Differential localisation of UDP-glucuronosyltransferase in kidney during human embryonic and fetal development.
The aim of our study was to localise UDP-glucuronosyltransferase (UDPGT) in the developing mesonephric and metanephric kidneys of the human embryo and fetus, using immunohistochemical methods and an antibody preparation with broad specificity to the human isoforms. In embryonic and early fetal development of the metanephric kidney, UDPGT is located primarily in derivatives of the ureteric bud such as the ureter, pelvis, calyces and collecting ducts. This early predominance of UDPGT to ureteric bud derivatives declines by mid-fetal life: a) as nephrons evolve and develop they become increasingly UDPGT immunoreactive such that in mature metanephric kidney, the proximal tubules are highly UDPGT reactive, with other elements of the nephron also immunopositive (albeit at lower reactivities) and b) with the formation of an immunonegative transitional epithelium in ureter, pelvis and calyces, the reactivity retained in collecting ducts is only a small proportion of the total. The distribution of UDPGT immunoreactivity is relatively uniform in proximal tubular cells throughout development. This is in contrast to collecting ducts where, in fetal life, this reactivity is displaced to apices and bases by intracellular glycogen deposits. Parietal cells of Bowman's capsule are immunoreactive, but glomeruli are negative. In mesonephric kidney, as early as 32 days post-ovulation, tubules and the mesonephric duct are UDPGT immunoreactive and mesonephric immunopositivity overlaps with that in the developing metanephric kidney.
Hume
R
R
Department of Obstetrics and Gynaecology, University of Dundee Medical School, Ninewells Hospital, UK.
Coughtrie
M W
MW
Burchell
B
B
D005314:Embryonic and Fetal Development; D005333:Fetus / Q000201:enzymology; D014453:Glucuronosyltransferase / Q000378:metabolism*; D006801:Humans; D007124:Immunoenzyme Techniques; D007668:Kidney / Q000196:embryology* / Q000201:enzymology*
D014453:Glucuronosyltransferase