exert their effects. It appears that granulysin enters cells and kills intracellular pathogens with the aid of pore-forming perforin. This arsenal of human defense proteins not only keeps us healthy but also inspires the development of a new generation of personalized medicine to combat drug-resistant superbugs, fungi, viruses, parasites, or cancer. Alternatively, multiple factors (e.g., albumin, arginine, butyrate, calcium, cyclic AMP, isoleucine, short-chain fatty acids, UV B light, vitamin D, and zinc) are able to induce the expression of antimicrobial peptides, opening new avenues to the development of anti-infectious drugs.

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Alarin but not its alternative-splicing form, GALP (Galanin-like peptide) has antimicrobial activity

Cited by 18 publications

References 28 publications

Physiology, Signaling, and Pharmacology of Galanin Peptides and Receptors: Three Decades of Emerging Diversity

Physiology, Signaling, and Pharmacology of Galanin Peptides and Receptors: Three Decades of Emerging Diversity

Central alarin ameliorated insulin resistance of adipocytes in type 2 diabetic rats

Human Antimicrobial Peptides and Proteins

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