Abstract
Mammalian nephrogenesis is modulated by a number of extracellular matrix (ECM) glycoproteins, integrins and cell adhesion molecules. We demonstrated the existence of integrins αvβ1, αvβ3, αvβ5 and αvβ6 in epithelial elements of developing nephrons. Fibrillin-1 is a putative ligand for integrin αvβ3, and tubulo-interstitial nephritis antigen (TIN-ag) is a ligand for integrins αvβ3 and α31. Fibrillin-1 and TIN-ag are also differentially expressed in the developing kidney. The inclusion of antisense oligonucleotide in a mouse kidney organ culture system indicated that the αv-related integrins and their ligands play an important role in mammalian nephrogenesis. Recently identified modulators of cell-matrix interactions, i.e. β-galactoside-binding mammalian lectins (galectins), are involved in cell-cell and cell-matrix interactions by cross-linking glycoconjugates located on the ECM and membrane-bound glycoproteins. We identified and cloned a new member of the galectins from embryonic kidneys, and designated it galectin-9. Since high glucose alters the expression of ECM proteins and integrins, we also investigated the influence of glucose on metanephric development. The presence of 30 mM D-glucose in metanephric organ culture induced dysmorphogenesis of the kidney accompanied by decreased expression of perlecan. Furthermore, we screened the genes differentially expressed under high glucose conditions in streptozotocin-induced newborn mouse kidneys by representational difference analysis of cDNA. We identified translocase of inner mitochondrial membrane (Tim44) and renal-specific oxido-reductase (RSOR). The roles of these molecules in glucose-induced dysmorphogenesis and the relationship with ECM-related molecules need to be addressed.
| Original language | English |
|---|---|
| Pages (from-to) | 75-77 |
| Number of pages | 3 |
| Journal | Nephrology Dialysis Transplantation |
| Volume | 17 |
| Issue number | SUPPL. 9 |
| Publication status | Published - 2002 |
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Keywords
- Fibrilin-1
- Galectin-9
- Integrin αv
- Tim44
- TIN-ag
ASJC Scopus subject areas
- Nephrology
- Transplantation
Cite this
Relevance of extracellular matrix and its receptors in mammalian nephrogenesis revealed by metanephric organ culture sysrem. / Wada, Jun; Kanwar, Yashpal S.; Makino, Hirofumi.
In: Nephrology Dialysis Transplantation, Vol. 17, No. SUPPL. 9, 2002, p. 75-77.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Relevance of extracellular matrix and its receptors in mammalian nephrogenesis revealed by metanephric organ culture sysrem
AU - Wada, Jun
AU - Kanwar, Yashpal S.
AU - Makino, Hirofumi
PY - 2002
Y1 - 2002
N2 - Mammalian nephrogenesis is modulated by a number of extracellular matrix (ECM) glycoproteins, integrins and cell adhesion molecules. We demonstrated the existence of integrins αvβ1, αvβ3, αvβ5 and αvβ6 in epithelial elements of developing nephrons. Fibrillin-1 is a putative ligand for integrin αvβ3, and tubulo-interstitial nephritis antigen (TIN-ag) is a ligand for integrins αvβ3 and α31. Fibrillin-1 and TIN-ag are also differentially expressed in the developing kidney. The inclusion of antisense oligonucleotide in a mouse kidney organ culture system indicated that the αv-related integrins and their ligands play an important role in mammalian nephrogenesis. Recently identified modulators of cell-matrix interactions, i.e. β-galactoside-binding mammalian lectins (galectins), are involved in cell-cell and cell-matrix interactions by cross-linking glycoconjugates located on the ECM and membrane-bound glycoproteins. We identified and cloned a new member of the galectins from embryonic kidneys, and designated it galectin-9. Since high glucose alters the expression of ECM proteins and integrins, we also investigated the influence of glucose on metanephric development. The presence of 30 mM D-glucose in metanephric organ culture induced dysmorphogenesis of the kidney accompanied by decreased expression of perlecan. Furthermore, we screened the genes differentially expressed under high glucose conditions in streptozotocin-induced newborn mouse kidneys by representational difference analysis of cDNA. We identified translocase of inner mitochondrial membrane (Tim44) and renal-specific oxido-reductase (RSOR). The roles of these molecules in glucose-induced dysmorphogenesis and the relationship with ECM-related molecules need to be addressed.
AB - Mammalian nephrogenesis is modulated by a number of extracellular matrix (ECM) glycoproteins, integrins and cell adhesion molecules. We demonstrated the existence of integrins αvβ1, αvβ3, αvβ5 and αvβ6 in epithelial elements of developing nephrons. Fibrillin-1 is a putative ligand for integrin αvβ3, and tubulo-interstitial nephritis antigen (TIN-ag) is a ligand for integrins αvβ3 and α31. Fibrillin-1 and TIN-ag are also differentially expressed in the developing kidney. The inclusion of antisense oligonucleotide in a mouse kidney organ culture system indicated that the αv-related integrins and their ligands play an important role in mammalian nephrogenesis. Recently identified modulators of cell-matrix interactions, i.e. β-galactoside-binding mammalian lectins (galectins), are involved in cell-cell and cell-matrix interactions by cross-linking glycoconjugates located on the ECM and membrane-bound glycoproteins. We identified and cloned a new member of the galectins from embryonic kidneys, and designated it galectin-9. Since high glucose alters the expression of ECM proteins and integrins, we also investigated the influence of glucose on metanephric development. The presence of 30 mM D-glucose in metanephric organ culture induced dysmorphogenesis of the kidney accompanied by decreased expression of perlecan. Furthermore, we screened the genes differentially expressed under high glucose conditions in streptozotocin-induced newborn mouse kidneys by representational difference analysis of cDNA. We identified translocase of inner mitochondrial membrane (Tim44) and renal-specific oxido-reductase (RSOR). The roles of these molecules in glucose-induced dysmorphogenesis and the relationship with ECM-related molecules need to be addressed.
KW - Fibrilin-1
KW - Galectin-9
KW - Integrin αv
KW - Tim44
KW - TIN-ag
UR - http://www.scopus.com/inward/record.url?scp=0036380545&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0036380545&partnerID=8YFLogxK
M3 - Article
VL - 17
SP - 75
EP - 77
JO - Nephrology Dialysis Transplantation
JF - Nephrology Dialysis Transplantation
SN - 0931-0509
IS - SUPPL. 9
ER -