32 research outputs found

    Cadherin-7 function in zebrafish development

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    Cadherin cell adhesion molecules play crucial roles in vertebrate development. Most studies have focused on examining the functions of classical type I cadherins (e.g., cadherin-2) in the development of vertebrates. Little information is available concerning the function of classical type II cadherins (e.g., cadherin-7) in vertebrate development. We have previously shown that cadherin-7 mRNA exhibits a dynamic expression pattern in the central nervous system and notochord in embryonic zebrafish. To gain insight into the role of cadherin-7 in the formation of these structures, we analyzed their formation in zebrafish embryos injected with cadherin-7-specific antisense morpholino oligonucleotides (MO). Notochord development was severely disrupted in MO-injected embryos, whereas gross defects in the development of the central nervous system were not detected in MO-injected embryos. Our results thus demonstrate that cadherin-7 plays an important role in the normal development of the zebrafish notochord

    Cold Acclimation Strategy is Highly Variable Among the Sunfishes (Centrarchidae)

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    We tested the hypothesis that the physiological strategy for acclimating to low body temperature is similar among closely related fish. Largemouth bass (Micropterus salmoides), green sunfish (Lepomis cyanellus), bluegill sunfish (Lepomis macrochirus), black crappie (Pomonix nigromaculatus), and white crappie (Pomonix annularis), all members of the family Centrarchidae, were acclimated to 5degrees and 25degreesC. Morphometric variables (total mass, total length, organ masses) and enzyme activities (hexokinase; lactate dehydrogenase; and cytochrome oxidase in heart, liver, and muscle) were measured in 5degreesC- and 25degreesC- acclimated fish at 5degrees and 25degreesC assay temperatures. Each species displayed a distinct physiological response to cold acclimation that differed among tissues. These data suggest that the response to cold acclimation is highly variable within families. Our findings are consistent with other studies suggesting that acclimation responses are labile and may evolve independently even among closely related species

    Leptin in Teleost Fishes: An Argument for Comparative Study

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    All organisms face tradeoffs with regard to how limited energy resources should be invested. When is it most favorable to grow, to reproduce, how much lipid should be allocated to storage in preparation for a period of limited resources (e.g., winter), instead of being used for growth or maturation? These are a few of the high consequence fitness “decisions” that represent the balance between energy acquisition and allocation. Indeed, for animals to make favorable decisions about when to grow, eat, or reproduce, they must integrate signals among the systems responsible for energy acquisition, storage, and demand. We make the argument that leptin signaling is a likely candidate for an integrating system. Great progress has been made understanding the leptin system in mammals, however our understanding in fishes has been hampered by difficulty in cloning fish orthologs of mammalian proteins and (we assert), underutilization of the comparative approach

    Melanocortin/melanocortin receptors

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    The melanocortin receptors (MCRs) are a family of G protein-coupled receptors that are activated by melanocortin ligands derived from the proprotein, proopiomelanocortin (POMC). During the radiation of the gnathostomes, the five receptors have become functionally segregated (i.e. melanocortin 1 receptor (MC1R), pigmentation regulation; MC2R, glucocorticoid synthesis; MC3R and MC4R, energy homeostasis; and MC5R, exocrine gland physiology). A focus of this review is the role that ligand selectivity plays in the hypothalamus/pituitary/adrenal-interrenal (HPA-I) axis of teleosts and tetrapods as a result of the exclusive ligand selectivity of MC2R for the ligand ACTH. A second focal point of this review is the roles that the accessory proteins melanocortin 2 receptor accessory protein 1 (MRAP1) and MRAP2 are playing in, respectively, the HPA-I axis (MC2R) and the regulation of energy homeostasis by neurons in the hypothalamus (MC4R) of teleosts and tetrapods. In addition, observations are presented on trends in the ligand selectivity parameters of cartilaginous fish, teleost, and tetrapod MC1R, MC3R, MC4R, and MC5R paralogs, and the modeling of the HFRW motif of ACTH(1-24) when compared with alpha-MSH. The radiation of the MCRs during the evolution of the gnathostomes provides examples of how the physiology of endocrine and neuronal circuits can be shaped by ligand selectivity, the intersession of reverse agonists (agouti-related peptides (AGRPs)), and interactions with accessory proteins (MRAPs)

    Comparative endocrinology of leptin: Assessing function in a phylogenetic context

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    •Leptin diversity within and among vertebrates is reviewed with a new phylogeny of leptins.•Leptin universally reduces appetite among all vertebrates tested, but does not reflect fat stores in fish.•Leptin is a stress-responsive hormone in multiple contexts and is an important immunomodulator throughout vertebrates.•Several comparative models offer opportunity for studying human disease. As we approach the end of two decades of leptin research, the comparative biology of leptin is just beginning. We now have several leptin orthologs described from nearly every major clade among vertebrates, and are moving beyond gene descriptions to functional studies. Even at this early stage, it is clear that non-mammals display clear functional similarities and differences with their better-studied mammalian counterparts. This review assesses what we know about leptin function in mammals and non-mammals, and gives examples of how these data can inform leptin biology in humans

    Copy number estimations from qPCR background material tests for OB-RGRP and leptin.

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    <p>Graphs represent copy numbers of leptin and OB-RGRP determined using yeast RNA and yeast cDNA as qPCR background material. Note that copy numbers determined from yeast RNA and yeast cDNA plasmid standards show no significant difference. Error bars depict 95% confidence interval.</p
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