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1 Department of Nephrology, University Hospital, Lund, Sweden
2 Department of Physiology, University of Bergen, Bergen, Norway
3 Department of Clinical Chemistry, University Hospital, Lund, Sweden
* To whom correspondence should be addressed. E-mail: Bengt.Rippe{at}njur.lu.se.
The size and charge selective properties of the glomerular barrier are partly controversial. Glomerular sieving coefficients (
) for proteins have rarely been determined non-invasively before in vivo. Therefore, was assessed vs. GFR (51Cr-EDTA clearance) in intact rats for radiolabelled myoglobin, 
-dimer, neutral horseradish peroxidase (nHRP), neutral albumin (nHSA) and native albumin (HSA). To obtain , glomerular tracer clearance, assessed from the 7-8 min kidney uptake of protein, was divided by the GFR. The data fitted with a two-pore model of glomerular permeability, where the small pore radius was 37.35±1.11 Å (±SE), and the "unrestricted pore area over diffusion path length" (A0/
X) 1.84±0.43 x 106 cm. Although seemingly horizontal for nHRP and nHSA, the log vs. GFR curves showed slightly neg. slopes for the proteins investigated in the GFR interval of 2-4.5 ml/min. Strong neg. (linear) correlations between (log) and GFR were obtained for myoglobin (p = 0.002) and HSA (p = 0.006), while they were relatively weak for nHRP and nHSA and non-significant 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.
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