Galectin-3 modulates ureteric bud branching in organ culture of the developing mouse kidney.
Galectin-3 is a mammalian beta-galactoside-specific lectin with functions in cell growth, adhesion, and neoplastic transformation. On the basis of expression patterns in humans, it is proposed that galectin-3 modulates fetal collecting duct growth. This article provides evidence that galectin-3 can modulate branching morphogenesis of the mouse ureteric bud/collecting duct lineage. With the use of immunohistochemistry, galectin-3 was not detected in early metanephrogenesis but was upregulated later in fetal kidney maturation when the protein was prominent in basal domains of medullary collecting ducts. Addition of galectin-3 to embryonic days 11 and 12 whole metanephric cultures inhibited ureteric bud branching, whereas galectin-1 did not perturb morphogenesis, nor did a galectin-3 mutant lacking wild-type high-affinity binding to extended oligosaccharides. Exogenous galectin-3 retarded conversion of renal mesenchyme to nephrons in whole metanephric explants but did not affect nephron induction by spinal cord in isolated renal mesenchymes. Finally, addition of a blocking antiserum to galectin-3 caused dilation and distortion of developing epithelia in embryonic day 12 metanephroi cultured for 1 wk. The upregulation of galectin-3 protein during kidney maturation, predominantly at sites where it could mediate cell/matrix interactions, seems to modulate growth of the ureteric tree.
Bullock
Simon L
SL
Division of Mammalian Development, National Institute for Medical Research, London, United Kingdom.
Johnson
Tanya M
TM
Division of Protein Structure, National Institute for Medical Research, London, United Kingdom.
Bao
Q I
QI
Nephro-Urology Unit, Institute of Child Health, London, United Kingdom.
Hughes
R Colin
RC
Nephro-Urology Unit, Institute of Child Health, London, United Kingdom.
Winyard
Paul J D
PJD
Division of Protein Structure, National Institute for Medical Research, London, United Kingdom.
Woolf
Adrian S
AS
Division of Protein Structure, National Institute for Medical Research, London, United Kingdom.
D000818:Animals; D000943:Antigens, Differentiation / Q000235:genetics / Q000494:pharmacology / Q000502:physiology*; D001483:Base Sequence; D064026:Calbindins; D002460:Cell Line; D017931:DNA Primers / Q000235:genetics; D004285:Dogs; D005314:Embryonic and Fetal Development / Q000187:drug effects; D037502:Galectin 3; D005865:Gestational Age; D007150:Immunohistochemistry; D007668:Kidney / Q000187:drug effects / Q000196:embryology*; D007797:Laminin / Q000378:metabolism; D051379:Mice; D009154:Mutation; D009924:Organ Culture Techniques; D064030:S100 Calcium Binding Protein G / Q000378:metabolism; D014513:Ureter / Q000187:drug effects / Q000196:embryology*
D000943:Antigens, Differentiation; D064026:Calbindins; D017931:DNA Primers; D037502:Galectin 3; D007797:Laminin; D064030:S100 Calcium Binding Protein G