Comparative studies of the sugar chains of aminopeptidase N and dipeptidylpeptidase IV purified from rat kidney brush-border membrane

Biochemistry ◽  
1988 ◽  
Vol 27 (15) ◽  
pp. 5565-5573 ◽  
Author(s):  
Katsuko Yamashita ◽  
Yoko Tachibana ◽  
Yoshiko Matsuda ◽  
Nobuhiko Katunuma ◽  
Naohisa Kochibe ◽  
...  
Keyword(s):  
Brush Border ◽  
Comparative Studies ◽  
Brush Border Membrane ◽  
Rat Kidney ◽  
Aminopeptidase N ◽  
Dipeptidylpeptidase Iv ◽  
Sugar Chains

N-linked neutral sugar chains of aminopeptidase N purified from rat small intestinal brush-border membrane

Biochemistry ◽  
1991 ◽  
Vol 30 (37) ◽  
pp. 9102-9110 ◽  
Author(s):  
Seiichi Takasaki ◽  
Roger H. Erickson ◽  
Young S. Kim ◽  
Naohisa Kochibe ◽  
Akira Kobata
Keyword(s):  
Brush Border ◽  
Brush Border Membrane ◽  
Aminopeptidase N ◽  
Neutral Sugar ◽  
Intestinal Brush Border Membrane ◽  
Intestinal Brush Border ◽  
Small Intestinal ◽  
Sugar Chains

scholarly journals Studies on the orientation of brush-border membrane vesicles

1978 ◽  
Vol 172 (1) ◽  
pp. 57-62 ◽  
Author(s):  
W Haase ◽  
A Schäfer ◽  
H Murer ◽  
R Kinne
Keyword(s):  
Brush Border ◽  
Brush Border Membrane ◽  
Rat Kidney ◽  
Freeze Fracture ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Immunological Methods ◽  
Kidney Cortex ◽  
Asymmetric Distribution ◽  
Rat Kidney Cortex

Orientation of rat renal and intestinal brush-border membrane vesicles was studied with two independent methods: electron-microscopic freeze-fracture technique and immunological methods. With the freeze-fracture technique a distinct asymmetric distribution of particles on the two membrane fracture faces was demonstrated; this was used as a criterion for orientation of the isolated membrane vesicles. For the immunological approach the accessibility or inaccessibility of aminopeptidase M localized on the outer surface of the cell membrane to antibodies was used. With both methods we showed that the brush-border membrane vesicles isolated from rat kidney cortex and from rat small intestine for transport studies are predominantly orientated right-side out.

Immunolocalization of NHE8 in rat kidney

2005 ◽  
Vol 288 (3) ◽  
pp. F530-F538 ◽  
Author(s):  
Sunita Goyal ◽  
SueAnn Mentone ◽  
Peter S. Aronson
Keyword(s):  
Proximal Tubule ◽  
Brush Border ◽  
Brush Border Membrane ◽  
Rat Kidney ◽  
Surface Membrane ◽  
Proximal Tubules ◽  
Intense Staining ◽  
Proximal Tubule Cells ◽  
Nephron Segment ◽  
Tubule Cells

In situ hybridization studies demonstrated that Na+/H+ exchanger NHE8 is expressed in kidney proximal tubules. Although membrane fractionation studies suggested apical brush-border localization, precise membrane localization could not be definitively established. The goal of the present study was to develop isoform-specific NHE8 antibodies as a tool to directly establish the localization of NHE8 protein in the kidney by immunocytochemistry. Toward this goal, two sets of antibodies that label different NHE8 epitopes were developed. Monoclonal antibody 7A11 and polyclonal antibody Rab65 both specifically labeled NHE8 by Western blotting as well as by immunofluorescence microscopy. The immunolocalization pattern in the kidney seen with both antibodies was the same, thereby validating NHE8 specificity. In particular, NHE8 expression was observed on the apical brush-border membrane of all proximal tubules from S1 to S3. The most intense staining was evident in proximal tubules in the deeper cortex and medulla with a significant but somewhat weaker staining in superficial proximal tubules. Colocalization studies with γ-glutamyltranspeptidase and megalin indicated expression of NHE8 on both the microvillar surface membrane and the coated-pit region of proximal tubule cells, suggesting that NHE8 may be subject to endocytic retrieval and recycling. Although colocalizing in the proximal tubule with NHE3, no significant alteration in NHE8 protein expression was evident in NHE3-null mice. We conclude that NHE8 is expressed on the apical brush-border membrane of proximal tubule cells, where it may play a role in mediating or regulating ion transport in this nephron segment.

Internalization and intracellular transport of folate-binding protein in rat kidney proximal tubule

1993 ◽  
Vol 264 (2) ◽  
pp. C302-C310 ◽  
Author(s):  
H. Birn ◽  
J. Selhub ◽  
E. I. Christensen
Keyword(s):  
Plasma Membrane ◽  
Proximal Tubule ◽  
Brush Border ◽  
Intracellular Transport ◽  
Brush Border Membrane ◽  
Specific Binding ◽  
Binding Protein ◽  
Rat Kidney ◽  
Folate Binding Protein

Folate-binding protein (FBP) is involved in folate reabsorption in the renal proximal tubule. Immunocytochemical studies have located FBP to the brush-border membrane, endocytic vacuoles, and dense apical tubules. We applied the same polyclonal antibody (anti-FBP) against FBP to investigate the dynamic relationship between FBP in the different compartments by microinjecting the antibody into rat kidney proximal tubules in situ. Specific binding of anti-FBP in vivo to the brush-border membrane was followed by fixation at various times. Protein A-gold labeling shows that anti-FBP is transported from endocytic invaginations into vacuoles followed by transport into dense apical tubules within 15 s. Thus FBP is rapidly internalized, and together with previous studies this study strongly suggests recycling of FBP back to the luminal plasma membrane through dense apical tubules. The results are consistent with reabsorption of folate through endocytosis of the FBP-folate complex followed by dissociation and recycling of FBP. When time is allowed there is a steady accumulation of FBP in dense apical tubules combined with an increase in surface density of the same compartment. A possible explanation involves partial inhibition of the fusion between dense apical tubules and plasma membrane because of the anti-FBP labeling of the receptor.

Adenosine (Ado) uptake in brush-border membrane vesicles from rat kidney (BBM)

1991 ◽  
Vol 19 (3) ◽  
pp. 323S-323S ◽  
Author(s):  
J. SAYOS ◽  
J. J. CENTELLES ◽  
J. MALLOL ◽  
E. I. CANELA ◽  
C. LLUIS ◽  
...  
Keyword(s):  
Brush Border ◽  
Brush Border Membrane ◽  
Rat Kidney ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles

scholarly journals Aminopeptidase N (CD13) Is a Molecular Target of the Cholesterol Absorption Inhibitor Ezetimibe in the Enterocyte Brush Border Membrane

2004 ◽  
Vol 280 (2) ◽  
pp. 1306-1320 ◽  
Author(s):  
Werner Kramer ◽  
Frank Girbig ◽  
Daniel Corsiero ◽  
Anja Pfenninger ◽  
Wendelin Frick ◽  
...  
Keyword(s):  
Brush Border ◽  
Brush Border Membrane ◽  
Cholesterol Absorption ◽  
Molecular Target ◽  
Aminopeptidase N ◽  
Cholesterol Absorption Inhibitor
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