Systems Approach to Study of Solute Transport Across Membranes Using Suspension Cultures of Mammalian Cells II: Experimental Procedures and Uptake Studies with Cholesterol

1972 ◽  
Vol 61 (10) ◽  
pp. 1618-1624 ◽  
Author(s):  
J.S. Turi ◽  
W.I. Higuchi ◽  
C. Shipman ◽  
N.F.H. Ho
Keyword(s):  
Solute Transport ◽  
Mammalian Cells ◽  
Systems Approach ◽  
Suspension Cultures ◽  
Uptake Studies

Structure, function, and genomic organization of human Na+-dependent high-affinity dicarboxylate transporter

2000 ◽  
Vol 278 (5) ◽  
pp. C1019-C1030 ◽  
Author(s):  
Haiping Wang ◽  
You-Jun Fei ◽  
Ramesh Kekuda ◽  
Teresa L. Yang-Feng ◽  
Lawrence D. Devoe ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Catalytic Domain ◽  
Xenopus Laevis Oocytes ◽  
Ph Titration ◽  
High Affinity ◽  
Inward Currents ◽  
Induced Currents ◽  
Uptake Studies ◽  
A Charge ◽  
Carboxy Terminal

We have cloned and functionally characterized the human Na+-dependent high-affinity dicarboxylate transporter (hNaDC3) from placenta. The hNaDC3 cDNA codes for a protein of 602 amino acids with 12 transmembrane domains. When expressed in mammalian cells, the cloned transporter mediates the transport of succinate in the presence of Na+ [concentration of substrate necessary for half-maximal transport ( K t) for succinate = 20 ± 1 μM]. Dimethylsuccinate also interacts with hNaDC3. The Na+-to-succinate stoichiometry is 3:1 and concentration of Na+ necessary for half-maximal transport[Formula: see text]is 49 ± 1 mM as determined by uptake studies with radiolabeled succinate. When expressed in Xenopus laevis oocytes, hNaDC3 induces Na+-dependent inward currents in the presence of succinate and dimethylsuccinate. At a membrane potential of −50 mV,[Formula: see text] is 102 ± 20 μM and[Formula: see text]is 22 ± 4 mM as determined by the electrophysiological approach. Simultaneous measurements of succinate-evoked charge transfer and radiolabeled succinate uptake in hNaDC3-expressing oocytes indicate a charge-to-succinate ratio of 1:1 for the transport process, suggesting a Na+-to-succinate stoichiometry of 3:1. pH titration of citrate-induced currents shows that hNaDC3 accepts preferentially the divalent anionic form of citrate as a substrate. Li+inhibits succinate-induced currents in the presence of Na+. Functional analysis of rat-human and human-rat NaDC3 chimeric transporters indicates that the catalytic domain of the transporter lies in the carboxy-terminal half of the protein. The human NaDC3 gene is located on chromosome 20q12–13.1, as evidenced by fluorescent in situ hybridization. The gene is >80 kbp long and consists of 13 exons and 12 introns.

Modeling Suspension Cultures of Microbial and Mammalian Cells with an Adaptable Six-Compartment Model

2017 ◽  
Vol 40 (5) ◽  
pp. 956-966 ◽  
Author(s):  
Simone Brüning ◽  
Inga Gerlach ◽  
Ralf Pörtner ◽  
Carl-Fredrik Mandenius ◽  
Volker C. Hass
Keyword(s):  
Mammalian Cells ◽  
Compartment Model ◽  
Suspension Cultures

Synchrony of Long Duration in Suspension Cultures of Mammalian Cells

1971 ◽  
Vol 234 (48) ◽  
pp. 148-149 ◽  
Author(s):  
R. SCHINDLER ◽  
C. HÜRNI
Keyword(s):  
Mammalian Cells ◽  
Suspension Cultures ◽  
Long Duration

scholarly journals A systems approach to hemostasis: 3. Thrombus consolidation regulates intrathrombus solute transport and local thrombin activity

Blood ◽  
2014 ◽  
Vol 124 (11) ◽  
pp. 1824-1831 ◽  
Author(s):  
Timothy J. Stalker ◽  
John D. Welsh ◽  
Maurizio Tomaiuolo ◽  
Jie Wu ◽  
Thomas V. Colace ◽  
...  
Keyword(s):  
Solute Transport ◽  
Tyrosine Phosphorylation ◽  
Platelet Activation ◽  
Systems Approach ◽  
Thrombus Formation ◽  
Thrombin Activity ◽  
Key Points ◽  
Β3 Integrin

Key Points β3 integrin tyrosine phosphorylation regulates thrombus consolidation in vivo. Intrathrombus solute transport regulates local thrombin activity and platelet activation during hemostatic thrombus formation in vivo.

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