Uptake of Lanthanum by Smooth Muscle

1972 ◽  
Vol 50 (7) ◽  
pp. 730-733 ◽  
Author(s):  
B. J. Hodgson ◽  
A. M. Kidwai ◽  
E. E. Daniel
Keyword(s):  
Smooth Muscle ◽  
Cell Surface ◽  
Extracellular Space ◽  
Volume Of Distribution ◽  
Cell Fractionation ◽  
Tissue Water ◽  
Calculated Volume

140La3+ was taken up and tightly bound by rat myometrium. Its calculated volume of distribution was much greater than tissue water, and it was associated after cell fractionation with cellular particulates. The highest amounts were found in mitochondria. These results invalidate assumptions that La3+ is confined to the extracellular space and limited in its action to the cell surface.

Tissue water and electrolytes in an isolated perfused rat's heart preparation

1961 ◽  
Vol 16 (1) ◽  
pp. 95-102 ◽  
Author(s):  
I. M. Taylor ◽  
W. D. Huffines ◽  
D. T. Young
Keyword(s):  
Extracellular Space ◽  
Volume Of Distribution ◽  
Space Distribution ◽  
Force Of Contraction ◽  
Cell Water ◽  
Perfusion Medium ◽  
Tissue Water ◽  
Perfused Rat Heart ◽  
Carbon 14 ◽  
Heart Preparation

An apparatus and technique for perfusion of rats' hearts is described. At 27°C hearts beat spontaneously, and the preparation is stable for periods in excess of 12 hours as judged by heart rate, EKG configuration, force of contraction, pH of perfusion medium and intracellular potassium. Carbon-14 labeled sucrose has been compared with chloride as a measure of tissue extracellular space and has been found unsatisfactory because volume of distribution for carbon-14 is larger than for chloride in most experiments. Carbon-14 labeled inulin-carboxylic acid (ICA), in contrast, appears to be a satisfactory marker for extracellular space. Distribution of ICA is complete in 1 hour. Values for intracellular electrolytes and water, derived assuming extracellularity of ICA, are: water, 2.56 α 0.14 gm/gm dry tissue; Na+ 24.36 α 14.12 mEq/kg cell water or 6.18 α 3.53 mEq/100 gm dry tissue; Cl- 23.16 α 6.70 mEq/kg cell water or 5.96 α 1.93 mEq/100 gm dry tissue; and K+ 144.69 α 7.31 mEq/kg cell water or 36.99 α 1.55 mEq/100 gm dry tissue. Chloride is not a satisfactory measure of extracellular space in the isolated perfused rat heart. Submitted on July 20, 1960

EFFECTS OF OVARIAN HORMONES ON THE CONTENT AND DISTRIBUTION OF CATION IN INTACT AND EXTRACTED RABBIT AND CAT UTERUS

1957 ◽  
Vol 35 (12) ◽  
pp. 1205-1223 ◽  
Author(s):  
Edwin E. Daniel ◽  
Betty N. Daniel
Keyword(s):  
Extracellular Space ◽  
Striate Muscle ◽  
Choline Chloride ◽  
Extracellular Fluid ◽  
Volume Of Distribution ◽  
Tissue Water ◽  
Cation Composition ◽  
The Best Approximation ◽  
Cellular Water

The uteri of rabbits and cats have been analyzed for sodium, potassium, and chloride, usually after various preliminary treatments with estrogen and progesterone. These tissues contain less potassium (50–80 meq./kg.) than striate muscle and more sodium (75–118 meq./kg.) than other highly cellular tissues. It appears that this cation composition can be attributed in part to a relatively large extracellular fluid volume (EFV).Various methods have been used to estimate the EFV in these tissues. The radiosulphate space (in vitro) does not appear to be reliable as a measure of extracellular space. The chloride space varies, but exceeds 400 ml./kg. in all cases, and in some approaches 700 ml./kg. Inulin space (in vitro) is about 60% of the chloride space, which in turn is usually smaller than the sodium space. The chloride space appears to provide the best approximation to the EFV since its volume of distribution rarely exceeds the sodium space, and since chloride (but not sodium) can be removed completely on leaching in isotonic sucrose.Calculated cellular potassium concentrations are as high as or higher (150–210 meq./l.) than in striate muscle. Apparently the low total tissue potassium concentration is a consequence of the large EFV.Appreciable quantities of sodium (20–50 meq./l.) reside outside of the chloride space in most cases, presumably in cellular water. Furthermore, a residue of sodium remains in uterine tissue after leaching in isotonic sucrose or choline chloride. With appropriate leaching procedures, an initial rapid depletion of tissue sodium is followed by a period of relatively slow loss, indicating derivation of sodium from at least two separate tissue spaces. Equilibration in isotonic potassium chloride causes nearly complete equilibration of potassium and chloride throughout tissue water, but does not remove residual sodium, suggesting chemical binding rather than Donnan distribution as the mechanism of sodium retention.The effects of estrogen and progesterone on the concentrations of cations in uterine cells are shown to be relatively small. Estrogen causes expansion of the cellular compartment relative to the extracellular space in both rabbit and cat and decreases the concentration of cation (per liter of tissue water and per liter of intracellular fluid). Progesterone treatment, given after estrogen, interfered with the ready entrance of chloride into the cellular space of rabbit uterus exposed to isotonic choline chloride. Cat uterus was not so affected, there being very little penetration of chloride even after estrogen alone.

Estimation of extracellular spaces of smooth muscle using different-sized molecules

1965 ◽  
Vol 208 (5) ◽  
pp. 1042-1045 ◽  
Author(s):  
Lloyd Barr ◽  
Richard L. Malvin
Keyword(s):  
Smooth Muscle ◽  
Serum Albumin ◽  
Extracellular Space ◽  
Molecular Size ◽  
Intestinal Smooth Muscle ◽  
Tissue Water ◽  
Sodium Potassium ◽  
Ion Concentrations ◽  
Intracellular Ion Concentrations ◽  
To Come

The apparent fraction of tissue water available as solvent was determined for a number of test substances: urea, arabinose, mannitol, sucrose, raffinose, inulin, and radioiodinated serum albumin. The apparent extracellular spaces decrease with increasing molecular size. Urea seems to come to concentration equilibrium in all tissue water. Arabinose and mannitol values are close together at about 70% tissue water. Similarly sucrose, raffinose, and inulin values cluster at about 48% tissue water, while RISA can reach only about 20%. The amounts of sodium, potassium, and chloride in canine intestinal smooth muscle are similar to values given for other smooth muscle. Intracellular ion concentrations similar to those of other tissues can be calculated if the true extracellular space is between that measured by RISA and sucrose.

EFFECTS OF OVARIAN HORMONES ON THE CONTENT AND DISTRIBUTION OF CATION IN INTACT AND EXTRACTED RABBIT AND CAT UTERUS

1957 ◽  
Vol 35 (1) ◽  
pp. 1205-1223 ◽  
Author(s):  
Edwin E. Daniel ◽  
Betty N. Daniel
Keyword(s):  
Extracellular Space ◽  
Striate Muscle ◽  
Choline Chloride ◽  
Extracellular Fluid ◽  
Volume Of Distribution ◽  
Tissue Water ◽  
Cation Composition ◽  
The Best Approximation ◽  
Cellular Water

The uteri of rabbits and cats have been analyzed for sodium, potassium, and chloride, usually after various preliminary treatments with estrogen and progesterone. These tissues contain less potassium (50–80 meq./kg.) than striate muscle and more sodium (75–118 meq./kg.) than other highly cellular tissues. It appears that this cation composition can be attributed in part to a relatively large extracellular fluid volume (EFV).Various methods have been used to estimate the EFV in these tissues. The radiosulphate space (in vitro) does not appear to be reliable as a measure of extracellular space. The chloride space varies, but exceeds 400 ml./kg. in all cases, and in some approaches 700 ml./kg. Inulin space (in vitro) is about 60% of the chloride space, which in turn is usually smaller than the sodium space. The chloride space appears to provide the best approximation to the EFV since its volume of distribution rarely exceeds the sodium space, and since chloride (but not sodium) can be removed completely on leaching in isotonic sucrose.Calculated cellular potassium concentrations are as high as or higher (150–210 meq./l.) than in striate muscle. Apparently the low total tissue potassium concentration is a consequence of the large EFV.Appreciable quantities of sodium (20–50 meq./l.) reside outside of the chloride space in most cases, presumably in cellular water. Furthermore, a residue of sodium remains in uterine tissue after leaching in isotonic sucrose or choline chloride. With appropriate leaching procedures, an initial rapid depletion of tissue sodium is followed by a period of relatively slow loss, indicating derivation of sodium from at least two separate tissue spaces. Equilibration in isotonic potassium chloride causes nearly complete equilibration of potassium and chloride throughout tissue water, but does not remove residual sodium, suggesting chemical binding rather than Donnan distribution as the mechanism of sodium retention.The effects of estrogen and progesterone on the concentrations of cations in uterine cells are shown to be relatively small. Estrogen causes expansion of the cellular compartment relative to the extracellular space in both rabbit and cat and decreases the concentration of cation (per liter of tissue water and per liter of intracellular fluid). Progesterone treatment, given after estrogen, interfered with the ready entrance of chloride into the cellular space of rabbit uterus exposed to isotonic choline chloride. Cat uterus was not so affected, there being very little penetration of chloride even after estrogen alone.

Abstract 17084: Nuclear Smooth Muscle α-actin Participates in Chromatin Remodeling at Smooth Muscle Contractile Gene Promoters

Circulation ◽  
2020 ◽  
Vol 142 (Suppl_3) ◽  
Author(s):  
Callie Kwartler ◽  
Shuangtao Ma ◽  
Caroline Kernell ◽  
Xue-yan Duan ◽  
Charis Wang ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Cardiac Muscle ◽  
Chromatin Remodeling ◽  
Muscle Cells ◽  
Cytoskeletal Proteins ◽  
Nuclear Localization Sequence ◽  
Serum Starvation ◽  
Cell Fractionation ◽  
Gene Promoters ◽  
Chromatin Remodeling Complexes

Actin genes encode for cytoskeletal proteins that polymerize to function in cellular motility, adhesion, and contraction. In mammalian cells, ubiquitously expressed β-actin also moves into the nucleus and associates with chromatin remodeling complexes, however a nuclear function of muscle-specific α-actins has not been previously assessed. We hypothesized that smooth muscle α-actin (SMA) plays a role in chromatin remodeling during the differentiation of smooth muscle cells (SMCs) to enable cell fate specification of SMCs. In explanted SMCs from human and mouse ascending aortas, cell fractionation and 2D gel electrophoresis identify both SMA and β-actin in the nuclear lysates. Nuclear SMA but not β-actin accumulates with SMC differentiation driven by serum starvation and transforming growth factor-β1 treatment. SMA accumulates into the nucleus early in the differentiation of SMCs from neural crest progenitor cells, prior to cytosolic accumulation. Immunoprecipitation studies show that SMA binds specifically to the INO80 and the SWI/SNF chromatin remodeling complexes, and this binding increases with SMC differentiation. Chromatin immunoprecipitation reveals that SMA is bound to the promoters of SMC-specific genes, including Acta2 , Cnn1, and Myh11 and that SMA is enriched over β-actin at these promoters with SMC differentiation. Finally, overexpression of SMA tagged with a nuclear localization sequence (NLS) in multiple cell types increases expression of SMC markers, whereas NLS-tagged β-actin localizes to the nucleus to the same extent but does not increase SMC marker expression in any cell type. Finally, we assessed whether skeletal muscle α-actin (SKA) and cardiac muscle α-actin (CMA) may play a similar role in skeletal and cardiac muscle cells. Both SKA and CMA translocate into the nucleus. CMA accumulates into the nucleus early in the differentiation of cardiomyocytes from pluripotent stem cells. Immunoprecipitation reveals that SKA binds to the SWI/SNF complex in differentiated C2C12 myotube cell cultures. These data support that nuclear SMA enriches with and participates in SMC differentiation, and suggest a potential nuclear role for other muscle specific α-actins in developing muscle cells.

Espace extracellulaire, perméabilité à l'inuline et accumulation de L-alanine dans l'intestin isolé de Grenouille

1973 ◽  
Vol 51 (1) ◽  
pp. 22-28
Author(s):  
Joël de la Noüe ◽  
André Gagnon
Keyword(s):  
Extracellular Space ◽  
Muscle Layer ◽  
Solute Concentration ◽  
Tissue Water ◽  
Intracellular Amino Acid ◽  
Inulin Space ◽  
Total Tissue ◽  
Frog Intestine

In order to calculate the intracellular concentration of accumulated L-alanine, the extracellular space (inulin-14C) of frog intestine was measured. To check the validity of the technique, frog liver and gastrocnemius were used too. By scraping proximal portions of intestine, the inulin space was found to be similar (around 20% of total tissue water) in both the muscle layer and the mucosa. The mucosal epithelium is an imperfect barrier to inulin while the serosa is very permeable. These results suggest that the interstitial solute concentration is best approximated by equating it to that of the serosal solution. The in vitro inulin space, compared to the in vivo one, increases with time, as does the cellular hydration. The data obtained from measurements of extracellular space and from L-alanine uptake show that the intracellular amino acid is in a free state.

scholarly journals CD63 is a component of Weibel-Palade bodies of human endothelial cells

Blood ◽  
1993 ◽  
Vol 82 (4) ◽  
pp. 1184-1191 ◽  
Author(s):  
UM Vischer ◽  
DD Wagner
Keyword(s):  
Endothelial Cells ◽  
Cell Surface ◽  
Western Blotting ◽  
Vascular Endothelial Cells ◽  
Secretory Granules ◽  
Positive Staining ◽  
Cell Fractionation ◽  
Glycosylation Pattern ◽  
Adhesion Proteins ◽  
Shape Distribution

Weibel-Palade bodies are secretory granules of vascular endothelial cells specialized in the storage of von Willebrand factor (vWF) and P- selectin, two adhesion proteins that can be rapidly mobilized to the cell surface by exocytosis in response to thrombin or other agonists. In this study, we attempted to identify additional components of Weibel- Palade bodies by raising monoclonal antibodies to these granules, purified by cell fractionation. One antibody, 2C6, was found to be specific for CD63, a membrane glycoprotein previously described in the lysosomes of platelets and other cell types. The immunopurified 2C6 antigen was recognized by an anti-CD63 reference antibody, 2.28, by Western blotting. Also, the biosynthetic profile of the 2C6 antigen in endothelial cells showed a nascent molecular mass and a glycosylation pattern identical to that of CD63. Immunofluorescence staining with 2C6 showed the lysosomes, and also elongated structures identified as Weibel-Palade bodies by their shape, distribution, and positive staining with anti-vWF antibodies, CD63 was also found by Western blotting of subcellular fractions highly enriched in Weibel-Palade bodies. Our results indicate that CD63 colocalizes with vWF and P- selectin in the Weibel-Palade bodies of endothelial cells, and together with these adhesion proteins it could be rapidly expressed on the cell surface in areas of vascular injury and inflammation.

Cell surface components and growth regulation in cultivated arterial smooth muscle cells

1983 ◽  
Vol 64 (1) ◽  
pp. 107-121
Author(s):  
J. Nilsson ◽  
T. Ksiazek ◽  
J. Thyberg ◽  
A. Wasteson
Keyword(s):  
Smooth Muscle ◽  
Sialic Acid ◽  
Cell Surface ◽  
Smooth Muscle Cells ◽  
Dna Synthesis ◽  
Growth Regulation ◽  
Heparan Sulphate ◽  
Carboxyl Groups ◽  
Anionic Sites ◽  
Arterial Smooth Muscle Cells

The surface of rat arterial smooth muscle cells was characterized with respect to some of its chemical and functional properties. The effects of selective enzymic degradations (hyaluronidase, chondroitinases, heparitinase or neuraminidase) on [35S]sulphate-prelabelled cells and on binding sites for cationized ferritin (CF) were examined to assess the presence and relative importance of individual species of macromolecules on the cell surface. The results indicate that about half of the strongly anionic sites on the cell surface (binding CF at pH 2.0) could be ascribed to sulphate groups of glycosaminoglycans and about half to carboxyl groups of sialic acid residues in glycoproteins and/or glycolipids. Weaker anionic sites (binding CF at pH 7.0) largely originated from carboxyl groups of glycosaminoglycans. Chondroitin sulphate and heparan sulphate were the main glycosaminoglycans. The surface of cells from young animals showed a higher glycosaminoglycan and a lower sialic acid content than that of cells from adult animals. Continuous treatment of the cultures with neuraminidase stimulated serum-induced initiation of DNA synthesis, while treatment with hyaluronidase or heparitinase inhibited it. Addition of hyaluronic acid, heparin or heparan sulphate to the culture medium inhibited initiation of DNA synthesis as well as cell proliferation. The effect was more marked in cultures of cells from young animals than from adults, although the latter cells were found to grow at a higher rate and to higher densities. These results suggest a role for cell-surface and pericellular glycoconjugates in growth regulation. A possible mechanism of action is that these molecules, due to their anionic charge or by steric exclusion, interfere with the binding of platelet-derived growth factor, a highly cationic polypeptide, to its cell-surface receptor.

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