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Departments of 1 Nephrology and 3 Clinical Chemistry, University Hospital, S-221 85 Lund, Sweden; and 2 Department of Physiology, University of Bergen, N-5509 Bergen, Norway
The size and charge-selective properties
of the glomerular barrier are partly controversial. Glomerular sieving
coefficients (
) for proteins have rarely been determined
noninvasively before in vivo. Therefore, was assessed vs.
glomerular filtration rate (GFR; 51Cr-EDTA clearance) in
intact rats for radiolabeled myoglobin, 
-dimer, neutral horseradish
peroxidase (nHRP), neutral human serum albumin (nHSA), and native
albumin (HSA). To obtain , glomerular tracer clearance, assessed
from the 7- to 8-min kidney uptake of protein, was divided by the GFR.
The data were fitted with a two-pore model of glomerular permeability,
where the small-pore radius was 37.35 ± 1.11 (SE) Å, and the
"unrestricted pore area over diffusion path length"
(A0/
X) 1.84 ± 0.43 · 106 cm. Although seemingly
horizontal for nHRP and nHSA, the log vs. GFR curves showed
slightly negative slopes for the proteins investigated in the GFR
interval of 2-4.5 ml/min. Strong negative (linear) correlations
between (log) and GFR were obtained for myoglobin
(P = 0.002) and HSA (P = 0.006),
whereas they were relatively weak for nHRP and nHSA and nonsignificant
for -dimer. for nHSA was markedly higher than that for HSA. In
conclusion, there were no indications of increases in vs. GFR, as
indicative of concentration polarization, for the proteins investigated
at high GFRs. Furthermore, the glomerular small-pore radius assessed
from endogenous (neutral) protein sieving data was found to be smaller
than previously determined using dextran or Ficoll as test molecules.
glomerular permeability; macromolecules; reflection coefficient; transport
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