Catfishes
Ictaluridae
Edwardsiella ictaluri
Fish Diseases
Fishes
Aquaculture
Fish Venoms
Effect of low ambient mineral concentrations on the accumulation of calcium, magnesium and phosphorus by early life stages of the air-breathing armoured catfish Megalechis personata (Siluriformes: Callichthyidae). (1/338)
The accumulation of calcium, magnesium and phosphorus was measured during an 8-week period in the early life stages of the air-breathing armoured catfish Megalechis personata acclimated to low-mineral fresh water (0.073 mmol l-1 calcium, 0.015 mmol l-1 magnesium, <0.001 mmol l-1 phosphate) and high-mineral fresh water (0.59 mmol l-1 calcium, 1.94 mmol l-1 magnesium, <0.001 mmol l-1 phosphate). The fish accumulated calcium twice as fast and phosphorus 1.5 times as fast in low-mineral fresh water (LMF) as in high-mineral fresh water (HMF), while the rate of accumulation of magnesium did not differ in LMF and HMF. The difference in the rates of accumulation of calcium and phosphorus between LMF and HMF was independent of the growth performance (food intake) in LMF and HMF. The mineral content of young M. personata from natural swamps and rainforest creeks in Suriname followed the LMF accumulation curves. The transition from aquatic respiration to bimodal respiration in the third week after hatching did not affect rates of mineral accumulation. The high rates of accumulation of calcium and magnesium of M. personata in LMF of 654 and 58 micromol h-1 kg-1, respectively, exceed the rates of uptake of calcium and magnesium of teleosts reported in the literature. The high rates of mineral accumulation in the early life stages of M. personata reflect the exponential growth during the first 8 weeks after hatching and the requirements of the juveniles while building their dermal armour. M. personata is well-adapted to neotropical fresh waters with an extremely low mineral content. The accumulation of calcium and phosphorus is discussed in relation to the function of the bony armour of M. personata. (+info)Isolation of a single carboxyl-carboxylate proton binding site in the pore of a cyclic nucleotide-gated channel. (2/338)
The pore of the catfish olfactory cyclic nucleotide-gated (CNG) channel contains four conserved glutamate residues, one from each subunit, that form a high-affinity binding site for extracellular divalent cations. Previous work showed that these residues form two independent and equivalent high-pKa (approximately 7.6) proton binding sites, giving rise to three pH-dependent conductance states, and it was suggested that the sites were formed by pairing of the glutamates into two independent carboxyl-carboxylates. To test further this physical picture, wild-type CNG subunits were coexpressed in Xenopus oocytes with subunits lacking the critical glutamate residue, and single channel currents through hybrid CNG channels containing one to three wild-type (WT) subunits were recorded. One of these hybrid channels had two pH-dependent conductance states whose occupancy was controlled by a single high-pKa protonation site. Expression of dimers of concatenated CNG channel subunits confirmed that this hybrid contained two WT and two mutant subunits, supporting the idea that a single protonation site is made from two glutamates (dimer expression also implied the subunit makeup of the other hybrid channels). Thus, the proton binding sites in the WT channel occur as a result of the pairing of two glutamate residues. This conclusion places these residues in close proximity to one another in the pore and implies that at any instant in time detailed fourfold symmetry is disrupted. (+info)Protein kinase Cbeta and delta selectively phosphorylate odorant and metabotropic glutamate receptors. (3/338)
Recombinant protein segments from a metabotropic glutamate receptor and from an odorant receptor were used as substrates in protein kinase C phosphorylation assays. Protein kinase Cbeta and delta phosphorylated an intracellular consensus phosphorylation site in the metabotropic glutamate receptor. Only protein kinase Cdelta phosphorylated a novel extracellular consensus phosphorylation site in the odorant receptor. These results suggest differential regulation of these receptors by protein kinase C isotypes. (+info)Influence of the mu-chain C-terminal sequence on polymerization of immunoglobulin M. (4/338)
Immunoglobulin (IgM) is found in various states of covalent polymerization (microL)n, where n is typically 8, 10, or 12. The usual form of IgM of bony fish is tetrameric (8 microL units) as compared to the pentameric form (10 microL units) observed in cartilaginous fish and mammals. Two hypotheses were tested in this study. First, that the length of the mu-chain C terminus following Cys575 determines whether an IgM polymerizes as a tetramer or as a pentamer. This was tested by examining the covalent polymerization state of mouse IgM mutated to contain a series of mu-chain C-termini from bony and cartilaginous fish. The results proved this hypothesis wrong: mouse IgM bearing the C-terminal sequence of shark, salmon and cod mu-chain behaved identically to native mouse IgM, forming predominantly (microL)10 and (microL)12 forms. The second hypothesis was that an additional Cys residue near the C terminus of the mu-chain is responsible for the multiple covalent structures seen in IgM of the channel catfish. The addition of a catfish C terminus to the mouse mu-chain resulted, as predicted, in the production of a series of covalently bonded forms, with the major species being (microL)4. When a Ser-Cys unit was removed from the catfish C terminus added to the mouse mu-chain, this resulted in production of IgM indistinguishable in structure from that of wild-type mouse IgM. (+info)Zebrafish leopard gene as a component of the putative reaction-diffusion system. (5/338)
It has been suggested, on a theoretical basis, that a reaction-diffusion (RD) mechanism underlies pigment pattern formation in animals, but as yet, there is no molecular evidence for the putative mechanism. Mutations in the zebrafish gene, leopard, change the pattern from stripes to spots. Interestingly each allele gives a characteristic pattern, which varies in spot size, density and connectivity. That mutations in a single gene can generate such a variety of patterns can be understood using a RD model. All the pattern variations of leopard mutants can be generated in a simulation by changing a parameter value that corresponds to the reaction kinetics in a putative RD system. Substituting an intermediate value of the parameter makes the patterns similar to the heterozygous fish. These results suggest that the leopard gene product is a component of the putative RD mechanism. (+info)Tandem repeat structure of rhamnose-binding lectin from catfish (Silurus asotus) eggs. (6/338)
The primary structure of catfish (Silurus asotus) egg lectin (SAL) was determined. SAL cDNA contained 1448-bp nucleotides and 308 amino acid residues, deduced from open reading frame. The SAL mature protein composed of 285-amino acid residues was followed by a predicted signal sequence having 23 residues. The mRNA of SAL was found to be expressed in eggs, but not in liver. SAL is composed of three tandem repeat domain structures divided into exactly 95 amino acid residues each, and all cysteine positions of each domain were completely conserved. Sequence homologies between the three domains, termed D1 (1-95), D2 (96-190) and D3 (191-285), were as follows; D1-D2, 28%; D2-D3, 33%; D1-D3, 43%. Two conserved peptide motifs, -(AN)YGR(TD)S(T)XCS(TGR)P- and -DPCX(G)T(Y)KY(L)-, appear to exist at the N- and C-terminal regions of each domain, respectively. The kinetic parameters of SAL obtained by measuring surface plasmon resonance were as follows: K(a) (M(-1)) for neohesperidosyl-BSA, 7. 1 x 10(6); for melibiosyl-BSA, 4.9 x 10(6); and for lactosyl-BSA, 5. 2 x 10(5). These results show that RBLs including SAL comprise a family of alpha-galactosyl binding lectins having characteristic tandem repeat domain structures. (+info)Pivotal role for the cytoplasmic carboxyl-terminal tail of a nonmammalian gonadotropin-releasing hormone receptor in cell surface expression, ligand binding, and receptor phosphorylation and internalization. (7/338)
The gonadotropin-releasing hormone receptor (GnRH-R) of the African catfish couples to phospholipase C and belongs to the large family of G protein-coupled receptors. We recently demonstrated that removal of the carboxyl-terminal tail (S331-Q379) from the catfish GnRH-R results in a loss of agonist binding; the current study sought to define more precisely the role of this region in receptor function. Progressive truncations of the carboxyl-terminal tail decreased cell surface expression detected by either enzyme-linked immunosorbent assay or agonist-binding. The two most truncated receptors (stop331 and stop337) showed no binding but were detected at the cell surface by enzyme-linked immunosorbent assay. All receptors able to bind agonist were also able to activate phospholipase C. The catfish GnRH-R was phosphorylated after agonist-occupation and use of truncated mutants showed this phosphorylation to be within the carboxyl-terminal tail. Furthermore, studies with S356A, S363A and SS356,363AA mutant receptors demonstrated that Ser363 is a major site of agonist-induced phosphorylation. The absence of this phospho-acceptor site markedly impaired agonist-mediated receptor internalization. In addition, both, Ser363 and the last 12 residues of the tail (not containing Ser363) were shown to be important for beta-arrestin-dependent internalization. These observations are relevant to the regulatory function of the carboxyl-terminal tail of G protein-coupled receptors in general and are particularly intriguing given the absence of this region in mammalian GnRH-Rs. (+info)Inhibitory and stimulatory interactions between endogenous gonadotropin-releasing hormones in the African catfish (Clarias gariepinus). (8/338)
In the brain of all vertebrate classes, chicken (c) GnRH-II ([His(5), Trp(7),Tyr(8)]GnRH, cGnRH-II) is expressed in the mesencephalon. In addition, at least one other form of GnRH is expressed in the preoptical area/hypothalamus. In the human pituitary stalk and the mouse median eminence, cGnRH-II is present together with mammalian GnRH. Similarly, in the pituitary of several teleost fish (e.g., goldfish and eel, but not salmon or trout), a teleost GnRH is found together with cGnRH-II. These GnRHs are not colocalized in the same cells. Hence, these GnRH peptides may differentially regulate gonadotropin secretion and, in addition, may exert their effects simultaneously. The current study therefore investigated the effects of combinations of the two forms of GnRH present in the African catfish (Clarias gariepinus) pituitary-cGnRH-II and catfish GnRH ([His(5),Asn(8)]GnRH, cfGnRH)-on the cytosolic free calcium concentration ([Ca(2+)](i)) in single, Fura-2-loaded catfish gonadotrophs, as well as their effects on both in vitro and in vivo LH secretion. Both inhibitory and stimulatory effects of combinations of cfGnRH and cGnRH-II on [Ca(2+)](i) were observed, which were mirrored by their effects on both in vitro and in vivo LH secretion. The following pattern became apparent. The effect of intermediate or maximal effective cfGnRH doses was inhibited by the simultaneous presence of subthreshold or borderline effective cGnRH-II doses. Conversely, subthreshold or borderline effective concentrations of cfGnRH enhanced the effects of intermediate and maximal concentrations of cGnRH-II. In addition, combinations of cfGnRH and cGnRH-II concentrations that were equally active when tested separately showed an additive effect. The observed interactions between the two GnRHs may be of particular physiological relevance in the control of seasonal LH levels in the African catfish, as well as in other teleost species. Moreover, the occurrence of mutual inhibitory and stimulatory interactions between endogenous GnRHs may be a widespread aspect of GnRH action in vertebrates. (+info)"Catfishes" is a term that refers to a group of ray-finned fish belonging to the order Siluriformes. However, in a medical or clinical context, "catfishing" has taken on a different meaning. It is a term used to describe the phenomenon of creating a false online identity to deceive someone, particularly in social media or dating websites. The person who creates the fake identity is called a "catfish." This behavior can have serious emotional and psychological consequences for those who are being deceived.
Ictaluridae is not a term that has a medical definition, as it pertains to the field of biology and zoology rather than medicine. Ictaluridae is the family of freshwater fishes commonly known as "North American catfishes." These fishes are characterized by their barbels, which resemble cats' whiskers, and their armored bodies.
However, in a medical context, certain types of Ictaluridae may be mentioned in relation to food safety or allergies. For example, if a patient has an allergy to fish, they may need to avoid consuming Ictaluridae species such as channel catfish or blue catfish. Similarly, if there is a concern about foodborne illness, certain types of Ictaluridae may be implicated in outbreaks of diseases such as scombrotoxin poisoning.
Therefore, while "Ictaluridae" itself does not have a medical definition, it is a term that may be used in medicine in relation to food safety or allergies.
'Edwardsiella ictaluri' is a gram-negative, rod-shaped bacterium that belongs to the family Enterobacteriaceae. It is a facultative anaerobe, which means it can grow in both the presence and absence of oxygen. This bacterium is known to cause enteric septicemia of catfish (ESC), a significant disease in farm-raised catfish in the United States. The infection can lead to high mortality rates in young fish, causing significant economic losses for the aquaculture industry. It's essential to maintain proper biosecurity measures and use effective vaccines to control ESC in farmed catfish.
"Fish diseases" is a broad term that refers to various health conditions and infections affecting fish populations in aquaculture, ornamental fish tanks, or wild aquatic environments. These diseases can be caused by bacteria, viruses, fungi, parasites, or environmental factors such as water quality, temperature, and stress.
Some common examples of fish diseases include:
1. Bacterial diseases: Examples include furunculosis (caused by Aeromonas salmonicida), columnaris disease (caused by Flavobacterium columnare), and enteric septicemia of catfish (caused by Edwardsiella ictaluri).
2. Viral diseases: Examples include infectious pancreatic necrosis virus (IPNV) in salmonids, viral hemorrhagic septicemia virus (VHSV), and koi herpesvirus (KHV).
3. Fungal diseases: Examples include saprolegniasis (caused by Saprolegnia spp.) and cotton wool disease (caused by Aphanomyces spp.).
4. Parasitic diseases: Examples include ichthyophthirius multifiliis (Ich), costia, trichodina, and various worm infestations such as anchor worms (Lernaea spp.) and tapeworms (Diphyllobothrium spp.).
5. Environmental diseases: These are caused by poor water quality, temperature stress, or other environmental factors that weaken the fish's immune system and make them more susceptible to infections. Examples include osmoregulatory disorders, ammonia toxicity, and low dissolved oxygen levels.
It is essential to diagnose and treat fish diseases promptly to prevent their spread among fish populations and maintain healthy aquatic ecosystems. Preventative measures such as proper sanitation, water quality management, biosecurity practices, and vaccination can help reduce the risk of fish diseases in both farmed and ornamental fish settings.
I believe there may be a misunderstanding in your question. The term "fishes" is not typically used in a medical context. "Fish" or "fishes" refers to any aquatic organism belonging to the taxonomic class Actinopterygii (bony fish), Chondrichthyes (sharks and rays), or Agnatha (jawless fish).
However, if you are referring to a condition related to fish or consuming fish, there is a medical issue called scombroid fish poisoning. It's a foodborne illness caused by eating spoiled or improperly stored fish from the Scombridae family, which includes tuna, mackerel, and bonito, among others. The bacteria present in these fish can produce histamine, which can cause symptoms like skin flushing, headache, diarrhea, and itchy rash. But again, this is not related to the term "fishes" itself but rather a condition associated with consuming certain types of fish.
Aquaculture is the controlled cultivation and farming of aquatic organisms, such as fish, crustaceans, mollusks, and aquatic plants, in both freshwater and saltwater environments. It involves the breeding, rearing, and harvesting of these organisms under controlled conditions to produce food, feed, recreational resources, and other products for human use. Aquaculture can take place in a variety of systems, including ponds, raceways, tanks, and cages, and it is an important source of protein and livelihoods for many people around the world.
Ciliophora is a group of protozoan organisms that are characterized by the presence of hair-like structures called cilia. Some species of Ciliophora can cause infections in humans, known as ciliophoriasis or ciliate infections. These infections typically occur in individuals with weakened immune systems, such as those with HIV/AIDS, cancer, or who are taking immunosuppressive drugs.
The most common way that Ciliophora infect humans is through the ingestion of contaminated food or water. Once inside the body, the ciliates can cause a range of symptoms depending on the species and the location of the infection. For example, infections in the gastrointestinal tract can cause abdominal pain, diarrhea, and vomiting, while lung infections can lead to coughing, wheezing, and difficulty breathing.
Treatment for Ciliophora infections typically involves the use of antiprotozoal medications, such as metronidazole or tinidazole. In severe cases, hospitalization may be necessary to manage symptoms and prevent complications. Preventing ciliophoriasis involves practicing good hygiene, avoiding contaminated food and water, and taking steps to boost the immune system in individuals who are at high risk of infection.
"Fish proteins" are not a recognized medical term or concept. However, fish is a source of protein that is often consumed in the human diet and has been studied in various medical and nutritional contexts. According to the USDA FoodData Central database, a 100-gram serving of cooked Atlantic salmon contains approximately 25 grams of protein.
Proteins from fish, like other animal proteins, are complete proteins, meaning they contain all nine essential amino acids that cannot be synthesized by the human body and must be obtained through the diet. Fish proteins have been studied for their potential health benefits, including their role in muscle growth and repair, immune function, and cardiovascular health.
It's worth noting that some people may have allergies to fish or seafood, which can cause a range of symptoms from mild skin irritation to severe anaphylaxis. If you suspect you have a fish allergy, it's important to consult with a healthcare professional for proper diagnosis and management.
Fish venoms are toxic substances produced by some species of fish, primarily found in their spines, fins, or skin. These venoms are used for defense against predators and can cause painful injuries to humans who come into contact with them. The venomous fishes belong to various taxonomic groups, including catfishes (order Siluriformes), stingrays (superorder Batoidea), scorpionfishes (family Scorpaenidae), weevers (family Trachinidae), and stonefishes (family Synanceiidae).
The composition of fish venoms varies among species, but they typically contain a mixture of proteins, enzymes, and small molecules that can induce local and systemic effects. Local reactions usually involve pain, swelling, and redness at the site of the injury, while systemic symptoms may include nausea, vomiting, difficulty breathing, paralysis, or even death in severe cases.
Immediate medical attention is required for fish venom injuries to manage pain, prevent infection, and treat potential systemic effects. Treatment usually involves removing any remaining venomous spines or fragments, immersing the wound in hot water (>45°C/113°F) to denature the proteins in the venom, and administering appropriate analgesics, antibiotics, and supportive care as needed.
Gills are specialized respiratory organs found in many aquatic organisms such as fish, crustaceans, and some mollusks. They are typically thin, feathery structures that increase the surface area for gas exchange between the water and the animal's bloodstream. Gills extract oxygen from water while simultaneously expelling carbon dioxide.
In fish, gills are located in the gill chamber, which is covered by opercula or protective bony flaps. Water enters through the mouth, flows over the gills, and exits through the opercular openings. The movement of water over the gills allows for the diffusion of oxygen and carbon dioxide across the gill filaments and lamellae, which are the thin plates where gas exchange occurs.
Gills contain a rich supply of blood vessels, allowing for efficient transport of oxygen to the body's tissues and removal of carbon dioxide. The counter-current flow of water and blood in the gills ensures that the concentration gradient between the water and the blood is maximized, enhancing the efficiency of gas exchange.