Weinstein2000_OMCD

This a model from the article:
A mathematical model of the outer medullary collecting duct of the rat.

Weinstein AM. Am J Physiol Renal Physiol
2000 Jul;279(1):F24-45 10894785
,
Abstract:

A mathematical model of the outer medullary collecting duct (OMCD) has been
developed, consisting of alpha-intercalated cells and a paracellular pathway,
and which includes Na(+), K(+), Cl(-), HCO(3)(-), CO(2), H(2)CO(3), phosphate,
ammonia, and urea. Proton secretion across the luminal cell membrane is mediated
by both H(+)-ATPase and H-K-ATPase, with fluxes through the H-K-ATPase given by
a previously developed kinetic model (Weinstein AM. Am J Physiol Renal Physiol
274: F856-F867, 1998). The flux across each ATPase is substantial, and variation
in abundance of either pump can be used to control OMCD proton secretion. In
comparison with the H(+)-ATPase, flux through the H-K-ATPase is relatively
insensitive to changes in lumen pH, so as luminal acidification proceeds, proton
secretion shifts toward this pathway. Peritubular HCO(3)(-) exit is via a
conductive pathway and via the Cl(-)/HCO(3)(-) exchanger, AE1. To represent AE1,
a kinetic model has been developed based on transport studies obtained at 38
degrees C in red blood cells. (Gasbjerg PK, Knauf PA, and Brahm J. J Gen Physiol
108: 565-575, 1996; Knauf PA, Gasbjerg PK, and Brahm J. J Gen Physiol 108:
577-589, 1996). Model calculations indicate that if all of the chloride entry
via AE1 recycles across a peritubular chloride channel and if this channel is
anything other than highly selective for chloride, then it should conduct a
substantial fraction of the bicarbonate exit. Since both luminal membrane proton
pumps are sensitive to small changes in cytosolic pH, variation in density of
either AE1 or peritubular anion conductance can modulate OMCD proton secretory
rate. With respect to the OMCD in situ, available buffer is predicted to be
abundant, including delivered HCO(3)(-) and HPO(4)(2-), as well as peritubular
NH(3). Thus, buffer availability is unlikely to exert a regulatory role in total
proton secretion by this tubule segment.
This model was taken from the CellML repository
and automatically converted to SBML.
The original model was:
Weinstein AM. (2000) - version=1.0

The original CellML model was created by:
Jonna Terkildsen

[e-mail]
The University of Auckland
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