Circulating serotonin in vertebrates

Maurer‐Spurej, Elisabeth

doi:10.1007/s00018-005-5149-5

Cited by 35 publications

(19 citation statements)

References 65 publications

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“…Interestingly, it has been recently found that 5-HT is associated with thrombocytes of birds and endothermic reptilian species but not with thrombocytes of coldblooded vertebrates (39). Phylogenetic comparison of the presence of circulating 5-HT indicated an evolutionary divergence within reptilian species that might coincide with the emergence of endothermy ϳ320 million years ago (39). It is also interesting in this context that the integument, or specialized regions of the integument, is a major thermoregulatory organ in many vertebrates, both mammalian and nonmammalian.…”

Section: Resultsmentioning

confidence: 99%

“…If we assume that the primeval function of D7 proteins was to bind serotonin, it is pertinent to ask whether vertebrates at that time had this amine in their thrombocytes. Interestingly, it has been recently found that 5-HT is associated with thrombocytes of birds and endothermic reptilian species but not with thrombocytes of coldblooded vertebrates (39). Phylogenetic comparison of the presence of circulating 5-HT indicated an evolutionary divergence within reptilian species that might coincide with the emergence of endothermy ϳ320 million years ago (39).…”

Section: Resultsmentioning

confidence: 99%

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Function and Evolution of a Mosquito Salivary Protein Family

Calvo¹,

Mans²,

Andersen

et al. 2006

Journal of Biological Chemistry

236

299

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Saliva of blood-sucking arthropods contains a complex and diverse mixture of antihemostatic, antiinflammatory, and immunomodulatory compounds. The D7 salivary family of proteins is abundantly expressed in blood-feeding Diptera and is distantly related to the odorant-binding protein superfamily. In mosquitoes, two subfamilies exist, the long and short D7 proteins. Ticks and kissing bugs evolved salivary lipocalins that act as efficient scavengers of biogenic amines, and a similar function was postulated for the D7 proteins. Accordingly, we expressed the five members of the small D7 family of the African malaria vector Anopheles gambiae and a D7 long form from Aedes aegypti and showed by isothermal microcalorimetry, a modified and very sensitive non-equilibrium chromatography/spectrum distortion method, and by smooth muscle bioassay that four of these five short D7 proteins and the D7 long form bind serotonin with high affinity, as well as histamine and norepinephrine. The nonbinding D7 protein is poorly expressed in the salivary glands and appears to be on the path to becoming a pseudogene. Scavenging of host amines would antagonize their vasoconstrictor, platelet-aggregating, and pain-inducing properties. It appears that counteracting biogenic amines is of strong adaptive value in the convergent evolution of arthropods to hematophagy. This adaptation has been solved independently in ticks, bugs, and mosquitoes by co-option of either member of the lipocalin or, as shown here, by the odorant-binding protein families.At least 14 orders or families of arthropods (containing over 400 different genera and more than 15,000 species) independently evolved to feed on vertebrate blood (1). To accomplish this task, these animals evolved sophisticated cocktails of salivary pharmacologic reagents that affect blood clotting, platelet aggregation, vascular contraction, host immunity, inflammation, and angiogenesis. With the development of transcriptome analysis, the salivary compositional diversity of several hematophagous arthropods is being revealed at a fast pace; however, the majority of these proteins have no known function (2).Among many different families of proteins unique to hematophagous arthropods, the D7 family has been recognized to be specifically expressed in the salivary glands of adult Diptera. These proteins are distant relatives of the odorant-binding protein superfamily, of which they are a distinct branch. In mosquitoes, two D7 subfamilies exist, the short family having molecular mass of 15-20 kDa and the long with 27-30 kDa, whereas sand flies appear to have only the long forms (3-5). According to a recent sialotranscriptome analysis, Anopheles gambiae, the main African malaria vector, has three long and five short D7 proteins in chromosome arm 3R (6), arranged in an inverted tandem repeat. In the closely related mosquito Anopheles stephensi, one short D7 protein, named hamadarin, has been expressed and shown to have anticlotting activity (7). No other function has been described for the other protein memb...

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Function and Evolution of a Mosquito Salivary Protein Family

Calvo¹,

Mans²,

Andersen

et al. 2006

Journal of Biological Chemistry

236

299

View full text Add to dashboard Cite

show abstract

“…In mammals, anuclear small-sized platelets are produced in huge numbers by fragmentation of megakaryocytes, whereas in other vertebrates, thrombocytes containing nuclei play roles similar to those performed by platelets in mammals [47]. Traditionally, platelets have been considered to play major roles in hemostasis.…”

Section: Discussionmentioning

confidence: 99%

Pharmacological characterization of anaphylaxis-like shock responses induced in mice by mannan and lipopolysaccharide

Funayama¹,

Huang²,

Sato³

et al. 2009

International Immunopharmacology

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“…The inability of melanophores to exhibit a strong aggregative response to serotonin may be due to an altered or lack of serotonergic receptor expression in melanophores. While studies have shown varying serotonergic receptor expression in the Oncorhynchus mykiss (rainbow trout) brain (Khan and Deschaux, 1997;Khan et al, 1996), and it has been shown that serotonin does not circulate in the blood of salmon species (Maurer-Spurej, 2005), the presence or absence of such receptors has not been verified in O. tshawytscha melanophores. Adenosine and MSH both caused pigment dispersion, but interestingly, melanophores aggregated in the presence of 10 4 mM adenosine while dispersing at lower concentrations of adenosine.…”

Section: Discussionmentioning

confidence: 99%

Conservation of the chromatophore pigment response

Dukovcic

Hutchison

Trempy

2010

J of Applied Toxicology

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Toxicant sensing technology has evolved to include biological sensors, such as cell-based biosensors, which rely on viable cells to convey a measurable physiological signal. Chromatophores are a class of pigment cells that have been investigated as cell-based biosensors. We report the characterization of Oncorhynchus tshawytscha melanophores and describe the melanophore pigment response to neurotransmitters in terms of pigment area occupied. Compared with the previously described model, Betta splendens erythrophores, O. tshawytscha melanophores responded similarly, indicating that pigment responses are biologically conserved between these two species. Additionally, melanophores responded to mercuric chloride and sodium arsenite, similar to B. splendens erythrophores, suggesting that melanophores can be used as detectors for environmental toxicants. This report highlights the potential of O. tshawytscha melanophores to be used as cell-based biosensors to address environmental toxicity, and warrants a continued investigation to strengthen this technology and its applications.

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Circulating serotonin in vertebrates

Cited by 35 publications

References 65 publications

Function and Evolution of a Mosquito Salivary Protein Family

Function and Evolution of a Mosquito Salivary Protein Family

Pharmacological characterization of anaphylaxis-like shock responses induced in mice by mannan and lipopolysaccharide

Conservation of the chromatophore pigment response

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