Comparative studies of sodium transport and its relation to hydrostatic pressure in deep and shallow water gammarid crustaceans from Lake Baikal

• 1.1. Freshwater gammarids from 900–1400 m depths lose Na at 1 atm, 4°C, while related shallow water gammarids are near neutral Na balance.
• 2.2. Na⁺ influx rates are similar at 1 atm, 4°C, for abyssal and shallow water gammarids of similar weight.
• 3.3. Na⁺ efflux is faster for abyssal gammarids than for comparable shallow water gammarids.
• 4.4. Compressing abyssal gammarids to 90–140 atm increases Na⁺ influx rates enough to restore neutral Na balance, while in shallow water crustaceans, compression decreases Na⁺ influx.
• 5.5. Na⁺ influx rates in Baikalian gammarids vary with the 0.55 power of weight.
• 6.6. The equation F_{ma × t} = 1.3 × W^0.55 μEq/hr/animal applies to freshwater crustaceans over the weight range from 0.03 to 35 g.

     

Sodium transport in red blood cells of lamprey LAmpetra fluviatilis

• 1.1. Unidirectional Na⁺ influx in lamprey red blood cells was determined using ²²Na as a tracer.
• 2.2. Total Na⁺ uptake and amiloride-inhibitable Na⁺ influx increased in a saturable fashion as a function of external Na⁺ concentration (Na_e).
• 3.3. At 141 mM Na_e, the average value of net Na⁺ influx was 13 ± 1.1 and the amiloride-sensitive Na⁺ influx was 5.3±1.1 mmol/l cells per hr (±SE).
• 4.4. The amiloride-sensitive component of Na⁺ influx was significantly activated by 10⁻⁵ M isoproterenol, by 2 × 10⁻⁵ M DNP, and by cell shrinkage.
• 5.5. Furosemide (1 mM) had no effect on the Na⁺ transport in red cells.
• 6.6. The residual amiloride-insensitive component of Na⁺ transport was a linear function of Na_e in the range of 5–141 mM. This transport seems to be accounted for by simple diffusion.

     

Intestinal l-methionine transport in the cultured gilthead bream (Sparus aurata)

• 1.1. The influx and transepithelial movements of l-methionine and its effects on the electrophysiology and Na-Cl-transport in upper and lower intestine of the cultured fish, Spanis aurata, were measured.
• 2.2. The K_m and V_max of l-methionine influx into the tissues were higher in lower intestine than in upper intestine. A prominent diffusion-like transport component was also measured in both segments during influx experiments.
• 3.3. Net transepithelial fluxes of l-methionine (1 mM) were observed in both upper and lower intestine, this transport being Na⁺-dependent.
• 4.4. The two intestinal segments exhibited an electrical potential difference (PD) and a short circuit current (I_sc) serosa negative or near zero. Tissue conductance (G_t) was higher in posterior than in lower intestine.
• 5.5. Addition of l-methionine to the mucosal side of lower or upper intestine did not induce changes in PD in either part.
• 6.6. Isotopic fluxes of Cl⁻ or Na⁺ measurements under short circuit conditions showed that there were no net Cl⁻ or Na⁺ transport in either part.
• 7.7. l-Methionine additions to the mucosa did not induce changes in unidirectional fluxes of Cl⁻ or Na⁺ or in the (I_sc) in either the anterior or posterior intestine.

     

Vanadium inhibition of human parietal lobe ATPases

In vitro influence of vanadate and vanadyl ions on the activities of Na,K- and Ca,Mg-ATPase from synaptosomal membranes of the parietal lobe of the human brain were compared.

• 1.1. Vanadate and vanadyl inhibit the enzymes activities in the investigated fraction.
• 2.2. Vanadate is a more effective inhibitor of both ATPases in the concentrations above 50 μM and vanadyl is an effective inhibitor in a very low concentration (10 nM).
• 3.3. Vanadate seems to be an uncompetitive inhibitor of Na,K-ATPase (k₁ = 880 nM).

     

Modulation of active potassium transport by aldosterone

• 1.1. The role of aldosterone on active potassium transport across lizard colon under voltage-clamped conditions has been investigated.
• 2.2. Control colons exhibited no net potassium flux (J^k_net) despite of the existence of active opposite unidi ectional fluxes.
• 3.3. An important net secretory potassium flux was found in short-circuited aldosterone-stimulated colons.
• 4.4. Mucosal amiloride did not change (J^k_net) either in control or aldosterone-stimulated colons.
• 5.5. Luminal barium alters K ⁺ transport in a manner consistent with the presence of barium-sensitive conductances at the apical membrane of both control and aldosterone-treated colons.
• 6.6. The effects of ouabain and barium on control and aldosterone-induced potassium flows were consistent with a model involving basolateral uptake by an Na ⁺-K ⁺-ATPase and conductive exit across the apical membrane.
• 7.7. The stimulatory effect of aldosterone on potassium secretion is associated with parallel increases of both basolateral K ⁺ entry and the apical conductive pathway.

     

A role for skin in Ca metabolism of frogs?

• 1.1. In the leopard frog, Rana pipiens, in vivo Ca loss occurs in similar amounts across the skin and the urine. No change was detected in Ca loss when frogs were injected with either calcitonin or parathyroid hormone. Large doses of 1,25-(OH)₂vitamin D₃ increased urinary Ca loss.
• 2.2. ⁴⁵Ca accumulation across the skin in vivo each day is equivalent to 0.04% of total body Ca or 14% of the total Ca in the extracellular fluids. This accumulation was enhanced by prior adaptation of the frogs to a low Ca pond water.
• 3.3. Unidirectional influx (from 0.2 mM Ca on pond side) was remarkably similar in vitro: 0.56 and in vivo: 0.65 nmol cm⁻² h⁻¹. Based on in vitro measurements, an active transport process does not appear to be involved in this transcutaneous Ca movement.
• 4.4. Substantial deposits of Ca equivalent to five times the total in other “soft” tissues and eleven times that in the total extracellular fluids are found in R. pipiens skin.
• 5.5. Although cutaneous Ca does “turnover” slowly as shown by exchange with external ⁴⁵Ca. the skin Ca concentration does not change with the environmental Ca concentration.
• 6.6. Possible role(s) of cutaneous Ca in frogs' overall Ca metabolism are discussed.

     

Ostrich fructose-1,6-bisphosphatase: Kinetic characterization of the liver isoenzyme

• 1.1. Purified ostrich (Struthio camelus) liver fructose-1,6-bisphosphatase exhibited an absolute requirement for Mg²⁺.
• 2.2. The enzyme catalyzed the hydrolysis of fructose-1,6-bisphosphate, sedoheptulose-l,7-bisphosphate and ribulose-l,5-bisphosphate.
• 3.3. S_0.5 for substrate was 1.4 μM.
• 4.4. AMP was a potent non-competitive inhibitor with respect to substrate (K_i of 25 μM).
• 5.5. Fructose-2,6-bisphosphate was a potent competitive inhibitor of the enzyme (K_i of 4.8 μM).

     

Evidence for hyporegulation in the calanoid copepod,Acartia tonsa

• 1.1. The euryaline calanoid copepod, Acartia tonsa, maintains haemolymph Na below that of the external medium in salinities above 34^o_oo (475 mM Na).
• 2.2. The measured transepithelial electrical potential. −9.97 ± 1.0 mV, indicates that Na is regulated out of electrochemical equilibrium.
• 3.3. Water osmotically lost in hyporegulation is replaced by Na-dependent absorption by the gut.
• 4.4. High osmotic water permeability is evidenced by the fact that with an increase in external salinity from 475 mM Na to 580 mM Na the copepod's drinking rate nearly doubles.
• 5.5. Sodium efflux measurements indicate that ionic permeability is much lower than other hyporegulating crustaceans.
• 6.6. The energetic advantage of hyporegulation in this species is considered.

     

Reabsorption and accumulation of α-amino-iso-butyric acid in the nephridia of Sabella pavonina Sa vigny (Annelida polychaeta)

• 1.l. High amino acid concentrations were found in the anterior coelomic fluid of a Polychaeta (Sabella pavonina Savigny).
• 2.2. The concentrations being much higher in the fluid which penetrates the nephrostomia into the nephridia lumen than in the final urine indicates that the nephridia reabsorbs large amounts of amino acids.
• 3.3. Nephridial perfusion experiments showed that an amino acid analogue (α-amino-iso-butyric acid, AIB) is transported by the nephidia.
• 4.4. The transport took place across the nephridial wall owing to the presence of a carrier-mediated transport system and a diffusion system.
• 5.5. For the carrier-mediated transport, the V_max was 0.234 ± 0.025 nmol·min⁻ and the K_m 3.715 ± 0.315mmol·l⁻.
• 6.6. AIB accumulated in the nephridial cells up to a maximum rate of 01.17 nmol·min⁻.
• 7.7. Intracellular accumulation stopped increasing when the V_max for reabsorption was reached.
• 8.8. These results indicate that the carrier-mediated transport of AIB is located at the apical membrane of the nephridial cell, and that AIB transport by simple diffusion takes place through the paracellular pathway.

     

A novel inhibitor of glycogen phosphorylase from crayfish hepatopancreas

• 1.1. A novel glycogen phosphorylase inhibitor was partially purified from crayfish hepatopancreas.
• 2.2. The inhibitor was found only in two species of crayfish examined, and not in lobster, fresh and salt water clams, mussels or cockroaches.
• 3.3. The inhibitor is a small protein (M_r = 23,000) which did not show proteolytic activity.
• 4.4. Preliminary kinetic analysis of the inhibitory mechanism indicated that it bound to both glycogen and the glycogen phosphorylase protein.
• 5.5. Inhibitor binding to glycogen resulted in a competitive inhibition pattern with respect to glycogen phosphorylase (inhibition constant of ca 10 μg/ml).
• 6.6. The inhibitor also bound glycogen phosphorylase directly with a binding coefficient of 100 μg/ml resulting in a partially non-competitive inhibition pattern with respect to phosphate.

     

Evidence of an egg-laying factor in the prostatic secretions of Helix aspersa müller

• 1.1. A high percentage (53%) of isolated snails injected with prostate gland homogenates lay eggs.
• 2.2. These egg masses consist of a few eggs which contain many nonviable oocytes.
• 3.3. Preliminary experiments suggest that an egg-laying factor may be present in prostatic secretions.
• 4.4. Snails bred in isolation from hatching, whether injected or not, occasionally lay viable eggs.
• 5.5. This observation shows that self-fertilization or parthenogenesis is, in fact, possible in Helix aspersa Müller.

     

Seasonal changes of water,electrolytes and aldosterone levels in blood serum,brain and kidney of the Egyptian cobra “Naja haje haje”

 

• 1.The levels of water, Na, K, Ca and Mg in blood serum, brain and kidney and aldosterone level in blood of Naja haje haje were studied during the different phases of the annual cycle.
• 2.The water content in the tissues studied displayed only minor changes as the animals passed from one phase to the other.
• 3.A significant increase in Na was recorded in the brain during the different phases indicating a depressed sodium pump, whereas the blood Na level showed a significant decrease during hibernation.
• 4.K increased in blood serum, brain and kidney during hibernation, while a nonsignificant decrease was found in blood serum during arousal. The brain may act as a potassium reservoir.
• 5.An increase in Ca and Mg concentration was recorded in blood serum, brain and kidney during prehibernation and hibernation. The data suggested a homeostatic function in the transport and metabolism of these cations.
• 6.Aldosterone exhibited a highly significant decrease especially during hibernation. The aldosterone regulation of ionic composition is discussed.
• 7.Na/K and Ca/Mg ratios in the brain may explain the decreased excitability during winter torpor.

     

Ion transport in crab gills: A new method using isolated half platelets of Eriocheir gills in an ussing-type chamber

• 1.1. A half platelet preparation from Chinese crab (Eriocheir sinensis) gill is described which allows electrophysiological investigations of ion transport by gill epithelial monolayer when mounted in a modified Ussing chamber.
• 2.2. The resistance of these preparations equals half that of complete gill platelets (containing the gill epithelium and cuticle twice) indicating that cell damage during preparation of half platelets is negligible.
• 3.3. The transepithelial resistance (resistance of cuticle subtracted previously) was determined to be about 140 Ω cm² when both sides are bathed with identical salines.
• 4.4. Similarities to the results obtained with perfused complete gills demonstrates the reliability of this preparation.
• 5.5. When identical salines are applied on both sides of the epithelium an outside positive transepithelial potential difference (PD_te) up to 40 mV was measured.
• 6.6. The occurrence of such a high PD_te under symmetric conditions and its sensitivity to CN⁻ suggests the PD_te to be generated by active transport processes.

     

2-Deoxyglucose transport by the frog sartorius: Effects of electrical stimulation and N-carbobenzoxy-glycyl-l-phenylalaninamide

• 1.1. Studies characterizing glucose transport in the frog sartorius were performed.
• 2.2. For nonstimulated and stimulated muscles, intracellular 2-deoxyglucose exceeded 2-deoxyglucose-6-phosphate at 15 min, showed little further increase, and was maintained below the extracellular concentration for 2 hr.
• 3.3. Accumulated 2-deoxyglucose-6-phosphate did not inhibit glucose transport.
• 4.4. Unlike in adipocytes, basal and stimulated 2-deoxyglucose transport showed no difference in sensitivity to N-carbobenzoxy-glycyl-l-phenylalaninamide.
• 5.5. Phenylarsine oxide blocked contraction-enhanced 2-deoxyglucose uptake.
• 6.6. These results suggest that the glucose transporter of the sartorius exhibits auto-regulation, and that basal transport is not regulated by the same process as in adipocytes.

     

Effect of aminooxyacetate and α-ketoglutarate on glutamate deamination by rat kidney mitochondria

• 1.1. Glutamate dehydrogenase flux by rat kidney mitochondria incubated with 1 mM glutamine plus 2–3 mM glutamate was stimulated by aminooxyacetate. This effect was inhibited by α-ketoglutarate.
• 2.2. Studies with intact mitochondria and mitochondrial sonicates revealed a linear inverse relationship between glutamate deamination and α-ketoglutarate levels.
• 3.3. The data revealed that α-ketoglutarate is a competitive inhibitor of glutamate dehydrogenase with an apparent K_i of 0.6mM.
• 4.4. The data suggest that aminooxyacetate stimulates glutamate deamination by a mechanism mediated by α-ketoglutarate.

     

Purification and properties of tetralysine endopeptidase from Escherichia coli AJ005

• 1.1. A new tetralysine endopeptidase from Escherichia coli AJ005 has been purified about 135-fold.
• 2.2. The peptidase seems to be specific to tetralysine among lysine homopolymers.
• 3.3. The optimal pH was about 7.5
• 4.4. The activity was inhibited by KCN but not inhibited by soybean trypsin inhibitor.
• 5.5. The apparent K_m value was 2.5 × 1O⁻³ M for tetralysine.

     

δ-Aminolevulinic acid transport in Saccharomyces cerevisiae

• 1.1. This work represents the first approach to characterize the transport system of haem pathway precursors, such as δ-aminolevulinic acid (ALA), in two strains of Saccharomyces cerevisiae, a wild type, D27, and a HEM R⁺ mutant.
• 2.2. ALA transport occurs unidirectionally by a sole active system with an apparent K_M of 0.10 mM, at the optimum pH of 5.0. ALA uptake is influenced by both the carbon and nitrogen source; this suggests a rather complex regulation mechanism.
• 3.3. This transport is not mediated by the general amino acid permease (GAP).
• 4.4. ALA uptake is strongly inhibited by compounds harboring a methyl-amine terminus suggesting that this group is essential for ALA transport; however, the electric environment of the carboxylic group may be also important for the interaction between ALA and its transporter active site.
• 5.5. We have found differences in ALA transport which would indicate a different regulation mechanism for this system in both strain cells.

     

Kinetic study of the inhibition of rat liver ornithine decarboxylase by diamines; considerations on the mechanism of interaction between enzyme and inhibitor

• 1.1. Partially purified rat liver ornithine decarboxylase is inhibited by several diamines including putrescine, 1,3-diaminopropane, cadaverine and p-phenylenediamine.
• 2.2. The inhibition is dependent on pH, being strong at pH above 8 and negligible below pH 6.5.
• 3.3. The kinetic study of the inhibition showed that while the aromatic diamine behaved as a simple competitive inhibitor, the aliphatic diamines presented a more complex pattern of inhibition in which two molecules of inhibitor might bind to the enzyme active site.
• 4.4. The K_I values for the different inhibitors were calculated and the degree of affinity for the enzyme was p-phenylenediamine > putrescine > cadaverine > 1,3-diaminopropane.
• 5.5. A molecular mechanism explaining how one or two molecules of inhibitor can bind to the enzyme is proposed.

     

Purification and characterization of the endonuclease present in Physalia physalis venom

• 1.1. Physalia physalis nematocyst venom contains a DNase which has a non-specific endonucleolytic action.
• 2.2. This enzyme has an approximate molecular weight of 75,000 daltons.
• 3.3. The enzyme can cleave DNA over a wide pH range with an optimum near neutrality.
• 4.4. The enzyme is thermolabile and its activity can be stimulated by 80 nM NaCl or 10 mM MgCl₂.

     

Sodium balance in adult atlantic salmon (Salmo salar L.) during migration into neutral and acid fresh water

• 1.1. In sea-water, adult salmon (S. salar) exchange an average of 12.6% of total body sodium/hr.
• 2.2. Following transfer to fresh water sodium uptake follows Michaelis-Menton kinetics. F_max = 2.40 mmol Na/1 ECF/hr, K_m = 0.26 mmol Na/1. The uptake system is fully activated immediately following transfer to fresh water.
• 3.3. Post smolts adapted to sea-water for 3 months take up sodium at only one third of the rate of adult fish following return to fresh water.
• 4.4. The concentration of prolactin in the plasma is low in sea-water adapted fish and does not rise during the first 8 hr in fresh water.
• 5.5. At pH 5 sodium uptake is reduced by almost 90%, even in the absence of aluminium, but recovers immediately on return to neutral water.
• 6.6. At pH 5 and 20 μmol Al/1 there is little further effect on sodium uptake but after 6 hr in aluminium the inhibition of sodium uptake continues after return to neutral aluminium fresh water and uptake is only 50% of normal 24 hr later.