Search PubMed⌕ Search

Biomedical subjects

L Hopp

Publications and source records attributed to L Hopp.

47 records · Page 3Linked to original sources
PubMed1986

Na+-K+ regulation in cultured vascular smooth muscle cell of the spontaneously hypertensive rat.

Na+-K+ passive transport and activity of the Na+ pump were examined in serially passed cultured vascular smooth muscle cells originating from spontaneously hypertensive (SH), Wistar-Kyoto (WKY), and Wistar (W) rats. Measurements included 22Na+ and 86Rb+ (K+ analogue) uptake and washout rate constants as well as intracellular Na+ and K+ levels. The aforementioned variables were studied in cells subjected to either 2 mM Ca2+ or Ca2+-deficient media. In 2 mM Ca2+ medium, SH rat cells demonstrated the highest exchange (uptake and washout) rate constants for Na+ and Rb+ (K+) among cells of the three rat strains. At this extracellular Ca2+ concentration, the Na+ pump activity of SH rat cells was higher than that of WKY rat cells and was not different from that of W rat cells. Incubation in Ca2+-deficient medium resulted in increased magnitudes of Rb+ washout and Na+ uptake rate constants in all cell preparations associated with elevated intracellular Na+ concentrations and augmented activity of the Na+ pump. Under this condition, cells derived from SH rats showed the highest Na+ uptake and Rb+ washout rate constants associated with the highest Na+ pump activity. The increase in intracellular Na+ level in Ca2+-deficient medium was the highest in SH rat cells. These findings show that innate membrane defects and the response of the Na+ pump to these abnormalities can be demonstrated in in vitro-grown vascular smooth muscle cells of the SH rat.

Animals↗
PubMed1986

Ouabain binding to cultured vascular smooth muscle cells of the spontaneously hypertensive rat.

The binding of ouabain and K+ to the Na+ pump were analyzed in serially passed cultured vascular smooth muscle cells (VSMCs) originating from spontaneously hypertensive (SH), Wistar-Kyoto (WKY), and American Wistar (W) rats. Our techniques have utilized analyses of displacement of [3H]ouabain by both unlabeled ouabain and K+ from specific binding sites on the VSMCs. We have found that each of the VSMC preparations from the three rat strains appeared to demonstrate one population of specific ouabain receptors (Na+ pumps); the number of Na+ pump units (mean +/- SE, expressed as 10(5) units/cell; number of observations indicated in parentheses) of both the SH and WKY rats was significantly lower than the number of Na+ pump units of W rat VSMCs [SH: 3.00 +/- 0.02 (231), WKY: 2.87 +/- 0.05 (245), and W: 3.62 +/- 0.04 (225)]; the equilibrium dissociation constant values (microM) for ouabain in VSMCs of SH and WKY rats were similar but were significantly higher than that of VSMCs derived from W rats [SH: 4.69 +/- 0.09 (231), WKY: 4.57 +/- 0.12 (245), and W: 3.69 +/- 0.17 (225)]; and among the VSMCs originating from the three rat strains, the apparent equilibrium dissociation constant value for K+ (mM) was the lowest in those of the SH rat [1.04 +/- 0.003 (143), compared with VSMCs of the WKY rat [1.54 +/- 0.006 (135)] and W rat [1.19 +/- 0.003 (136)]. Our previous studies have demonstrated increased passive Na+ and K+ transport rate constants of SH rat VSMCs compared with either W or WKY rat cells. These findings suggest the possibility of higher permeabilities of the SH cells.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1986

[3H]ouabain binding of red blood cells in whites and blacks.

In a previous study, we demonstrated that the red blood cell Na+ concentration and Na+,K+-ATPase activity are sex-dependent and race-dependent: a higher intracellular Na+ concentration in blacks and men was associated with a lower Na+,K+-ATPase activity. To examine whether the low Na+,K+-ATPase activity is due to a decreased number of enzyme units, altered structure of the enzyme, or the presence of an endogenous digoxinlike substance, ouabain binding studies were performed on the same subject group. The measurements included displacement of [3H]ouabain from its specific binding sites by unlabeled ouabain or potassium. The results demonstrate that groups with lower enzyme activity manifest lower numbers of total specific ouabain binding sites on the surface of the red blood cell (mean +/- SD: blacks, 654 +/- 24.4; whites, 806 +/- 18.3; women, 806 +/- 26.9; men, 728 +/- 21.2). Other kinetic parameters of [3H]ouabain displacement appear to be the same among the groups. The respective red blood cell Na+ and K+ concentrations were negatively and positively correlated with the number of ouabain binding sites. Our findings suggest that the lower activity of red blood cell Na+,K+-ATPase in blacks and men is a function of a lower number of Na+-K+ pump units. The results also indicate that sex and race should be considered when red blood cell ouabain binding is examined.

Adenosine Triphosphatases↗
PubMed1986

Bumetanide-sensitive sodium-22 transport in vascular smooth muscle cell of the spontaneously hypertensive rat.

The effect of bumetanide, a known probe of Na+, K+ cotransport, on 22Na+ uptake and washout was examined in serially passed cultured vascular smooth muscle cells of spontaneously hypertensive rats (SHR), Wistar-Kyoto rats (WKY), and Wistar rats. In Ca2+-deficient medium, the drug exerted the greatest effect on 22Na+ washout in vascular smooth muscle cells from SHR and the least effect on cells from WKY. The respective mean values for the apparent bumetanide-sensitive 22Na+ washout rate constants (Ke; X 10(-2)/min) were 7.2, 4.3, and 1.7 for cells from SHR, WKY, and Wistar rats. In both 1 mM Ca2+ and Ca2+-deficient medium, in the presence of 1 mM ouabain, vascular smooth muscle cells from SHR had the highest plateau phase of 22Na+ uptake among the three cell preparations. All cells exhibited higher 22Na+ uptake in Ca2+-deficient medium than in 1 mM Ca2+ medium. Under this condition, bumetanide caused an additional rise in steady state 22Na+ uptake that was most pronounced in cells from SHR (21.3% versus 16.6% for Wistar rats and 4.8% for WKY). This finding indicates that a quantitatively greater inhibition of washout than of the uptake component of the bumetanide-sensitive 22Na+ transport occurs in Ca2+-deficient medium. It is concluded that, in Ca2+-deficient medium, the bumetanide-sensitive 22Na+ washout is higher in vascular smooth muscle cells of SHR than in those of normotensive controls and that this phenomenon reflects a higher Na+ turnover in vascular smooth muscle cell in the hypertensive rat strain.

Animals↗
PubMed1985

Cultured rat vascular smooth muscle cells: extracellular calcium and Na+-K+ regulation.

This study explores the relationship between extracellular calcium (Cao) and Na+-K+ regulation as it particularly pertains to the activity of the Na+ pump in cultured vascular smooth muscle cells (VSMCs) originating from Sprague-Dawley rats. As compared with cells incubated in media containing 0.5, 2.0, or 4.0 mM calcium, when the Na pump is active, VSMCs incubated in a Ca-deficient medium show a marked increase in intracellular sodium and no significant change in intracellular potassium. Associated with the rise in intracellular sodium there is an augmented activity of the Na pump. When the Na pump is inhibited, VSMCs incubated in either high-Ca medium (Cao = 4.0 mM) or Ca-deficient medium manifest a greater decline in intracellular potassium than cells incubated in media containing 0.5 or 2.0 mM calcium. Furthermore, when the Na pump is inhibited, VSMCs incubated in a Ca-deficient medium exhibit higher intracellular sodium levels in comparison with their counterparts incubated in media containing calcium. Flux experiments indicate that the aforementioned changes reflect increased membrane permeabilities to Na+ and K+. It is concluded that by regulating the permeability of the VSMC membrane, Cao plays an important role in the intracellular Na+-K+ homeostasis and that its effect on the Na pump is mediated via perturbations in the intracellular Na+ and K+ concentrations.

Animals↗
PubMed1985

Race and sex differences in erythrocyte Na+, K+, and Na+-K+-adenosine triphosphatase.

Several reports indicate that erythrocytes (RBCs) from blacks and men have higher sodium concentrations than those from whites and women. One possible mechanism to explain this finding is a difference in the activity of Na+-K+-ATPase. To explore this possibility, we have studied the Na+ and K+ kinetics of RBC Na+-K+-ATPase and RBC Na+ and K+ concentrations in 37 normotensive blacks and whites, both males and females. The maximal initial reaction velocity (Vmax) values for RBC Na+-K+-ATPase were lower in blacks and men as compared with whites and women. Higher RBC Na+ levels were observed in blacks and males vs. whites and females. Significant inverse correlations were noted between the Na+-K+-ATPase activity and RBC Na+ concentrations. These findings indicate that cellular Na+ homeostasis is different in blacks and men as compared with whites and women. Since higher RBC Na+ concentrations have also been observed in patients with essential hypertension as compared with normotensive subjects, the higher intracellular Na+ concentrations in blacks and men may contribute to the greater predisposition of these groups to essential hypertension.

Adult↗
PubMed1985

The effect of melittin on Na+ and Rb+ transport in cultured skin fibroblasts of the spontaneously hypertensive rat.

Melittin effect on transport of Na+ and Rb+(K+ analog) was examined in cultured skin fibroblasts originating from the Spontaneously Hypertensive, Wistar Kyoto and Wistar rats. Melittin increased both Na+ (22Na+) uptake and 86Rb+ efflux as well as the activity of the Na+-pump (ouabain sensitive 86Rb+ uptake) in all three preparations. The effect of the toxin was maximal at a dose of 160-240ng/10(5) cells/ml. At this dose, fibroblasts of the Spontaneously Hypertensive rat demonstrated the greatest response to melittin with respect to the increase in Na+ and Rb+ fluxes and increase in the intracellular Na+ concentrations. It is concluded that melittin can be utilized as a probe to delineate subtle differences in the cellular regulation of Na+ and K+ in the Spontaneously Hypertensive rat as compared with its normotensive controls.

Animals↗
PubMed1985

Correlation between post-replication repair and metastatic potential in B16 mouse melanoma cell lines.

The rate of postreplication repair of the B16-F1 and the B16-F10 variant clones was compared to the parent B16CL4 mouse melanoma cells in an attempt to correlate the postreplication repair efficiency with the metastatic potential of these melanoma cells. The rate of postreplication repair of the B16-F10 subline was 47% higher than that of the parent B16CL4 mouse melanoma cells and 20% higher than that of the B16-F1 cells. This higher rate of postreplication repair in the B16-F10 cells correlates with its higher metastatic potential. It was also of interest to notice that the rate of postreplication repair of the B16-F1 and the B16-F10 cells are comparable to their rate of replicon joining in non-irradiated cells, in contrast to the parent B16CL4 cells whose rate of post-replication repair was significantly lower than its rate of replicon joining.

Animals↗
PubMed1984

[3H]ouabain binding to cultured rat vascular smooth muscle cells.

The number of Na+ pump units (Bmax) and the equilibrium dissociation constant (Kd) for ouabain as well as parameters of K+ binding to the Na+ pump were examined in in vitro-grown vascular smooth muscle cells ( VSMC ) derived from Sprague-Dawley rats. The technique to measure these variables utilizes analyses of [3H]ouabain displacement from its VSMC receptors by nonlabeled ouabain and K+. The mean values for Bmax and Kd in the cultured VSMCs were 1.95 X 10(5) receptor sites per single VSMC and 2.68 X 10(-6) M, respectively. The equilibrium dissociation constant for K+ (Ki) was 0.92 mM. K+ binding to the cultured VSMCs demonstrated positive cooperativity with a Hill coefficient (n) of 1.78.

Animals↗
PubMed1981

In vitro induction of ornithine decarboxylase in urinary bladder carcinoma cells.

The induction of ornithine decarboxylase by normal rat urine in bladder cancer cell cultures was tested in view of recent observations that urine acts as a tumor promoter. Addition of urine up to 15% in final concentration to culture medium resulted in a 10-fold increase in ornithine decarboxylase activity over the control. The stimulatory factor(s) contained in urine appears heat stable and may be multiple. 12-O-Tetradecanoylphorbol-13-acetate, a potent promoter in mouse skin carcinogenesis, induced a 39-fold increase in ornithine decarboxylase activity, the best response among the various substances tested. This suggests that it may act as a promoter of bladder cancer.

Animals↗