Squalus acanthias
Dogfish
Sharks
Salt Gland
Squalus
Skates (Fish)
Cadmium Radioisotopes
Dihydroorotate Oxidase
Gills
Melanocyte-Stimulating Hormones
Acid-Base Equilibrium
Water-Electrolyte Balance
Urea
Sodium-Potassium-Exchanging ATPase
Endothelin B receptor Ca2+ signaling in shark vascular smooth muscle: participation of inositol trisphosphate and ryanodine receptors. (1/31)
In mammals, endothelin receptors are sub-classified into ET(A) receptors (ET(A)R), which are purely constrictive in vascular smooth muscle (VSM), and ET(B)R, which may produce constriction in VSM or dilatation by stimulating the production of nitric oxide (NO) from endothelial cells. In contrast, previous studies suggested that shark VSM is stimulated exclusively by ET(B)R. The Ca(2+) signaling pathways utilized by shark VSM in response to stimulation by endothelin-1 (ET-1) have not previously been investigated. We measured cytosolic Ca(2+) concentration ([Ca(2+)](i)) in fura-2-loaded VSM of anterior mesenteric artery of Squalus acanthias and show that the ET(B)R agonists IRL 1620 and sarafotoxin S6c (SRX) increase [Ca(2+)](i) in VSM to the same extent as ET-1 and ET(B)R appears to be the only ETR subtype in sharks. To investigate the participation of the inositol trisphosphate (IP(3)) receptors (IP(3)R), we utilized two inhibitors of the mammalian IP(3)R, TMB-8 and 2-APB. In Ca(2+)-free Ringer, these agents inhibit the response to ET(B)R agonist stimulation by 71%. The ryanodine-sensitive receptor (RyR) may be activated by low concentrations of ryanodine, by abrupt local increases of [Ca(2+)](i), (calcium-induced calcium release) or by cyclic adeninediphosphate ribose (cADPR). We employed three inhibitors of activation of the RyR, Ruthenium Red, 8-Br cADPR and high concentrations of ryanodine; these agents blocked the [Ca(2+)](i) response to ET(B)R agonist stimulation by a mean of 39%. These data show for the first time that in VSM of the shark, ET(B)R activation stimulates both IP(3)R and RyR, and that cADPR is involved in RyR activation. (+info)Characterization of a novel interaction between the secretory Na+-K+-Cl- cotransporter and the chaperone hsp90. (2/31)
The first isoform of the Na(+)-K(+)-Cl(-) cotransporter (NKCC1) is of central importance for the control of cellular ion concentration and epithelium-mediated salt secretion. Several studies have established that a change in intracellular [Cl(-)] (Cl(-)(i)) represents a key signaling mechanism by which NKCC1-induced Cl(-) movement is autoregulated and by which Cl(-) entry and exit on opposite sides of polarized cells are coordinated. Although this signaling mechanism is coupled to a pathway that leads to post-translational modification of the carrier, no unifying model currently accounts for the ion dependence of NKCC1 regulation. In this paper, evidence is presented for the first time that hsp90 associates with the cytosolic C terminus of NKCC1, probably when the carrier is predominantly in its unfolded form during early biogenesis. Evidence is also presented that the Cl(-)(i)-dependent regulatory pathway can be activated by a thermal stress but that it is no longer operational if NKCC1-expressing cells are pretreated with geldanamycin, an antibiotic that inhibits hsp90, albeit nonspecifically. Taken together, our data indicate that binding of hsp90 to NKCC1 may be required for Na(+)-K(+)-Cl(-) cotransport to occur at the cell surface and that it could play an important role in ion-dependent signaling mechanisms, insofar as the maneuvers that were used to alter the expression or activity of the chaperone do not exert their main effect by inducing other cellular events such as the unfolded protein response. Further studies will be required to elucidate the functional relevance of this novel interaction. (+info)Stage and season effects on cell cycle and apoptotic activities of germ cells and Sertoli cells during spermatogenesis in the spiny dogfish (Squalus acanthias). (3/31)
To understand the processes involved in the spatial and temporal maturation of testicular cells in Squalus acanthias, we used standard morphometry, proliferating-cell nuclear antigen (PCNA) and terminal deoxynucleotidyl transferase-mediated dUTP nick end-labelling (TUNEL) immunohistochemistry. Except for immature spermatocysts (germinal zone, GZ; early-stage pre-meiotic, E-PrM), the number of cysts in all subsequent stages and the total number of cysts in the spermatogenic progression varied seasonally. The spermatogenic cycle spans about 2 years and is interrupted by germcell clone deletion via apoptosis at the mitosis-meiosis transition in April/May, manifesting as a zone of degeneration (ZD). Rate of displacement of the ZD across the testis diameter indicates that late-stage premeiotic (L-PrM) generations 12-13 require 9-10 months to reach the mature-spermatid stage. Also, the number of cysts completing spermatogenesis is approximately 4-5-fold less than the number that entered spermatogenesis proper 2 years earlier. Pronounced gonocytogenesis in the germinal ridge was coincident with ZD formation in April/May, but it was absent in the fall when mature spermatogonial and meiotic activities had resumed. Whereas strong Sertoli cell PCNA immunoreactivity dominated the GZ cyst cell-cycle activities throughout the year, except during the spring/summer months, the spermatogonial- and Sertoli-cell PCNA indices in E-PrM cysts were inversely related. PCNA immunoreactivity in spermatocytes was seasonal and dependent on the stage of meiosis. TUNEL labelling was limited to spermatogonia and increased stage-dependently in the PrM region (L-PrM = mid-stage PrM >>E-PrM >>GZ), correlating with ZD formation, in a season-dependent manner. Results imply that effects of normal regulatory factors in Squalus are stage- and process-specific. (+info)Regulation of branchial V-H(+)-ATPase, Na(+)/K(+)-ATPase and NHE2 in response to acid and base infusions in the Pacific spiny dogfish (Squalus acanthias). (4/31)
To study the mechanisms of branchial acid-base regulation, Pacific spiny dogfish were infused intravenously for 24 h with either HCl (495+/- 79 micromol kg(-1) h(-1)) or NaHCO(3) (981+/-235 micromol kg(-1) h(-1)). Infusion of HCl produced a transient reduction in blood pH. Despite continued infusion of acid, pH returned to normal by 12 h. Infusion of NaHCO(3) resulted in a new steady-state acid-base status at approximately 0.3 pH units higher than the controls. Immunostained serial sections of gill revealed the presence of separate vacuolar proton ATPase (V-H(+)-ATPase)-rich or sodium-potassium ATPase (Na(+)/K(+)-ATPase)-rich cells in all fish examined. A minority of the cells also labeled positive for both transporters. Gill cell membranes prepared from NaHCO(3)-infused fish showed significant increases in both V-H(+)-ATPase abundance (300+/-81%) and activity. In addition, we found that V-H(+)-ATPase subcellular localization was mainly cytoplasmic in control and HCl-infused fish, while NaHCO(3)-infused fish demonstrated a distinctly basolateral staining pattern. Western analysis in gill membranes from HCl-infused fish also revealed increased abundance of Na(+)/H(+) exchanger 2 (213+/-5%) and Na(+)/K(+)-ATPase (315+/-88%) compared to the control. (+info)Selective permeability barrier to urea in shark rectal gland. (5/31)
Elasmobranchs such as the dogfish shark Squalus acanthius achieve osmotic homeostasis by maintaining urea concentrations in the 300- to 400-mM range, thus offsetting to some degree ambient marine osmolalities of 900-1,000 mosmol/kgH(2)O. These creatures also maintain salt balance without losing urea by secreting a NaCl-rich (500 mM) and urea-poor (18 mM) fluid from the rectal gland that is isotonic with the plasma. The composition of the rectal gland fluid suggests that its epithelial cells are permeable to water and not to urea. Because previous work showed that lipid bilayers that permit water flux do not block flux of urea, we reasoned that the plasma membranes of rectal gland epithelial cells must either have aquaporin water channels or must have some selective barrier to urea flux. We therefore isolated apical and basolateral membranes from shark rectal glands and determined their permeabilities to water and urea. Apical membrane fractions were markedly enriched for Na-K-2Cl cotransporter, whereas basolateral membrane fractions were enriched for Na-K-ATPase. Basolateral membrane osmotic water permeability (P(f)) averaged 4.3 +/- 1.3 x 10(-3) cm/s, whereas urea permeability averaged 4.2 +/- 0.8 x 10(-7) cm/s. The activation energy for water flow averaged 16.4 kcal/mol. Apical membrane P(f) averaged 7.5 +/- 1.6 x 10(-4) cm/s, and urea permeability averaged 2.2 +/- 0.4 x 10(-7) cm/s, with an average activation energy for water flow of 18.6 kcal/mol. The relatively low water permeabilities and high activation energies argue strongly against water flux via aquaporins. Comparison of membrane water and urea permeabilities with those of artificial liposomes and other isolated biological membranes indicates that the basolateral membrane urea permeability is fivefold lower than would be anticipated for its water permeability. These results indicate that the rectal gland maintains a selective barrier to urea in its basolateral membranes. (+info)Endothelin-1, superoxide and adeninediphosphate ribose cyclase in shark vascular smooth muscle. (6/31)
In vascular smooth muscle (VSM) of Squalus acanthias, endothelin-1 (ET-1) signals via the ET(B) receptor. In both shark and mammalian VSM, ET-1 induces a rise in cytosolic Ca(2+) concentration ([Ca(2+)](i)) via activation of the inositol trisphosphate (IP(3)) receptor (IP(3)R) and subsequent release of Ca(2+) from the sarcoplasmic reticulum (SR). IP(3)R-mediated release of SR Ca(2+) causes calcium-induced calcium release (CICR) via the ryanodine receptor (RyR), which can be sensitized by cyclic adeninediphosphate ribose (cADPR). cADPR is synthesized from NAD(+) by a membrane-bound bifunctional enzyme, ADPR cyclase. We have previously shown that the antagonists of the RyR, Ruthenium Red, high concentrations of ryanodine and 8-Br cADPR, diminish the [Ca(2+)](i) response to ET-1 in shark VSM. To investigate how ET-1 might influence the activity of the ADPR cyclase, we employed inhibitors of the cyclase. To explore the possibility that ET-1-induced production of superoxide (O(2)*-) might activate the cyclase, we used an inhibitor of NAD(P)H oxidase (NOX), DPI and a scavenger of O(2)*-, TEMPOL. Anterior mesenteric artery VSM was loaded with fura-2AM to measure [Ca(2+)](i). In Ca(2+)-free shark Ringers, ET-1 increased [Ca(2+)](i) by 104+/-8 nmol l(-1). The VSM ADPR cyclase inhibitors, nicotinamide and Zn(2+), diminished the response by 62% and 72%, respectively. Both DPI and TEMPOL reduced the response by 63%. The combination of the IP(3)R antagonists, 2-APB or TMB-8, with DPI or TEMPOL further reduced the response by 83%. We show for the first time that in shark VSM, inhibition of the ADPR cyclase reduces the [Ca(2+)](i) response to ET-1 and that superoxide may be involved in the activation of the cyclase. (+info)Interaction of FXYD10 (PLMS) with Na,K-ATPase from shark rectal glands. Close proximity of Cys74 of FXYD10 to Cys254 in the a domain of the alpha-subunit revealed by intermolecular thiol cross-linking. (7/31)
FXYD domain-containing proteins are tissue-specific regulators of the Na,K-ATPase that have been shown to have significant physiological implications. Information about the sites of interaction between some FXYD proteins and subunits of the Na,K-ATPase is beginning to emerge. We previously identified an FXYD protein in plasma membranes from shark rectal gland cells and demonstrated that this protein (FXYD10) modulates shark Na,K-ATPase activity. The present study was undertaken to identify the location of the C-terminal domain of FXYD10 on the alpha-subunit of Na,K-ATPase, using covalent cross-linking combined with proteolytic cleavage. Treatment of Na,K-ATPase-enriched membranes with the homobifunctional thiol cross-linker 1,4-bismaleimidyl-2,3-dihydroxybutane resulted in cross-linking of FXYD10 to the alpha-subunit. Cross-linking was not affected by preincubation with sodium or potassium but was significantly reduced after pre-incubation with the non-hydrolyzable ATP analog beta,gamma-methyleneadenosine 5'-triphosphate (AMP-PCP). A peptic assay was developed, in which pepsin treatment of Na,K-ATPase at low pH resulted in extensive cleavage of the alpha-subunit while FXYD10 was left intact. Proteolytic fragments of control and cross-linked preparations were isolated by immunoprecipitation and analyzed by gel electrophoresis. A proteolytic fragment containing FXYD10 cross-linked to a fragment from the alpha-subunit could be localized on SDS gels. Sequencing of this fragment showed the presence of FXYD10 as well as a fragment within the A domain of the alpha-subunit comprising 33 amino acids, including a single Cys residue, Cys254. Thus, regulation of Na,K-ATPase by FXYD10 occurs in part via cytoplasmic interaction of FXYD10 with the A domain of the shark alpha-subunit. (+info)Alkaline tide and nitrogen conservation after feeding in an elasmobranch (Squalus acanthias). (8/31)
We investigated the consequences of feeding for acid-base balance, nitrogen excretion, blood metabolites and osmoregulation in the Pacific spiny dogfish. Sharks that had been starved for 7 days were surgically fitted with indwelling stomach tubes for gastric feeding and blood catheters for repetitive blood sampling and were confined in chambers, allowing measurement of ammonia-N and urea-N fluxes. The experimental meal infused via the stomach tube consisted of flatfish muscle (2% of body mass) suspended in saline (4% of body mass total volume). Control animals received only saline (4% of body mass). Feeding resulted in a marked rise in both arterial and venous pH and HCO3- concentrations at 3-9 h after the meal, with attenuation by 17 h. Venous P(O2) also fell. As there were negligible changes in P(CO2), the response was interpreted as an alkaline tide without respiratory compensation, associated with elevated gastric acid secretion. Urea-N excretion, which comprised >90% of the total, was unaffected, while ammonia-N excretion was very slightly elevated, amounting to <3% of the total-N in the meal over 45 h. Plasma ammonia-N rose slightly. Plasma urea-N, TMAO-N and glucose concentrations remained unchanged, while free amino acid and beta-hydroxybutyrate levels exhibited modest declines. Plasma osmolality was persistently elevated after the meal relative to controls, partially explained by a significant rise in plasma Cl-. This marked post-prandial conservation of nitrogen is interpreted as reflecting the needs for urea synthesis for osmoregulation and protein growth in animals that are severely N-limited due to their sporadic and opportunistic feeding lifestyle in nature. (+info)'Squalus acanthias' is the scientific name for the species known as the spiny dogfish shark. While it is sometimes used in medical contexts, such as in research or when discussing potential zoonotic diseases, it is not a medical condition or disease itself. Therefore, there isn't a formal medical definition for 'Squalus acanthias'. However, I can provide some information about this species.
The spiny dogfish shark is a small shark species, with adults reaching an average length of 3 to 4 feet (about 1 meter). They are found in temperate and cold waters worldwide, including the Atlantic and Pacific Oceans. The 'acanthias' part of their scientific name refers to the presence of spines on their dorsal fins, which they can use to defend themselves against predators.
Spiny dogfish sharks play an essential role in marine ecosystems as both predators and prey. They feed on various fish species and invertebrates, while larger sharks, seals, and sea lions may prey upon them. The meat, skin, liver oil, and cartilage of spiny dogfish sharks have been used in human industries such as food, leather production, and dietary supplements. However, overfishing has led to population declines in some regions, making the species a subject of conservation concern.
A "dogfish" is a common name that refers to several species of small sharks. The term is not a formal medical or scientific term, but rather a colloquial one used to describe these marine animals. There are two main types of dogfish: the spiny dogfish (Squalus acanthias) and the smooth dogfish (Mustelus canis).
The spiny dogfish is characterized by two dorsal fins, the second of which is larger than the first and has a venomous spine. This species is found in both the Atlantic and Pacific Oceans and can grow up to about three feet in length. The smooth dogfish, on the other hand, lacks spines on its dorsal fins and is found primarily in warmer waters along the coasts of North and South America.
While not a medical term, it's worth noting that some species of dogfish are used in medical research and have contributed to our understanding of various physiological processes. For example, the electric organs of certain types of dogfish have been studied for their potential applications in nerve impulse transmission and muscle contraction.
I'm sorry for any confusion, but "sharks" are not a medical term. Sharks are a group of elasmobranch fish characterized by a cartilaginous skeleton, five to seven gill slits on the sides of the head, and pectoral and dorsal fins without spines.
If you have any medical questions or terms that you would like defined, I'd be happy to help!
A salt gland is a type of exocrine gland found in certain animals, including birds and reptiles, that helps regulate the balance of salt and water in their bodies. These glands are capable of excreting a highly concentrated solution of sodium chloride, or salt, which allows these animals to drink seawater and still maintain the proper osmotic balance in their tissues.
In birds, salt glands are typically located near the eyes and are responsible for producing tears that contain high levels of salt. These tears then drain into the nasal passages and are eventually expelled from the body. In reptiles, salt glands can be found in various locations, depending on the species, but they serve the same function of helping to regulate salt and water balance.
It's worth noting that mammals do not have salt glands and must rely on other mechanisms to regulate their salt and water balance, such as through the kidneys and the production of sweat.
"Squalus" is a genus of sharks, also known as the spiny dogfish. However, in a medical context, "squalus" is often used to refer to squalene, a polyunsaturated hydrocarbon that is found naturally in various animals and plants, including human sebum (the oily substance secreted by the skin's sebaceous glands). Squalene is a precursor to steroids and is used in some medical and cosmetic products. It is also being studied for its potential health benefits, such as its antioxidant properties.
Cadmium radioisotopes are unstable forms of the heavy metal cadmium that emit radiation as they decay into more stable elements. These isotopes can be created through various nuclear reactions, such as bombarding a cadmium atom with a high-energy particle. Some common cadmium radioisotopes include cadmium-109, cadmium-113, and cadmium-115.
These radioisotopes have a wide range of applications in medicine, particularly in diagnostic imaging and radiation therapy. For example, cadmium-109 is used as a gamma ray source for medical imaging, while cadmium-115 has been studied as a potential therapeutic agent for cancer treatment.
However, exposure to cadmium radioisotopes can also be hazardous to human health, as they can cause damage to tissues and organs through ionizing radiation. Therefore, handling and disposal of these materials must be done with care and in accordance with established safety protocols.
Dihydroorotate oxidase is a mitochondrial enzyme that plays a crucial role in the de novo biosynthesis of pyrimidines, which are essential nucleotides required for the synthesis of DNA, RNA, and other vital molecules in the body.
The enzyme catalyzes the oxidation of dihydroorotate to orotate, using molecular oxygen as an electron acceptor. This reaction is the third step in the pyrimidine biosynthesis pathway, following the condensation of carbamoyl phosphate and aspartate to form carbamoylaspartate, and the decarboxylation of carbamoylaspartate to form dihydroorotate.
Dihydroorotate oxidase is a flavoprotein that contains a FAD cofactor, which accepts electrons from dihydroorotate and transfers them to molecular oxygen, generating hydrogen peroxide as a byproduct. The enzyme is inhibited by the drug leflunomide, which is used in the treatment of rheumatoid arthritis and other autoimmune diseases.
In humans, dihydroorotate oxidase is encoded by two genes, DHODH and SUOX, which are located on different chromosomes. Mutations in these genes can lead to deficiencies in pyrimidine biosynthesis and result in various genetic disorders, such as Miller syndrome, a rare autosomal recessive disorder characterized by craniofacial abnormalities, limb defects, and hearing loss.
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.
Melanocyte-stimulating hormones (MSH) are a group of peptide hormones that originate from the precursor protein proopiomelanocortin (POMC). They play crucial roles in various physiological processes, including pigmentation, energy balance, and appetite regulation.
There are several types of MSH, but the most well-known ones include α-MSH, β-MSH, and γ-MSH. These hormones bind to melanocortin receptors (MCRs), which are found in various tissues throughout the body. The binding of MSH to MCRs triggers a series of intracellular signaling events that ultimately lead to changes in cell behavior.
In the context of skin physiology, α-MSH and β-MSH bind to melanocortin 1 receptor (MC1R) on melanocytes, which are the cells responsible for producing pigment (melanin). This binding stimulates the production and release of eumelanin, a type of melanin that is brown or black in color. As a result, increased levels of MSH can lead to darkening of the skin, also known as hyperpigmentation.
Apart from their role in pigmentation, MSH hormones have been implicated in several other physiological processes. For instance, α-MSH has been shown to suppress appetite and promote weight loss by binding to melanocortin 4 receptor (MC4R) in the hypothalamus, a region of the brain that regulates energy balance. Additionally, MSH hormones have been implicated in inflammation, immune response, and sexual function.
Overall, melanocyte-stimulating hormones are a diverse group of peptide hormones that play important roles in various physiological processes, including pigmentation, energy balance, and appetite regulation.
Acid-base equilibrium refers to the balance between the concentration of acids and bases in a solution, which determines its pH level. In a healthy human body, maintaining acid-base equilibrium is crucial for proper cellular function and homeostasis.
The balance is maintained by several buffering systems in the body, including the bicarbonate buffer system, which helps to regulate the pH of blood. This system involves the reaction between carbonic acid (a weak acid) and bicarbonate ions (a base) to form water and carbon dioxide.
The balance between acids and bases is carefully regulated by the body's respiratory and renal systems. The lungs control the elimination of carbon dioxide, a weak acid, through exhalation, while the kidneys regulate the excretion of hydrogen ions and the reabsorption of bicarbonate ions.
When the balance between acids and bases is disrupted, it can lead to acid-base disorders such as acidosis (excessive acidity) or alkalosis (excessive basicity). These conditions can have serious consequences on various organ systems if left untreated.
Water-electrolyte balance refers to the regulation of water and electrolytes (sodium, potassium, chloride, bicarbonate) in the body to maintain homeostasis. This is crucial for various bodily functions such as nerve impulse transmission, muscle contraction, fluid balance, and pH regulation. The body maintains this balance through mechanisms that control water intake, excretion, and electrolyte concentration in various body fluids like blood and extracellular fluid. Disruptions in water-electrolyte balance can lead to dehydration or overhydration, and imbalances in electrolytes can cause conditions such as hyponatremia (low sodium levels) or hyperkalemia (high potassium levels).
Urea is not a medical condition but it is a medically relevant substance. Here's the definition:
Urea is a colorless, odorless solid that is the primary nitrogen-containing compound in the urine of mammals. It is a normal metabolic end product that is excreted by the kidneys and is also used as a fertilizer and in various industrial applications. Chemically, urea is a carbamide, consisting of two amino groups (NH2) joined by a carbon atom and having a hydrogen atom and a hydroxyl group (OH) attached to the carbon atom. Urea is produced in the liver as an end product of protein metabolism and is then eliminated from the body by the kidneys through urination. Abnormal levels of urea in the blood, known as uremia, can indicate impaired kidney function or other medical conditions.
Sodium-Potassium-Exchanging ATPase (also known as Na+/K+ ATPase) is a type of active transporter found in the cell membrane of many types of cells. It plays a crucial role in maintaining the electrochemical gradient and membrane potential of animal cells by pumping sodium ions (Na+) out of the cell and potassium ions (K+) into the cell, using energy derived from ATP hydrolysis.
This transporter is composed of two main subunits: a catalytic α-subunit that contains the binding sites for Na+, K+, and ATP, and a regulatory β-subunit that helps in the proper targeting and functioning of the pump. The Na+/K+ ATPase plays a critical role in various physiological processes, including nerve impulse transmission, muscle contraction, and kidney function.
In summary, Sodium-Potassium-Exchanging ATPase is an essential membrane protein that uses energy from ATP to transport sodium and potassium ions across the cell membrane, thereby maintaining ionic gradients and membrane potentials necessary for normal cellular function.
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