David A. Scheiblin
University of Delaware
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Publication
Featured researches published by David A. Scheiblin.
Journal of Cellular and Molecular Medicine | 2014
Fahmy A. Mamuya; Yan Wang; Victoria Roop; David A. Scheiblin; Jocelyn C. Zajac; Melinda K. Duncan
Posterior capsular opacification (PCO) is the major complication arising after cataract treatment. PCO occurs when the lens epithelial cells remaining following surgery (LCs) undergo a wound healing response producing a mixture of α‐smooth muscle actin (α‐SMA)‐expressing myofibroblasts and lens fibre cells, which impair vision. Prior investigations have proposed that integrins play a central role in PCO and we found that, in a mouse fibre cell removal model of cataract surgery, expression of αV integrin and its interacting β‐subunits β1, β5, β6, β8 are up‐regulated concomitant with α‐SMA in LCs following surgery. To test the hypothesis that αV integrins are functionally important in PCO pathogenesis, we created mice lacking the αV integrin subunit in all lens cells. Adult lenses lacking αV integrins are transparent and show no apparent morphological abnormalities when compared with control lenses. However, following surgical fibre cell removal, the LCs in control eyes increased cell proliferation, and up‐regulated the expression of α‐SMA, β1‐integrin, fibronectin, tenascin‐C and transforming growth factor beta (TGF‐β)–induced protein within 48 hrs, while LCs lacking αV integrins exhibited much less cell proliferation and little to no up‐regulation of any of the fibrotic markers tested. This effect appears to result from the known roles of αV integrins in latent TGF‐β activation as αV integrin null lenses do not exhibit detectable SMAD‐3 phosphorylation after surgery, while this occurs robustly in control lenses, consistent with the known roles for TGF‐β in fibrotic PCO. These data suggest that therapeutics antagonizing αV integrin function could be used to prevent fibrotic PCO following cataract surgery.
Mechanisms of Development | 2014
Abby L. Manthey; Salil A. Lachke; Paul G. FitzGerald; Robert W. Mason; David A. Scheiblin; John H. McDonald; Melinda K. Duncan
SIP1 encodes a DNA-binding transcription factor that regulates multiple developmental processes, as highlighted by the pleiotropic defects observed in Mowat-Wilson syndrome, which results from mutations in this gene. Further, in adults, dysregulated SIP1 expression has been implicated in both cancer and fibrotic diseases, where it functionally links TGFβ signaling to the loss of epithelial cell characteristics and gene expression. In the ocular lens, an epithelial tissue important for vision, Sip1 is co-expressed with epithelial markers, such as E-cadherin, and is required for the complete separation of the lens vesicle from the head ectoderm during early ocular morphogenesis. However, the function of Sip1 after early lens morphogenesis is still unknown. Here, we conditionally deleted Sip1 from the developing mouse lens shortly after lens vesicle closure, leading to defects in coordinated fiber cell tip migration, defective suture formation, and cataract. Interestingly, RNA-Sequencing analysis on Sip1 knockout lenses identified 190 differentially expressed genes, all of which are distinct from previously described Sip1 target genes. Furthermore, 34% of the genes with increased expression in the Sip1 knockout lenses are normally downregulated as the lens transitions from the lens vesicle to early lens, while 49% of the genes with decreased expression in the Sip1 knockout lenses are normally upregulated during early lens development. Overall, these data imply that Sip1 plays a major role in reprogramming the lens vesicle away from a surface ectoderm cell fate towards that necessary for the development of a transparent lens and demonstrate that Sip1 regulates distinctly different sets of genes in different cellular contexts.
BioTechniques | 2012
Elisabeth Knapp; Rosemary Flores; David A. Scheiblin; Shannon Modla; Kirk J. Czymmek; Vidadi Yusibov
In this study, we have developed a robust cryohistological method that allows imaging of virtually any type of plant cell or tissue while preserving fluorescent protein signals and maintaining excellent cellular and subcellular morphology. This method involves modified fixation of plant tissues (i.e., leaves, stems, and petioles), infiltration in a sucrose gradient, freezing, and collection of cryosections directly onto a cryoadhesive tape. Using this method followed by microscopic analysis, we demonstrated a localized accumulation of green fluorescent protein (GFP) in Nicotiana benthamiana plants agroinfiltrated with the movement-incompetent tobacco mosaic virus-based vector and systemic accumulation of GFP in plants infiltrated with the movement-competent vector. Overall, this simple cryohistological procedure reduced sample preparation time and allowed processing of tissue sections for high-resolution imaging of targeted fluorescent proteins in all plant tissues.
Experimental Eye Research | 2017
Dylan S. Audette; David A. Scheiblin; Melinda K. Duncan
Lens fiber cells are highly elongated cells with complex membrane morphologies that are critical for the transparency of the ocular lens. Investigations into the molecular mechanisms underlying lens fiber cell elongation were first reported in the 1960s, however, our understanding of the process is still poor nearly 50 years later. This review summarizes what is currently hypothesized about the regulation of lens fiber cell elongation along with the available experimental evidence, and how this information relates to what is known about the regulation of cell shape/elongation in other cell types, particularly neurons.
Journal of Biomolecular Structure & Dynamics | 2015
Archana D. Siddam; Carole Gautier-Courteille; Atul Kakrana; Vincent Legagneux; Christine A. Dang; Linette Perez-Campos; Agnès Méreau; David A. Scheiblin; Justine Viet; David C. Beebe; Jeffery M. Gross; Luc Paillard; Salil A. Lachke
551–561. Chawla, M., Safwat, A.-A., Romina, O., & Cavallo, L. (2014). Higher order structural effects stabilizing the reverse Watson–Crick guanine–cytosine base pair in functional RNAs. Nucleic Acids Research, 42, 714–726. Serra, M. J., Baird, J. D., Taraka, D., Fey, B. L., Retatagos, K., & Westhof, E. (2002). Effects of magnesium ions on the stabilization of RNA oligomers of defined structures. RNA, 8, 307–323. Réblová, K., Špačková, N., Koča, J., Leontis, N. B., & Šponer, J. (2004). Long-residency hydration, cation binding, and dynamics of loop E/helix IV rRNA-L25 protein complex. Biophysical Journal, 87, 3397–3412.
Microscopy and Microanalysis | 2011
David A. Scheiblin; Kirk J. Czymmek; Y Wang; M Duncan
Extended abstract of a paper presented at Microscopy and Microanalysis 2011 in Nashville, Tennessee, USA, August 7–August 11, 2011.
Human Genetics | 2015
Smriti A. Agrawal; Deepti Anand; Archana D. Siddam; Atul Kakrana; Soma Dash; David A. Scheiblin; Christine A. Dang; Anne M. Terrell; Stephanie Waters; Abhyudai Singh; Hozumi Motohashi; Masayuki Yamamoto; Salil A. Lachke
The International Journal of Biochemistry & Cell Biology | 2014
David A. Scheiblin; Junyuan Gao; Jeffrey L. Caplan; Vladimir N. Simirskii; Kirk J. Czymmek; Richard T. Mathias; Melinda K. Duncan
Investigative Ophthalmology & Visual Science | 2014
Melinda K. Duncan; Fahmy A. Mamuya; Corinne Elaine Decker; Megan Fisher; Shaukat Khan; Victoria Roop; David A. Scheiblin; Vladimir N. Simirskii; Takeshi Tsuda
Investigative Ophthalmology & Visual Science | 2014
Carrie Ellen Barnum; Shaili Patel; David A. Scheiblin; Shawn W. Polson; Shinichiro Chuma; David C. Beebe; Salil A. Lachke