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Articles by D. Q Li
Total Records ( 3 ) for D. Q Li
  C. S De Paiva , S. B Pangelinan , E Chang , K. C Yoon , W. J Farley , D. Q Li and S. C. Pflugfelder
 

Objective  To investigate the protective effects of c-Jun N-terminal kinase (JNK)–1 and -2 gene knockout (KO) on the corneal epithelial response to desiccating stress.

Methods  The C57BL/6, JNK1KO, and JNK2KO mice were subjected to desiccating stress (DS) for 5 days. The effects of DS on the corneal epithelium were evaluated by measuring corneal smoothness and permeability. Expression of matrix metalloproteinases (MMP)–1, MMP-9, and cornified envelope protein precursors (small proline-rich protein [SPRR]–1a, SPRR-2a, and involucrin) in the corneal epithelia was evaluated by immunostaining and real-time polymerase chain reaction. Collagenase and gelatinase activity in corneal sections as measured with in situ fluorescent assays.

Results  The JNK2KO mice had smoother corneal surfaces and less corneal barrier disruption in response to DS than JNK1KO mice and C57BL/6 wild-type control mice. The DS increased levels of MMP-1, MMP-9, SPRR-1a, SPRR-2a, involucrin immunoreactivity, and mRNA transcripts in the corneal epithelium of JNK1KO and C57BL/6 mice, but not in JNK2KO mice. Knockout of JNK2 prevented DS-induced increase in gelatinase and collagenase activity in the cornea.

Conclusion  The JNK2 protein appears to have an essential role in desiccation-induced corneal epithelial disease by stimulating production of MMP-1, MMP-9, and cornified envelope precursors.

Clinical Relevance  The JNK2 protein could be a novel therapeutic target in dry eye disease.

  T. M Reinbothe , R Ivarsson , D. Q Li , O Niazi , X Jing , E Zhang , L Stenson , U Bryborn and E. Renstrom
 

Nicotinamide adenine dinucleotide phosphate (NADPH) enhances Ca2+-induced exocytosis in pancreatic β-cells, an effect suggested to involve the cytosolic redox protein glutaredoxin-1 (GRX-1). We here detail the role of GRX-1 in NADPH-stimulated β-cell exocytosis and glucose-stimulated insulin secretion. Silencing of GRX-1 by RNA interference reduced glucose-stimulated insulin secretion in both clonal INS-1 832/13 cells and primary rat islets. GRX-1 silencing did not affect cell viability or the intracellular redox environment, suggesting that GRX-1 regulates the exocytotic machinery by a local action. By contrast, knockdown of the related protein thioredoxin-1 (TRX-1) was ineffective. Confocal immunocytochemistry revealed that GRX-1 locates to the cell periphery, whereas TRX-1 expression is uniform. These data suggest that the distinct subcellular localizations of TRX-1 and GRX-1 result in differences in substrate specificities and actions on insulin secretion. Single-cell exocytosis was likewise suppressed by GRX-1 knockdown in both rat β-cells and clonal 832/13 cells, whereas after overexpression exocytosis increased by approximately 40%. Intracellular addition of NADPH (0.1 mm) stimulated Ca2+-evoked exocytosis in both cell types. Interestingly, the stimulatory action of NADPH on the exocytotic machinery coincided with an approximately 30% inhibition in whole-cell Ca2+ currents. After GRX-1 silencing, NADPH failed to amplify insulin release but still inhibited Ca2+ currents in 832/13 cells. In conclusion, NADPH stimulates the exocytotic machinery in pancreatic β-cells. This effect is mediated by the NADPH acceptor protein GRX-1 by a local redox reaction that accelerates β-cell exocytosis and, in turn, insulin secretion.

  P. R Molli , D. Q Li , R Bagheri Yarmand , S. B Pakala , H Katayama , S Sen , J Iyer , J Chernoff , M. Y Tsai , S. S Nair and R. Kumar
 

In addition to its function as an Arp2/3 complex subunit, Arp1cb interacts with and stimulates Aurora A at centrosomes, functioning in cell cycle progression.

 
 
 
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