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Query: UMLS:C0432222 (SEM)
 47,337 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Calcium uptake produced by a potassium contracture in isolated frog twitch fibers was 6.7 +/- 0.8 pmol in 0.7 cm of fiber (mean +/- SEM, 21 observations) in the presence of 30 microM D600. When potassium was applied to fibers paralyzed by the combination of 30 microM D600, cold, and a prior contracture, the calcium uptake fell to 3.0 +/- 0.7 pmol (11): the fibers were soaked in 45Ca in sodium Ringer for 3 min before 45Ca, in a potassium solution, was added for 2 min; each estimate of uptake was corrected for 5 min of resting influx, measured from the same fiber (average = 2.3 +/- 0.3 pmol). The calcium influx into paralyzed fibers is unrelated to contraction. This voltage-sensitive, slowly inactivating influx, which can be blocked by 4 mM nickel, has properties similar to the calcium current described by several laboratories. The paired difference in calcium uptake between contracting and paralyzed fibers, 2.9 +/- 0.8 pmol (16), is a component of influx related to contraction. Its size varies with contracture size and it occurs after tension production: 45Ca applied immediately after contracture is taken up in essentially the same amounts as 45Ca added before contraction. This delayed uptake is probably a "reflux" refilling a binding site on the cytoplasmic side of the T membrane, which had been emptied during the prior contracture, perhaps to initiate it. We detect no component of calcium uptake related to excitation-contraction coupling occurring before or during a contracture.
J Gen Physiol 1985 Mar
PMID:Calcium influx in contracting and paralyzed frog twitch muscle fibers. 387 27

This paper reports experiments designed to find the concentrations of internal and external Na and K at which inward and outward furosemide-sensitive (FS) Na and K fluxes are equal, so that there is no net FS movement of Na and K. The red cell cation content was modified by using the ionophore nystatin, varying cell Na (Nai) from 0 to 34 mM (K substitution, high-K cells) and cell K (Ki) from 0 to 30 mM (Na substitution, high-Na cells). All incubation media contained NaCl (Nao = 130 or 120 nM), and KCl (Ko = 0-30 mM). In high-K cells, incubated in the absence of Ko, there was net extrusion of Na through the FS pathway. The net FS Na extrusion increased when Nai was increased. Low concentrations of Ko (0-6 mM) slightly stimulated, whereas higher concentrations of Ko inhibited, FS Na efflux. Increasing Ko stimulated the FS Na influx (K0.5 = 4 mM). Under conditions similar to those that occur in vivo (Nai = 10, Ki = 130, Nao = 130, Ko = 4 mM, Cli/Clo = 0.7), net extrusion of Na occurs through the FS pathway (180-250 mumol/liter cell X h). The concentration of Ko at which the FS Na influx and efflux and the FS K influx and efflux become equal increased when Nai increased in high-K cells and when Ki was increased in high-Na cells. The net FS Na and K fluxes both approached zero at similar internal and external Na and K concentrations. In high-K cells, under conditions when net Na and K fluxes were near zero, the ratio of FS Na to FS K unidirectional flux was found to be 2:3. In high-K cells, the empirical expression (Nai/Nao)2(Ki/Ko)3 remained at constant value (apparent equilibrium constant, Kappeq +/- SEM = 22 +/- 2) for each set of internal and external cation concentrations at which there was no net Na flux. These results indicate that in the physiological region of concentrations of internal and external Na, K, and Cl, the stoichiometry of the FS Na and K fluxes is 2 Na:3 K. In high-Na cells under conditions when net FS Na and K fluxes were near zero, the ratio of FS Na to FS K unidirectional fluxes was 3:2 (1).(ABSTRACT TRUNCATED AT 400 WORDS)
J Gen Physiol 1986 Jan
PMID:Furosemide-sensitive Na and K fluxes in human red cells. Net uphill Na extrusion and equilibrium properties. 395 May 77

The degree of tyrosine sulfation and the distribution between gastrin-17- and gastrin-34-like immunoreactivity (LI) were studied in the antra of ten mammalian species. Specific radioimmunoassays, gel-, and ion-exchange chromatography as well as enzymatic cleavage with trypsin and arylsulfatase were used. The percentage of sulfation varied from 24.4 +/- 4.2 (mean +/- SEM) in dogs to 80.1 +/- 2.6 in sheep, 46.8 +/- 3.3 in humans, 50.1 +/- 3.2 in cows, 55.9 +/- 2.3 in rats, 57.4 +/- 3.1 in pigs, 61.3 +/- 2.2 in guinea pigs, 64.1 +/- 4.7 in cats, 64.8 +/- 2.1 in mice and 68.2 +/- 2.8 in rabbits. Gastrin-34-LI in antral extracts could be converted to gastrin-17-LI by trypsin in all species. Five percent of antral gastrins eluted as gastrin-34-LI in all species. We conclude that while the ratio of gastrin-34-LI to gastrin-17-LI varies little in mammals, large differences occur in the degree of sulfation.
Gen Comp Endocrinol 1985 Apr
PMID:Species variation in the tyrosine sulfation of mammalian gastrins. 398 36

This paper describes experiments designed to evaluate Na(+) and Cl(-) transport in isolated proximal straight tubules from rabbit kidneys. When the perfusing solution was Krebs-Ringer buffer with 25 mM HCO(3) (-) (KRB) and the bath contained KRB plus 6% albumin, net volume reabsorption (J(v), nl min(-1) mm(-1) was -0.46 +/- 0.03 (SEM); V(e), the spontaneous transepithelial potential difference, was -1.13 +/- 0.05 mV, lumen negative. Both J(v), and V(e), were reduced to zero at 21 degrees C or with 10(-4) M ouabain, but J(v), was not HCO(3) (-) dependent. Net Na(+) reabsorption, measured as the difference between (22)Na(+) fluxes, lumen to bath and bath to lumen, accounted quantitatively for volume reabsorption, assuming the latter to be an isotonic process, and was in agreement with the difference between lumen to bath (22)Na(+) fluxes during volume reabsorption and at zero volume flow. The observed flux ratio for Na(+) was 1.46, and that predicted for a passive process was 0.99; thus, Na(+) reabsorption was rationalized in terms of an active transport process. The Cl(-) concentration of tubular fluid rose from 113.6 to 132.3 mM during volume reabsorption. Since V(e), rose to +0.82 mV when tubules were perfused with 138.6 mM Cl(-) solutions, V(e) may become positive when tubular fluid Cl(-) concentrations rise during volume reabsorption. The permeability coefficients P(Na) and P(Cl) computed from tracer fluxes were, respectively, 0.23 x 10(-4) and 0.73 x 10(-4) cm s(-1). A P(Na)/P(Cl) ratio of 0.3 described NaCl dilution potentials at zero volume flow. The magnitudes of the potentials were the same for a given NaCl gradient in either direction and P(Na)/P(Cl) was constant in the range 32-139 mM NaCl. We infer that the route of passive ion permeation was through symmetrical extracellular interfaces, presumably tight junctions, characterized by neutral polar sites in which electroneutrality is maintained by mobile counterions.
J Gen Physiol 1974 Nov
PMID:Volume reabsorption, transepithelial potential differences, and ionic permeability properties in mammalian superficial proximal straight tubules. 444 93

The present experiments were designed to evaluate the effects of varying the osmolality of luminal solutions on the antidiuretic hormone (ADH)-independent water and solute permeability properties of isolated rabbit cortical collecting tubules. In the absence of ADH, the osmotic water permeability coefficient (cm s(-1)) P(f) (l-->b), computed from volume flows from hypotonic lumen to isotonic bath, was 20 +/- 4 x 10(-4) (SEM); the value of P(f) (b-->l) in the absence of ADH, computed from volume flows from isotonic bath to hypertonic lumen, was 88 +/- 15 x 10(-4) cm s(-1). We also measured apparent urea permeability coefficients (cm s(-1)) from (14)C-urea fluxes from lumen to bath (P(DDurea) (l-->b)) and from bath to lumen (P(DDurea) (b-->l)). For hypotonic luminal solutions and isotonic bathing solutions, P(DDurea) (l-->b) was 0.045 +/- 0.004 x 10(-4) and was unaffected by ADH. The ADH-independent values of P(DDurea) (l-->b) and P(urea) (b-->l) were, respectively, 0.216 +/- 0.022 x 10(-4) cm s(-1) and 0.033 +/- 0.002 x 10(-4) cm s(-1) for isotonic bathing solutions and luminal solutions made hypertonic with urea, i.e., there was an absolute increase in urea permeability and asymmetry of urea fluxes. Significantly, P(DDurea) (l-->b) did not rise when luminal hypertonicity was produced by sucrose; and, bathing fluid hypertonicity did not alter tubular permeability to water or to urea. We interpret these data to indicate that luminal hypertonicity increased the leakiness of tight junctions to water and urea but not sucrose. Since the value of P(f) (b-->l) in the absence of ADH, when tight junctions were open to urea, was approximately half of the value of P(f) (l-->b) in the presence of ADH, when tight junctions were closed to urea, we conclude that tight junctions are negligible paracellular shunts for lumen to bath osmosis with ADH. These findings, together with those in the preceding paper, are discussed in terms of a solubility-diffusion model for water permeation in which ADH increases water solubility in luminal plasma membranes.
J Gen Physiol 1974 Aug
PMID:Osmosis in cortical collecting tubules. ADH-independent osmotic flow rectification. 484 68

A fall in extracellular pH increased membrane conductance of the giant cell in the abdominal ganglion of Aplysia californica. Chloride conductance was trebled whereas potassium conductance was increased by 50%. Half the giant cells were hyperpolarized (2-8 mv) and half were depolarized (3-10 mv) by lowering the pH. The hyperpolarizing response always became a depolarizing response in half-chloride solutions. When internal chloride was increased electrophoretically, the hyperpolarization was either decreased or changed to depolarization. The depolarizing response was reduced or became a hyperpolarizing response after soaking the cell in 10.0 mM chloride, artificial seawater solution for 1 hr. Depolarization was unaffected when either external sodium, calcium, or magnesium was omitted. A glass micropipette having an organic liquid chloride ion exchanger in its tip was used to measure intracellular chloride activity in 14 giant cells; 7 had values of 27.7 +/- 1.8 mM (SEM) and 7 others 40.7 +/- 1.5 mM. Three of the first group were hyperpolarized when pH was lowered and three of the second group were depolarized. In all six cells, these changes of membrane potential were in the direction of the chloride equilibrium potential. Intracellular potassium activity was measured by means of a potassium ion exchanger microelectrode.
J Gen Physiol 1970 Nov
PMID:Increased chloride conductance as the proximate cause of hydrogen ion concentration effects in Aplysia neurons. 547 96

The penetration of (14)C-labeled erythritol, mannitol, and sucrose through the axolemma was determined in medium sized paired axons, one at rest and the other stimulated 25 times per sec. The resting permeabilities, in 10(-7) cm/sec, are erythritol, 2.9 +/- 0.3 (mean +/- SEM); mannitol, 2.3 +/- 0.4; and sucrose 0.9 +/- 0.1. In the stimulated axons they are: erythritol, 5.2 +/- 0.3; mannitol, 4.0 +/- 0.5; and sucrose, 1.8 +/- 0.3. Thus, the calculated permeabilities during activity (1 msec per impulse), in the same units, are: 100, 75, and 38, respectively. These changes in permeability are reversible. The effects of external potassium and sodium concentrations on erythritol penetration were also studied. At rest, erythritol penetration is independent of potassium and sodium concentrations. In the stimulated axons, erythritol penetration decreases when the extracellular sodium is diminished. Sodium influx (not the efflux) decreases during rest and activity when the extracellular sodium is diminished. The diminution during activity of erythritol and sodium entries in low sodium solutions may be related to a decrease of a drag effect of sodium ions on the nonelectrolyte molecules or to independent effects of the sodium concentration on sodium influx and the nonelectrolyte pathways. The axolemma discriminates among erythritol, mannitol, sucrose, and the different ionic species during rest and activity.
J Gen Physiol 1966 Sep
PMID:Nonelectrolyte penetration and sodium fluxes through the axolemma of resting and stimulated medium sized axons of the squid Doryteuthis plei. 597 Oct 32

When retinal sections were isolated from dark-adapted bullfrogs and placed in normal ringer's solution, they contained 40.7 +/- 0.2 pmol cGMP/mg protein (mean +/- SEM, 30 samples). When isolated, dark-adapted retinal sections were removed from normal ringer's solution and placed in calcium-deficient ringer's solution with 3 mM EGTA, there was about a threefold rise in cyclic GMP (cGMP) levels by 1.5 min and about a 10-fold rise by 5 min. The cGMP level remained high with no detectable decrease for at least 40 min (the longest time measured). When isolated, dark- adapted retinal sections were removed from normal ringer's solution and placed in ringer's solution which contained high- calcium (20 mM CaCl(2)), there was a slow but significant decrease in cGMP levels. After 20 min in high-calcium ringer's solution the cGMP level was 0.58 +/- 0.07 (mean +/- SEM, eight samples) of the cGMP level in normal ringer's solution incubated for the same time. The rate at which 10-fold elevated cGMP levels in low calcium decreased upon illumination was examined using quick-freezing techniques on the retinal sections. The elevated cGMP level in retinal sections incubated in low-calcium decreased upon illumination was examined using quick-freezing techniques on the retinal sections. The elevated cGMP level in retinal sections incubated in low-calcium ringer's solution was found to decay about 15-fold faster than cGMP levels in retinal sections incubated in normal ringer's solution. The CGMP level in low calcium was significantly different (P=0.005) after 1 s illumination, whereas the cGMP level in normal calcium was not significantly different.
J Gen Physiol 1980 Apr
PMID:Calcium effects on frog retinal cyclic guanosine 3', 5'-monophosphate levels and their light-initiated rate of decay. 624 21

Temperature-sensitive (ts) mutants of the rhabdoviruses vesicular stomatitis virus and Chandipura virus have been used to measure the appearance of virus antigen on the surface of infected cells by the technique of surface analysis by bacterial adherence and scanning electron microscopy (SABA/SEM). The number of staphylococci specifically adhering to antiserum-treated infected PTK-2 or BSC-1 cells at permissive (31 degrees C) and restrictive (39 degrees C) temperatures was followed in time-course experiments and a close correspondence was observed between the proportion of staphylococci bound at 39 degrees C and the known phenotypic properties of the ts mutants. Virus surface antigen was undetected in cells infected by transcription- and replication-defective ts mutants with thermolabile L proteins under restrictive conditions up to an input multiplicity of infection of 50, and in cells infected by a replication-defective NS protein mutant. Some surface antigen was detected late in infection in PTK-2 cells infected by a replication-defective N protein mutant. Surface antigen accumulated normally in maturation-defective mutants with lesions in envelope proteins. These results establish the suitability of the SABA/SEM technique for quantitative estimation of virus antigen on the surface of infected cells.
J Gen Virol 1982 Mar
PMID:Measurement of surface antigen by specific bacterial adherence and scanning electron microscopy (SABA/SEM) in cells infected by vesiculovirus ts mutants. 627 72

The time course of force and stiffness during a twitch was determined at 6 and 26 degrees C in frog semitendinosus muscle bundles using the transmission time technique of Schoenberg, M., J.B. Wells, and R.J. Podolsky, 1974, J. Gen. Physiol. 64:623-642. Sarcomere shortening due to series compliance was also measured using a laser light diffraction technique. Following stimulation, stiffness developed more rapidly than force, but had a slower time course than published Ca2+ transients determined from light signals using Ca2+ sensitive dyes (Baylor, S.M., W.K. Chandler, and M.W. Marshall, 1982, J. Physiol. (Lond.). 331:139-177). Stiffness (S) did not reach its tetanic value during a twitch at 6 or 26 degrees C, although at 6 degrees C, it approached close to this value with S-twitch/S-tetanus = 0.82 +/- 0.07 (+/- SEM). During relaxation, force fell more rapidly than stiffness both for a twitch and also a tetanus. Also in this paper, several of the assumptions inherent in using the transmission time technique for the measurement of stiffness are considered in detail.
 ...
PMID:Stiffness, force, and sarcomere shortening during a twitch in frog semitendinosus muscle bundles. 660 49


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