T-/H-cadherin (CDH13):: a new marker for differentiating podocytes

被引:4
作者
Arnemann, J
Sultani, O
Hasgün, D
Coerdt, W
机构
[1] Univ Frankfurt Hosp, Inst Pathol, D-60590 Frankfurt, Germany
[2] Univ Frankfurt Hosp, Inst Human Genet, D-60590 Frankfurt, Germany
[3] Univ Mainz, Inst Pathol, Dept Paediat Pathol, D-6500 Mainz, Germany
关键词
T-; /H; -cadherin; GPI anchor; human foetal kidney; capillary loop stage; podocytes;
D O I
10.1007/s00428-005-0055-7
中图分类号
R36 [病理学];
学科分类号
100104 ;
摘要
Cadherin molecules are known to be involved in various biological processes other than cell adhesion such as morphogenesis, cell-cell communication, cell recognition or cell signalling. While the classical cadherin molecule is characterized by an extracellular moiety, a transmembrane region and a variable cytoplasmic domain, T-/H-cadherin differs from this pattern due to the absence of a transmembrane region and a cytoplasmic domain, respectively. Its extracellular moiety is bound to the apical cell membrane by a glycosyl-phosphatidyl-inositol anchor and localized to lipid raft domains. As its molecular function and expression pattern is still not fully understood, we used a newly generated anti-T-/H-cadherin antiserum to study immunohistochemically the expression of T-/H-cadherin during the differentiation of foetal human glomeruli. At the early capillary loop stage a strong apical signal comes up for visceral epithelial cells of Bowman's capsule, which begin to differentiate towards podocytes. At the advanced capillary loop stage, when podocytes have become part of the glomerular filtration barrier, the expression pattern, however, becomes more distinct and most likely restricted to the foot processes of the podocytes. We thus postulate a functional role of T-/H-cadherin for the differentiation of the podocytes and the formation of the glomerular capillary network.
引用
收藏
页码:160 / 164
页数:5
相关论文
共 12 条
[1]  
Angst BD, 2001, J CELL SCI, V114, P629
[2]  
ARNEMANN J, 1993, J CELL SCI, V104, P741
[3]   Growth and death in the developing mammalian kidney: signals, receptors and conversations [J].
Bard, JBL .
BIOESSAYS, 2002, 24 (01) :72-82
[4]   Genetic dissection of cadherin function during nephrogenesis [J].
Dahl, U ;
Sjödin, A ;
Larue, L ;
Radice, GL ;
Cajander, S ;
Takeichi, M ;
Kemler, R ;
Semb, H .
MOLECULAR AND CELLULAR BIOLOGY, 2002, 22 (05) :1474-1487
[5]  
DIECKMANN CL, 1985, J BIOL CHEM, V260, P1513
[6]   T-cadherin is a major glycophosphoinositol-anchored protein associated with noncaveolar detergent-insoluble domains of the cardiac sarcolemma [J].
Doyle, DD ;
Goings, GE ;
Upshaw-Earley, J ;
Page, E ;
Ranscht, B ;
Palfrey, HC .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (12) :6937-6943
[7]   Differential targeting of T- and N-cadherin in polarized epithelial cells [J].
Koller, E ;
Ranscht, B .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (47) :30061-30067
[8]   Membrane microdomains and caveolae [J].
Kurzchalia, TV ;
Parton, RG .
CURRENT OPINION IN CELL BIOLOGY, 1999, 11 (04) :424-431
[9]   Density- and proliferation status-dependent expression of T-cadherin, a novel lipoprotein-binding glycoprotein: a function in negative regulation of smooth muscle cell growth? [J].
Kuzmenko, YS ;
Kern, F ;
Bochkov, VN ;
Tkachuk, VA ;
Resink, TJ .
FEBS LETTERS, 1998, 434 (1-2) :183-187
[10]   H-cadherin, a novel cadherin with growth inhibitory functions and diminished expression in human breast cancer [J].
Lee, SW .
NATURE MEDICINE, 1996, 2 (07) :776-782