Bile Canalicular Membrane Na+, K+-ATPase

2015 ◽  
pp. 108-112
Author(s):  
James L. Boyer ◽  
Donna Reno ◽  
Thomas Layden
Keyword(s):  
Canalicular Membrane ◽  
Bile Canalicular Membrane

scholarly journals mdr2 encodes P-glycoprotein expressed in the bile canalicular membrane as determined by isoform-specific antibodies.

1992 ◽  
Vol 267 (25) ◽  
pp. 18093-18099
Author(s):  
E Buschman ◽  
R.J. Arceci ◽  
J.M. Croop ◽  
M Che ◽  
I.M. Arias ◽  
...  
Keyword(s):  
Canalicular Membrane ◽  
Specific Antibodies ◽  
P Glycoprotein ◽  
Bile Canalicular Membrane

Importance of bicarbonate in bile salt independent fraction of bile flow.

1978 ◽  
Vol 235 (2) ◽  
pp. E158 ◽  
Author(s):  
W G Hardison ◽  
C A Wood
Keyword(s):  
Bile Salt ◽  
Bile Flow ◽  
Transport Mechanism ◽  
Excretion Rate ◽  
Organic Anion ◽  
Weak Acid ◽  
Anion Transport ◽  
Bicarbonate Transport ◽  
Canalicular Membrane ◽  
Bile Canalicular Membrane

The bile salt independent fraction (BSIF) of canalicular bile flow from the isolated rat liver perfused with bicarbonate-free perfusate is 50% of that from the liver perfused with bicarbonate-containing perfusate. HCO3-excretion is nearly eliminated and Na+ and Cl- excretion is reduced 50%. Replacement of HCO3- into perfusate increased bile flow by 0.3 microliter/g.min without changing bile acid excretion rate. 5.5-Dimethyl-2,4-oxazolidinedione (DMO) produced a similar effect. DMO was passively distributed between bile and plasma. The data indicate that a bicarbonate transport mechanism is responsible for production of up to 50% of the BSIF. Another weak acid, N-5[5-(2-methoxyethoxy)-2-pyrimidinyl]sulfamoylbenzene (glymidine), was rapidly excreted into bile and increased bile flow by over 2.0 microliter/g.min. Glymidine is probably excreted by an independent organic anion transport mechanism, and any effect on the bicarbonate transport mechanism is obscured. Canaliculus-enriched hepatocyte membrane fractions contained no HCO3-stimulated ATPase activity. Either this enzyme is unimportant in hepatocyte bicarbonate transport or transport occurs across membranes other than the bile canalicular membrane.

scholarly journals Role of membranes in bile formation. Comparison of the composition of bile and a liver bile-canalicular plasma-membrane subfraction

1976 ◽  
Vol 154 (3) ◽  
pp. 589-595 ◽  
Author(s):  
W H. Evans ◽  
T Kremmmer ◽  
J G. Culvenor
Keyword(s):  
Molecular Weight ◽  
Plasma Membrane ◽  
Bile Acids ◽  
Secretory Process ◽  
Major Protein ◽  
Outer Face ◽  
Ph Optimum ◽  
Bile Formation ◽  
Canalicular Membrane ◽  
Bile Canalicular Membrane

1. Enzymes, proteins, glycoproteins and lipids of rodent bile were compared with those of a plasma-membrane subfraction originating from the hepatocyte bile-canalicular membrane. 2. Three bile-canalicular glycoprotein enzyme activities were detected in bile. Comparison of the pH optimum and immunoinhibition properties of membrane and bile 5′-nucleotidase activity indicated that they were the same enzyme. Correspondence between membrane and bile alkaline phosphodiesterases also suggested that they were the same enzymes. Activities of Mg2+-stimulated adenosine triphosphatase, a lipid-dependent intrinsic membrane protein, and galactosyltransferase, a Golgi membrane marker, were not detected in bile. 3. Rodent bile contained 15 polypeptide bands that differed radically from those of bile-canalicular membranes. Bands that may correspond in molecular weight to liver plasma-membrane glycoproteins were present at low staining intensities in bile. A major protein of apparent molecular weight 49 500 was present, and albumin was detected by immunodiffusion. 4. The lipid composition of bile and bile-canalicular membrane also differed. Phosphatidylcholine accounted for 82% of rat bile phospholipids, and only trace amounts of phosphatidylinositol, phosphatidylserine and sphingomyelin were present. 5. The results indicate that in healthy animals, the bile-canalicular membrane is refractory to the action of bile acids during the secretory process. The presence of only small amounts of bile-canalicular membrane components, especially glycoprotein enzymes located at the outer face of the membrane, suggests that these are released from the membrane by bile acids after secretion of bile into the canalicular spaces.

Peptidase content of the bile canalicular membrane

1995 ◽  
Vol 23 (2) ◽  
pp. 306S-306S ◽  
Author(s):  
KATHERINE A. ZUZEL ◽  
JOHN G. GRAHAM ◽  
JOHN HRYSZKO ◽  
DAVID BILLINGTON ◽  
ANTHONY J. TURNER
Keyword(s):  
Canalicular Membrane ◽  
Bile Canalicular Membrane

Micellar Solubilization of Lipid from Isolated Bile Canalicular Membrane

1982 ◽  
Vol 62 (2) ◽  
pp. 51P-51P
Author(s):  
J. Graham ◽  
R. Bird ◽  
K.B. Saunders ◽  
T.C. Northfield
Keyword(s):  
Micellar Solubilization ◽  
Canalicular Membrane ◽  
Bile Canalicular Membrane

scholarly journals ATP8B1 Deficiency Disrupts the Bile Canalicular Membrane Bilayer Structure in Hepatocytes, But FXR Expression and Activity Are Maintained

2009 ◽  
Vol 136 (3) ◽  
pp. 1060-1069.e4 ◽  
Author(s):  
Shi–Ying Cai ◽  
Samir Gautam ◽  
Trong Nguyen ◽  
Carol J. Soroka ◽  
Christoph Rahner ◽  
...  
Keyword(s):  
Bilayer Structure ◽  
Membrane Bilayer ◽  
Canalicular Membrane ◽  
Bile Canalicular Membrane ◽  
Expression And Activity
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