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PubMed1989

Afferent connections of the valvula cerebelli in two teleosts, the common goldfish and the green sunfish.

The afferent connections of the valvula cerebelli were examined in one cypriniform teleost (Carassius auratus) and one perciform teleost (Lepomis cyanellus) with the use of horseradish peroxidase as a retrograde tracer. Both species have ipsilateral input to the valvula from the central pretectal and dorsal accessory optic nuclei, the dorsal and ventral tegmental nuclei, the lateral nucleus of the valvula, the perilemniscal nucleus, and nucleus isthmi and contralateral input from the inferior olivary nucleus. In addition, Carassius has ipsilateral valvulopetal projections from the eminentia granularis, the prae-eminential nucleus, and the isthmic primary sensory trigeminal nucleus, whereas Lepomis has bilateral (stronger ipsilaterally) valvulopetal projections from the nucleus of the locus coeruleus and the rostral corpus cerebelli. The topographical order of the cerebellopetal projections of the lateral nucleus of the valvula and inferior olive is also described, as are differential inputs to various subdivisions of the cerebellum in the two species. Information on valvulopetal projections in teleosts has thus far been limited to electroreceptive mormyrids. The present study shows that many valvular inputs related to electroreception in mormyrids have no homologue in Carassius and Lepomis. Finally, the present study indicates that the rostral part of the corpus cerebelli, but not the valvula cerebelli, in teleosts is the homologue of the anterior lobe of the corpus cerebelli in cartilaginous fishes. Thus, the valvula cerebelli is a shared derived feature (synapomorphy) of all ray-finned fishes.

Animals↗
PubMed1994

6-phosphofructo 2-kinase/fructose 2,6-bisphosphatase in liver of the teleost Sparus aurata.

6-Phosphofructo 2-kinase/fructose 2,6-bisphosphatase was purified from the liver of the teleost fish Sparus aurata and the enzymatic activities were characterized kinetically. Both activities copurify, being dimers of relative molecular mass of 98 kDa with subunits of M(r) 54 kDa. Although both specific activities are in the range of mammalian liver isozymes, the Kmfru 6-P of teleost 6-phosphofructo 2-kinase is 3 times that in rat liver. The S. aurata 6-phosphofructo 2-kinase is inhibited by ADP, citrate and phosphoenolpyruvate, and fructose-2,6-bisphosphatase presents inhibition by fru 6-P. Unlike the rat liver enzyme, the kinase reaction is scarcely inhibited by glycerol 3-P. The teleost isozyme is substrate for the cyclic-AMP-dependent protein kinase, as can be followed by the incorporation of 32P from ATP into the enzyme. Phosphorylation of the enzyme changes its kinetic behavior, leading to a form with a lower kinase/bisphosphatase activity ratio. No change is detected in the fru 6-P dependence of 6-phosphofructo 2-kinase, but the phosphorylated form is more sensitive to inhibition by effectors, especially by glycerol 3-phosphate. Phosphorylation enhances the fructose-2,6-bisphosphatase Vmax activity twofold. The implications of all these kinetic characteristics in the control of hepatic fructose-2,6-bisphosphate levels are discussed in the context of the studies in S. aurata in vivo. The results support the hypothesis that differences in the regulation of 6-phosphofructo 2-kinase/fructose-2,6-bisphosphatase are a key point for the specific adaptations of carbohydrate metabolism in this teleost fish.

Animals↗
PubMed1995

The muscle isoform of 6-phosphofructo 2-kinase/fructose 2,6-bisphosphatase of the teleost Sparus aurata: relationship with the liver isoform.

The liver isoform of 6-phosphofructo 2-kinase/fructose 2,6-bisphosphatase of the teleost fish Sparaus aurata has several characteristics similar to the skeletal muscle isoform of mammals. In order to ascertain the relation between muscle and liver isoforms in teleost, 6-phosphofructo 2-kinase/fructose 2,6-bisphosphatase was purified from skeletal muscle of S. aurata. The muscle isozyme is composed of subunits with a molecular weight of 54 kDa, is bifunctional, and has an activity ratio kinase to bisphosphatase of 2.5. Muscle 6-phosphofructo 2-kinase is not sensitive to glycerol 3-phosphate inhibition and has noncooperative KmATP, higher than the liver isozyme. Thus, the kinetic characteristics of the muscle were distinguishable from the liver isozyme. Furthermore, the muscle isozyme is not a substrate of cAMP-dependent protein kinase. Despite those differences, two polyclonal antibodies raised against purified liver and muscle isozymes from S. aurata are not able to distinguish between them. Both antisera recognize with lower affinity recombinant rat liver 6-phosphofructo 2-kinase/fructose 2,6-bisphosphatase. A third antibody raised against the rat liver isozyme was also able to immunoprecipitate the teleost enzymes. The close immunological properties found suggest that S. aurata isozymes share epitopes in common. Considering the kinetic and immunological data reported, it is likely that the skeletal muscle/liver isozymes in teleost are products of a differentially spliced transcript of the same gene, as it is in rat. As those species are distant in vertebrate evolution, the similitude suggest that a common ancestral gene is involved in the muscle/liver 6-phosphofructo 2-kinase/fructose 2,6-bisphosphatase system in vertebrates.

Animals↗
PubMed1994

Induction of vitelline envelope proteins by estradiol-17 beta in 10 teleost species.

Induction of vitelline envelope proteins by estradiol-17 beta was investigated in 14 teleost species from five systematic groups to assess whether estradiol-17 beta controls the synthesis of vitelline envelope proteins in teleost fish. Vitelline envelope proteins were detected in plasma from fish treated with estradiol-17 beta using three different antisera directed against vitelline envelope proteins from three teleosts. Induction of vitelline envelope proteins was demonstrated in 10 species. In 6 of these species males were available and used to demonstrate that the synthesis of vitelline envelope proteins is not restricted to the ovaries. The immunoreactivity of the proteins varied considerably within and between species. It is suggested that the synthesis of vitelline envelope proteins is controlled by estradiol-17 beta in the majority of teleost species.

Animals↗
PubMed1998

Gonadotropin-releasing hormone (GnRH) in ancient teleosts, the bonytongue fishes: putative origin of salmon GnRH.

The molecular forms of gonadotropin-releasing hormone (GnRH) were examined in the bonytongue fishes (Osteoglossomorpha), one of the most ancient living teleost groups. These fish represent a phylogenetic link between the early ray-finned fishes and the modern teleosts. Five representative species from four of six bonytongue families were examined for GnRH using high-performance liquid chromatography and radioimmunoassay techniques with antisera raised against salmon (s), chicken-II (c-II), and mammalian (m) forms of GnRH. Salmon GnRH and cGnRH-II were identified in four of the species (arawana, elephantnose, false featherfin, Asiatic featherfin) whereas in the butterfly fish, mGnRH and cGnRH-II were identified. Our data suggest that teleosts such as eels and butterfly fish, which have mGnRH like that of even earlier ray-finned fishes, may have evolved before fish with sGnRH. We also suggest that sGnRH first appeared in the Osteoglossomorpha. The phylogenetic relationship of the eels (Anguillidae), butterfly fish (Pantodontidae), and bonytongue fish among other teleosts needs to be reexamined using additional characteristics.

Animals↗
PubMed1995

Obtaining a more resolute teleost growth hormone phylogeny by the introduction of gaps in sequence alignment.

In order to obtain a more resolute phylogeny of teleosts based on growth hormone (GH) sequences, phylogenetic analyses were performed in which deletions (gaps), which appear to be order specific, were upheld to maintain GH's structural information. Sequences were analyzed at 194 amino acid positions. In addition, the two closest genealogically related groups to the teleosts, Amia calva and Acipenser guldenstadti, were used as outgroups. Modified sequence alignments were also analyzed to determine clade stability. Analyses indicated, in the most parsimonious cladogram, that molecular and morphological relationships for the orders of fishes are congruent. With GH molecular sequence data it was possible to resolve all clades at the familial level. Analyses of the primary sequence data indicate that: (a) the halecomorphean and chondrostean GH sequences are the appropriate outgroups for generating the most parsimonious cladogram for teleosts; (b) proper alignment of teleost GH sequence by the inclusion of gaps is necessary for resolution of the Percomorpha; and (c) removal of sequence information by deleting improperly aligned sequence decreases the phylogenetic signal obtained.

Amino Acid Sequence↗
PubMed1992

Parvalbumin immunoreactive neurons and fibres in the teleost cerebellum.

The distribution of parvalbumin- (PV) immunopositive cell bodies and fibres in the cerebellum of two species of freshwater teleosts (Salmo gairdneri and Barbus meridonalis) was studied using a monoclonal antibody and the avidin-biotin immunoperoxidase technique. A clear laminated pattern of PV immunoreactivity was observed. After PV-immunostaining, Purkinje cells were strongly labelled in their cell bodies, the initial segments of the axons and the dendritic trees. In the molecular layer, only the dendritic branches of the Purkinje cells were PV-positive. In the granule cell layer, extensive axonal plexuses and scattered cell bodies were observed. Most of the immunopositive perikarya were unequivocally identified as displaced Purkinje cells, whereas a reduced number of smaller neurons with unstained dendrites was also found. Eurydendroid cells, the efferent neurons of the teleost cerebellum, were negative; however, they were impinged upon by numerous PV-positive boutons, corresponding to terminals of Purkinje cell axons. Parallel fibres and climbing fibres, as well as stellate cells and granule cells were negative. Basket cells (or deep stellate cells) whose existence in the teleost cerebellum is discussed, were also not observed. The immunoreactivity distribution pattern for PV in the teleost cerebellum differs from previous observations on the localization of this protein in the cerebellum of amniotes.

Animals↗
PubMed1998

Responses of the red blood cells from two high-energy-demand teleosts, yellowfin tuna (Thunnus albacares) and skipjack tuna (Katsuwonus pelamis), to catecholamines.

In fishes, catecholamines increase red blood cell intracellular pH through stimulation of a sodium/proton (Na+/H+) antiporter. This response can counteract potential reductions in blood O2 carrying capacity (due to Bohr and Root effects) when plasma pH and intracellular pH decrease during hypoxia, hypercapnia, or following exhaustive exercise. Tuna physiology and behavior dictate exceptionally high rates of O2 delivery to the tissues often under adverse conditions, but especially during recovery from exhaustive exercise when plasma pH may be reduced by as much as 0.4 pH units. We hypothesize that blood O2 transport during periods of metabolic acidosis could be especially critical in tunas and the response of rbc to catecholamines elevated to an extreme. We therefore investigated the in vitro response of red blood cells from yellowfin tuna (Thunnus albacares) and skipjack tuna (Katsuwonus pelamis) to catecholamines. Tuna red blood cells had a typical response to catecholamines, indicated by a rapid decrease in plasma pH. Amiloride reduced the response, whereas 4,4'diisothiocyanatostilbene-2,2'-disulphonic acid enhanced both the decrease in plasma pH and the increase in intracellular pH. Changes in plasma [Na+], [Cl-], and [K+] were consistent with the hypothesis that tuna red blood cells have a Na+/H+ antiporter similar to that described for other teleost red blood cells. Red blood cells from both tuna species were more responsive to noradrenaline than adrenaline. At identical catecholamine concentrations, the decrease in plasma pH was greater in skipjack tuna blood, the more active of the two tuna species. Based on changes in plasma pH, the response of red blood cells to catecholamines from both tuna species was less than that of rainbow trout (Oncorhynchus mykiss) red blood cells, but greater than that of cod (Gadus morhua) red blood cells. Noradrenaline had no measurable influence on the O2 affinity of skipjack tuna blood and only slightly increased the O2 affinity of yellowfin tuna blood. Our results, therefore, do not support our original hypothesis. The catecholamine response of red blood cells from high-energy-demand teleosts (i.e., tunas) is not enhanced compared to other teleosts. There are data on changes in cardio-respiratory function in tunas caused by acute hypoxia and modest increases in activity, but there are no data on the changes in cardio-respiratory function in tunas accompanying the large increases in metabolic rate seen during recovery from exhaustive exercise. However, we conclude that during those instances where high rates of O2 delivery to the tissues are needed, tunas' ability to increase cardiac output, ventilation volume, blood O2 carrying capacity, and effective respiratory (i.e., gill) surface area are probably more important than are the responses of red blood cells to catecholamines. We also use our data to investigate the extent of the Haldane effect and its relationship to blood O2 and CO2 transport in yellowfin tuna. Yellowfin tuna blood shows a large Haldane effect; intracellular pH increases 0.20 units during oxygenation. The largest change in intracellular pH occurs between 40-100% O2 saturation, indicating that yellowfin tuna, like other teleosts, fully exploit the Haldane effect over the normal physiological range of blood O2 saturation.

4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid↗
PubMed1985

Non-specific cytotoxic activity of teleost leukocytes.

The existence of lymphoid cells with "natural" killer activity in mammals and birds has been known for some time. Several previous reports have demonstrated similar activity in carp and catfish kidney leukocytes. However, the activity previously reported was directed towards established mammalian cell lines. In this report we confirm the existence of spontaneous killer activity in other species of teleosts, including salmonids. This spontaneous cytotoxic activity is directed towards several established teleost, as well as mammalian, cell lines. Cytotoxic activity appears to be optimal at 20 degrees C in an 8 hour 51Cr release assay. The RTG-2, AS, GS and EPC cell lines of teleost origin are susceptible to lysis by kidney, spleen, and blood leukocytes of Salmo salar, Salmo gairdneri, and Notemigonus crysoleucas. Furthermore, the susceptibility of the RTG-2 and AS teleost cell lines to killing by kidney leukocytes of both S. salar and S. gairdneri was significantly enhanced by preinfection of the target cells with infectious pancreatic necrosis virus.

Animals↗
PubMed1984

Isolation and characterization of an asparagine-linked keratan sulfate from the skin of a marine teleost, Scomber japonicus.

Keratan sulfate was isolated from the skin of Pacific mackerel (Scomber japonicus) after exhaustive digestion with pronase followed by ethanol precipitation and fractionation on a cellulose column with 0.3% recovery of dried material. The keratan sulfate preparation was separated into four major fractions by Dowex-1 column chromatography. The chemical and infrared spectrum analyses of the four fractions showed a high degree of heterogeneity in sulfation. Since the carbohydrate-peptide linkage in the teleost skin keratan sulfate was found to be stable in alkali, and asparagine was the predominant amino acid, the asparagine residue in the peptide backbone was most likely to be involved in the N-glycosyl linkage with the carbohydrate moiety. Besides the type of carbohydrate-peptide linkage, the teleost skin keratan sulfate is very similar to corneal keratan sulfate (keratan sulfate I) in two respects: (1) The teleost skin and bovine corneal keratan sulfates were hydrolyzed much faster by endo-beta-galactosidase than the whale nasal cartilage keratan sulfate (keratan sulfate II). (2) Although the teleost skin keratan sulfate showed considerable polydispersity, the molecular weight was in the same range as the corneal keratan sulfate, and it was relatively higher than that of the cartilage keratan sulfate.

Amino Acids↗
PubMed1987

Fish skin type I collagen: wide distribution of an alpha 3 subunit in teleosts.

1. Skin Type I collagen was isolated from 15 species of teleosts. 2. Chromatographic and electrophoretic analyses revealed that most of the teleost skin collagens possessed a unique subunit, alpha 3, which had not been detected in other vertebrate Type I collagens. 3. The skin collagen seems to exist as an alpha 1 alpha 2 alpha 3 heterotrimer in many teleosts and as an (alpha 1)2 alpha 2 heterotrimer in some teleosts.

Animals↗
PubMed2004

Two tyrosine hydroxylase genes in teleosts.

We report the finding of two non-allelic genes encoding tyrosine hydroxylase (TH) from the diploid teleost barramundi Lates calcarifer. Barramundi TH1 is the homologue of the higher vertebrate TH genes and encodes a protein of 489 amino acids that shares 90% sequence identity to the THs of other teleost species. A second non-allelic tyrosine hydroxylase gene (TH2) encodes a protein of 472 amino acids and shares 62% identity with TH1 and the vertebrate THs. TH1 mRNA is found in the brain and kidney of barramundi while TH2 mRNA is found only in brain. The TH2 gene is also present in the genomes of the pufferfish Takifugu and zebrafish Danio. Estimates of the rates of nucleotide substitution suggest the teleost TH2 genes are selectively constrained although not to the degree seen in the TH1 genes. Differential regulation of the two TH genes is, however, indicated by differences in transcript distribution, the nature of the Ca2+-responsive elements found in the proximal promoter region and the lack of recognised phosphorylation sites in TH2. Preservation of two apparently functional TH genes in phylogenetically distant teleost species is consistent with the notion of partitioning of function between duplicate genes.

Amino Acid Sequence↗
PubMed2005

Tributyltin inhibits osteoblastic activity and disrupts calcium metabolism through an increase in plasma calcium and calcitonin levels in teleosts.

To examine the direct effects of tributyltin acetate (TBTA) on osteoclasts and osteoblasts, teleost scale, which has both osteoclasts and osteoblasts and is similar to mammalian membrane bone, was used in the present study. The activities of tartrate-resistant acid phosphatase and alkaline-phosphatase, as respective indicators of activity in both cells, were used. In freshwater teleost (goldfish) and marine teleosts (nibbler and wrasse), the osteoclastic activity in the scales did not change as a result of TBTA treatment (10(-9) to 10(-5) M). However, the osteoblastic activity decreased in the goldfish, nibbler, and wrasse after 6 h of incubation. In goldfish, even 10(-10) M of TBTA significantly inhibited the osteoblastic activity. The inhibitory activity in goldfish was stronger than that in nibbler and wrasse. Therefore, details of the mechanism were examined using goldfish. The mRNA expressions of the estrogen receptor and insulin-like growth factor-I, which participate in osteoblastic growth and differentiation, decreased in the TBTA-treated scales. However, the mRNA expression of metallothionein (MT), a metal-binding protein that protects the organism from heavy metal, increased much less than those of cadmium and methyl-mercury. Furthermore, we showed that the plasma calcium and hypocalcemic hormone (calcitonin) level increased in goldfish kept in water containing TBTA (10(-10) and 10(-8) M). The current data are the first to demonstrate that, in teleosts, TBTA inhibits osteoblastic activity without affecting osteoclastic activity and disrupts the calcium metabolism, including the calcemic hormone, in goldfish.

Animals↗
PubMed2004

Intermedin, a novel calcitonin family peptide that exists in teleosts as well as in mammals: a comparison with other calcitonin/intermedin family peptides in vertebrates.

Endocrine regulation in vertebrates is critical for the adaptation and regulation of homeostasis. The G protein-coupled receptor (GPCR) signaling transduction system represents one of the most ancient forms of cell surface signaling. Recently, comparative sequence analysis has aided in the identification and pairing of a variety of ligand/GPCR signaling systems. Among the ligands of type II GPCRs, the calcitonin family peptides including calcitonin, alpha-calcitonin gene-related peptide (alphaCGRP), betaCGRP, adrenomedullin, and amylin are among the best studied hormones, and the founding member, calcitonin, was originally identified and isolated from teleosts. This unique group of peptides shares a conserved tertiary structure with an N-terminal disulfide-bridged ring. In mammals, these peptides signal through two closely related type II GPCRs and three unique receptor activity-modifying proteins. Recently, based on the analysis of multiple vertebrate genomes, we identified a novel calcitonin/CGRP family peptide named intermedin. Here we show that in humans the five paralogous family genes, calcitonin, CGRP, amylin, adrenomedullin, and intermedin, evolved before the emergence of modern vertebrates, and that teleost genomes carry multiple copies of these co-evolved hormone genes. Sequence comparison showed that each of these genes is highly conserved in different vertebrates and that multiple copies of these peptides in teleosts could be derived from ancient genome duplication and/or lineage-specific intragenic duplications. The present article provides an overview of the calcitonin/intermedin family peptides found in teleost and mammalian genomes, and describes their putative functions. In addition, we demonstrate that one of the intermedin orthologs deduced from the pufferfish (Fugu rubripes) genome shares a conserved signaling activity with mammalian intermedin. The combined results indicate that the physiology associated with each of these family peptides likely evolved during early vertebrate evolution and diverged to serve select physiological functions in different vertebrates.

Adrenomedullin↗
PubMed2026

Ovarian expression and function of neuropeptide systems in teleosts and anurans.

The hypothalamic-pituitary-gonadal axis regulates reproduction, sexual maturation, and spawning behaviours. Its evolutionary origins trace back to primitive jawless fish and has been well characterized in teleosts. Recent advances in multi-species genome sequencing, annotation, and experimental approaches for identifying and characterizing key regulators have advanced understanding of neuroendocrine regulation in teleost reproduction, reshaping existing models. Early studies in amphibians established that steroids are critical regulators of final oocyte maturation. Subsequent work in anurans revealed complex interactions among theca cells, follicular cells, and oocytes, supporting a three-cell model in which oocytes contribute to their own steroidogenic environment, challenging the traditional two-cell view of ovarian steroidogenesis. In teleosts, however, direct evidence that oocytes support steroid precursor delivery to theca and follicular cells is limited, and whether a comparable three-cell model applies remains an open hypothesis. Across both taxa, the roles of locally produced neuropeptides in coordinating interactions among theca cells, follicular cells, and oocytes remain largely uncharacterized. Here, we provide a short review of the localization and potential autocrine/paracrine functions of neuropeptides in teleost and amphibian ovaries and discuss existing knowledge gaps. We identify opportunities to leverage detailed localization studies that map neuropeptides to specific ovarian cell types and developmental stages, and discuss how integrating traditional and emerging experimental approaches can advance comparative studies in ovarian endocrinology. This work will improve our understanding of reproductive regulation in fishes and frogs, with applications in captive breeding, aquaculture, and endocrine disruption research.

Autocrine↗
PubMed1997

Genomic structure and sequence of the pufferfish (Fugu rubripes) growth hormone-encoding gene: a comparative analysis of teleost growth hormone genes.

A nested polymerase chain reaction (PCR) technique for amplifying a fragment of the gene (GH) encoding teleost growth hormone has been developed. Using this technique, a fragment of the pufferfish, Fugu rubripes and Arothron maculatus, dwarf gourami, Colisa lalia; guppy, Poecilia reticulata; and goldfish, Carassius auratus GH genes were cloned. The Fugu rubripes (Fugu) gene fragment was used to isolate the GH gene from a Fugu genomic library. The complete nucleotide sequence of a 8.5-kb SacI genomic fragment containing the Fugu GH gene has been determined. The GH gene spans 2.5 kb from the first codon to polyadenylation signal, and contains six exons and five introns similar to the GH genes of salmonids, tilapia, barramundi, flounder and yellowtail. The GH introns contain microsatellite and satellite sequences. The microsatellites found in the fifth intron of the GH gene are also present in the corresponding introns of tilapia, barramundi and flounder GH genes. Southern analysis revealed that the GH gene is a single-copy gene in the Fugu. The promoter region of the Fugu GH gene contains conserved sequences that are likely to be involved in the pituitary-specific expression of the gene. A phylogenetic tree of nucleotide (nt) sequences of all known teleost GH genes has been inferred using the distance matrix method. The topology of this tree reflects the major phylogenetic groupings of teleosts. The intron patterns and repetitive sequences of GH genes can serve as useful natural markers for the classification and phylogenetic studies of teleosts.

Amino Acid Sequence↗
PubMed1997

Expression of cytochrome oxidase in hair cells of the teleost utricle.

Ultrastructural variation in some cytoplasmic organelles and synaptic structures is one characteristic distinguishing the types of hair cells in the teleost ear. In this study, we explored differences in mitochondria by analyzing mitochondrial reactivity for cytochrome oxidase (COX) in hair cells of the teleost utricle. The reactivity for COX within mitochondria in the subcuticular compartment directly beneath the cuticular plate differentiated among hair cells in utricles of three teleost species, Carassius auratus, Pantodon buchholzi, and Astronotus ocellatus. Mitochondria in the subcuticular region of hair cells in the striola reacted intensely. Within juxtastriola and extrastriolar hair cells near the striola, mitochondria reacted at a lowered intensity than in striolar hair cells. Subcuticular mitochondria of extrastriolar hair cells located distant from the striola reacted negligibly. The reactivity of mitochondria in other cytoplasmic compartments did not provide similar evidence for distinguishing among teleost hair cells. Mitochondria within intraepithelial branches of the eighth nerve terminals in the different utricular regions reacted to COX histochemistry commensurate with their respective presynaptic hair cells. Branches of sensory afferent neurons innervating striolar hair cells displayed a dense COX reaction. Sensory afferents innervating the extrastriolar hair cells did not display many mitochondria at synapses nor, when present, was the staining as dense. The presynaptic side of the hair cell-afferent nerve synapse usually, but not always, contained reactive mitochondria. The presynaptic side of the efferent nerve-hair cell synapse did not necessarily contain mitochondria. Mitochondria filling the cytoplasm in a type of juxtamacula cell revealed uniformly dense COX reactivity.

Animals↗
PubMed2003

Iron acquisition by teleost fish.

Iron is a vital micronutrient for teleost fish, being an integral component of proteins involved in cellular respiration and oxygen transfer. However, in excess iron is toxic, and fish need to balance uptake to prevent deficiency vs. potential toxicity. This review assesses the current physiological and molecular knowledge of the mechanisms of iron acquisition in the teleost fish. It focuses on freshwater teleost fish when assessing the gill as a possible site for iron acquisition, and includes a summary of geochemical processes that govern aquatic iron bioavailability. It focuses on marine teleost fish for assessing the mechanism of intestinal iron uptake. Physiological evidence indicates that iron preferentially crosses the apical membrane of both the gills and intestine in the ferrous (Fe2+) state. Molecular evidence supports this, demonstrating the presence of homologues in fish to the large Slc 11a family of evolutionary conserved proteins linked to Fe2+ transport. This symporter is probably linked to a reductase, which reduces either ferric (Fe3+) or organic complexed iron to Fe2+ prior to uptake.

Animals↗