Qiwei Yang
Northwestern University
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Featured researches published by Qiwei Yang.
American Journal of Physiology-renal Physiology | 1999
Yashpal S. Kanwar; Kosuke Ota; Qiwei Yang; Jun Wada; Naoki Kashihara; Yufeng Tian; Elisabeth I. Wallner
Extracellular matrix (ECM) proteins, their integrin receptors, and matrix metalloproteinases (MMPs), the ECM-degrading enzymes, are believed to be involved in various biological processes, including embryogenesis. In the present study, we investigated the role of membrane type MMP, MT-1-MMP, an activator pro-MMP-2, in metanephric development. Also, its relationship with MMP-2 and its inhibitor, TIMP-2, was studied. Since mRNAs of MT-1-MMP and MMP-2 are respectively expressed in the ureteric bud epithelia and mesenchyme, they are ideally suited for juxtacrine/paracrine interactions during renal development. Northern blot analyses revealed a single ∼4.5-kb mRNA transcript of MT-1-MMP, and its expression was developmentally regulated. Inclusion of MT-1-MMP antisense oligodeoxynucleotide (ODN) in the culture media induced dysmorphogenetic changes in the embryonic metanephros. MMP-2 antisense ODN also induced similar changes, but they were relatively less; on the other hand TIMP-2 antisense ODN induced a mild increase in the size of explants. Concomitant exposure of MT-1-MMP and MMP-2 antisense ODNs induced profound alterations in the metanephroi. Treatment of TIMP-2 antisense ODN to metanephroi exposed to MT-1-MMP/MMP-2 antisense notably restored the morphology of the explants. Specificity of the MT-1-MMP antisense ODN was reflected in the selective decrease in its mRNA and protein expression. The MT-1-MMP antisense ODN also resulted in a failure in the activation of pro-MMP-2 to MMP-2. These findings suggest that the trimacromolecular complex of MT-1-MMP:MMP-2:TIMP-2 modulates the organogenesis of the metanephros, conceivably by mediating paracrine/juxtacrine epithelial:mesenchymal interactions.Extracellular matrix (ECM) proteins, their integrin receptors, and matrix metalloproteinases (MMPs), the ECM-degrading enzymes, are believed to be involved in various biological processes, including embryogenesis. In the present study, we investigated the role of membrane type MMP, MT-1-MMP, an activator pro-MMP-2, in metanephric development. Also, its relationship with MMP-2 and its inhibitor, TIMP-2, was studied. Since mRNAs of MT-1-MMP and MMP-2 are respectively expressed in the ureteric bud epithelia and mesenchyme, they are ideally suited for juxtacrine/paracrine interactions during renal development. Northern blot analyses revealed a single approximately 4.5-kb mRNA transcript of MT-1-MMP, and its expression was developmentally regulated. Inclusion of MT-1-MMP antisense oligodeoxynucleotide (ODN) in the culture media induced dysmorphogenetic changes in the embryonic metanephros. MMP-2 antisense ODN also induced similar changes, but they were relatively less; on the other hand TIMP-2 antisense ODN induced a mild increase in the size of explants. Concomitant exposure of MT-1-MMP and MMP-2 antisense ODNs induced profound alterations in the metanephroi. Treatment of TIMP-2 antisense ODN to metanephroi exposed to MT-1-MMP/MMP-2 antisense notably restored the morphology of the explants. Specificity of the MT-1-MMP antisense ODN was reflected in the selective decrease in its mRNA and protein expression. The MT-1-MMP antisense ODN also resulted in a failure in the activation of pro-MMP-2 to MMP-2. These findings suggest that the trimacromolecular complex of MT-1-MMP:MMP-2:TIMP-2 modulates the organogenesis of the metanephros, conceivably by mediating paracrine/juxtacrine epithelial:mesenchymal interactions.
American Journal of Physiology-renal Physiology | 1998
Yashpal S. Kanwar; Kosuke Ota; Qiwei Yang; Anil Kumar; Jun Wada; Naoki Kashihara; Darryl R. Peterson
The role of fibrillin-1 in metanephrogenesis was investigated. Fibrillin-1 cDNA was isolated from the rat kidney cDNA library and sequenced, and its spatiotemporal expression was studied. It had ∼88% homology with human fibrillin-1 and had Ca2+ binding epidermal growth factor-like domains, transforming growth factor-β binding protein motifs, and an RGD binding site. Northern blot analysis revealed an ∼10-kb transcript, and fibrillin-1 expression was developmentally regulated. In situ hybridization and immunofluorescence studies indicated that at day 15 of gestation, fibrillin-1 is expressed in the metanephric mesenchyme. At day 18, its expression was confined to nascent blood vessels and glomeruli, and it increased in the newborn and neonatal kidneys. Immunoprecipitation revealed an ∼300-kDa band by SDS-PAGE. Treatment with fibrillin-1 antisense oligodeoxynucleotide induced marked dysmorphogenesis of the embryonic metanephroi. Concomitantly, the fibrillin-1 mRNA, antibody reactivity in the metanephroi, and fibrillin-1-specific radioincorporation were reduced. These data indicate that, like αvβ3integrin, a known morphogen and a putative receptor of fibrillin-1, the fibrillin-1 modulates events related to early organogenesis and possibly also the vascularization of the rat kidney.
American Journal of Physiology-renal Physiology | 1998
Yashpal S. Kanwar; Jun Wada; Sun Lin; Farhad R. Danesh; Sumant S. Chugh; Qiwei Yang; Tushar Banerjee; Jon W. Lomasney
Proceedings of the National Academy of Sciences of the United States of America | 2000
Qiwei Yang; Bharat L. Dixit; Jun Wada; Yufeng Tian; Elisabeth I. Wallner; Satish K. Srivastva; Yashpal S. Kanwar
Kidney International | 1998
Kosuke Ota; William G. Stetler-Stevenson; Qiwei Yang; Anil Kumar; Jun Wada; Naoki Kashihara; Elisabeth I. Wallner; Yashpal S. Kanwar
Proceedings of the National Academy of Sciences of the United States of America | 1999
Yashpal S. Kanwar; Anil Kumar; Qiwei Yang; Yufeng Tian; Jun Wada; Naoki Kashihara; Elisabeth I. Wallner
Proceedings of the National Academy of Sciences of the United States of America | 2005
Baibaswata Nayak; Ping Xie; Shigeru Akagi; Qiwei Yang; Lin Sun; Jun Wada; Arun Thakur; Farhad R. Danesh; Sumant S. Chugh; Yashpal S. Kanwar
Developmental Biology | 1999
Qiwei Yang; Kosuke Ota; Yufeng Tian; Anil Kumar; Jun Wada; Naoki Kashihara; Elisabeth I. Wallner; Yashpal S. Kanwar
American Journal of Physiology-renal Physiology | 2000
Qiwei Yang; Yufeng Tian; Jun Wada; Naoki Kashihara; Elisabeth I. Wallner; Darryl R. Peterson; Yashpal S. Kanwar
American Journal of Physiology-renal Physiology | 2002
Yashpal S. Kanwar; Qiwei Yang; Yufeng Tian; Sun Lin; Jun Wada; Sumant S. Chugh; Satish K. Srivastava