Family Peptide (family + peptide)

Distribution by Scientific Domains

Selected Abstracts

An ecdysteroid-inducible insulin-like growth factor-like peptide regulates adult development of the silkmoth Bombyx mori

FEBS JOURNAL, Issue 5 2009
Naoki Okamoto
Insulin-like growth factors (IGFs) play essential roles in fetal and postnatal growth and development of mammals. They are secreted by a wide variety of tissues, with the liver being the major source of circulating IGFs, and regulate cell growth, differentiation and survival. IGFs share some biological activities with insulin but are secreted in distinct physiological and developmental contexts, having specific functions. Although recent analyses of invertebrate genomes have revealed the presence of multiple insulin family peptide genes in each genome, little is known about functional diversification of the gene products. Here we show that a novel insulin family peptide of the silkmoth Bombyx mori, which was purified and sequenced from the hemolymph, is more like IGFs than like insulin, in contrast to bombyxins, which are previously identified insulin-like peptides in B. mori. Expression analysis reveals that this IGF-like peptide is predominantly produced by the fat body, a functional equivalent of the vertebrate liver and adipocytes, and is massively released during pupa,adult development. Studies using in vitro tissue culture systems show that secretion of the peptide is stimulated by ecdysteroid and that the secreted peptide promotes the growth of adult-specific tissues. These observations suggest that this peptide is a Bombyx counterpart of vertebrate IGFs and that functionally IGF-like peptides may be more ubiquitous in the animal kingdom than previously thought. Our results also suggest that the known effects of ecdysteroid on insect adult development may be in part mediated by IGF-like peptides. [source]

Mutations in the Insulin-Like Factor 3 Receptor Are Associated With Osteoporosis,

Alberto Ferlin
Abstract Introduction: Insulin-like factor 3 (INSL3) is produced primarily by testicular Leydig cells. It acts by binding to its specific G protein,coupled receptor RXFP2 (relaxin family peptide 2) and is involved in testicular descent during fetal development. The physiological role of INSL3 in adults is not known, although substantial INSL3 circulating levels are present. The aim of this study was to verify whether reduced INSL3 activity could cause or contribute to some signs of hypogonadism, such as reduced BMD, currently attributed to testosterone deficiency. Materials and Methods: Extensive clinical, biochemical, and hormonal study, including bone densitometry by DXA, was performed on 25 young men (age, 27,41 yr) with the well-characterized T222P mutation in the RXFP2 gene. Expression analysis of INSL3 and RXFP2 on human bone biopsy and human and mouse osteoblast cell cultures was performed by RT-PCR, quantitative RT-PCR, and immunohistochemistry. Real-time cAMP imaging analysis and proliferation assay under the stimulus of INSL3 was performed on these cells. Lumbar spine and femoral bone of Rxfp2- deficient mice were studied by static and dynamic histomorphometry and ,CT, respectively. Results: Sixteen of 25 (64%) young men with RXFP2 mutations had significantly reduced BMD. No other apparent cause of osteoporosis was evident in these subjects, whose testosterone levels and gonadal function were normal. Expression analyses showed the presence of RXFP2 in human and mouse osteoblasts. Stimulation of these cells with INSL3 produced a dose- and time-dependent increase in cAMP and cell proliferation, confirming the functionality of the RXFP2/INSL3 receptor,ligand complex. Consistent with the human phenotype, bone histomorphometric and ,CT analyses of Rxfp2,/, mice showed decreased bone mass, mineralizing surface, bone formation, and osteoclast surface compared with wildtype littermates. Conclusions: This study suggests for the first time a role for INSL3/RXFP2 signaling in bone metabolism and links RXFP2 gene mutations with human osteoporosis. [source]

Expression of the PACAP-immunoreactivity in the Lymphoid Organs of the Duck

C. Squillacioti
Introduction:, The interactions occurring between nervous and immune systems are well documented. These interactions involve several types of chemical messengers including hormones, cytokines, classic neurotransmitters and neuropeptides. It has been observed that the lymphoid organs receive a dense peptidergic innervation and immune cells produce neuropeptides. Neuropeptides, in turn, are involved in the regulation of the inflammatory processes and in the maturation of the lymphoid organs. Several studies have demonstrated that the immunomodulatory neuropeptides and their receptors are expressed in the thymus and bursa of fabricius. PACAP is a glucagon/VIP/secretin family peptide. It was originally isolated from the ovine hypothalamus and then it was found in the autonomic nervous system. PACAP is involved in the regulation of the hypothalamic-pituitary function, neurotransmission and neuromodulation. In the immune system, PACAP is expressed in lymphoid tissues of the rat and in the lymphocytes of the duck GALT. PACAP, therefore, could be a messenger of the dialogue between nervous and immune system. It may have a role in the regulation of the inflammatory processes by stimulating histamine and serotonin and modulating the production of the cytokines in immune cells. Methods:, Immunohistochemistry on paraffin-embedded sections of thymus and bursa of fabricius of the duck of different ages by using an antibody anti-PACAP38. Results and Discussion:, In the thymus, PACAP-immunoreactivity was found in lymphoid cells and, with a lesser extent, in epithelial reticular cells. The immunoreactive lymphocytes were primarily observed in the interlobular septa in close vicinity to the interlobular veins. The number of positive lymphocytes increased with ageing. In the bursa of fabricius, PACAP-IR was found in nerve fibres and in a few lymphoid cells. These results suggest that PACAP could play a role in the maturation and involution of these organs and in the immune functions. [source]

Molecular diversity of PBAN family peptides from fire ants,

Man-Yeon Choi
Abstract The PBAN/Pyrokinin peptide family is a major neuropeptide family characterized with a common FXPRLamide in the C-termini. These peptides are ubiquitously distributed in the Insecta and are involved in many essential endocrinal functions, e.g., pheromone production. Previous work demonstrated the localization of PBAN in the fire ant central nervous system, and identified a new family of PBAN from the red imported fire ant, Solenopsis invicta. In this study, we identified five more PBAN/Pyrokinin genes from S. geminata, S. richteri, S. pergandii, S. carolinensis, and a hybrid of S. invicta and S. richteri. The gene sequences were used to determine the phylogenetic relationships of these species and hybrid, which compared well to the morphologically defined fire ant subgroup complexes. The putative PBAN and other peptides were determined from the amino acid sequences of the PBAN/pyrokinin genes. We summarized all known insect PBAN family neuropeptides, and for the first time constructed a phylogenetic tree based on the full amino acid sequences translated from representative PBAN cDNAs. The PBAN/pyrokinin gene is well conserved in Insecta and probably extends into the Arthropod phylum; however, translated pre-propeptides may vary and functional diversity may be retained, lost, or modified during the evolutionary process. Published 2010 Wiley Periodicals, Inc. [source]