@article{pittman_macmillan-crow_peters_allen_2002, title={Nitration of manganese superoxide dismutase during ocular inflammation}, volume={74}, ISSN={["0014-4835"]}, DOI={10.1006/exer.2002.1141}, abstractNote={Reactive nitrogen species, in particular, peroxynitrite (ONOO(-)) have been proposed to play an important role in the pathogenesis of endotoxin-induced uveitis (EIU). Tyrosine nitration by ONOO(-) has been shown in other model systems to inhibit the activity of the superoxide anion quenching enyzme, manganese superoxide dismutase (MnSOD), perhaps contributing to progression of disease. In this study, it is confirmed through immunoanalysis that nitrated proteins are produced during EIU, and furthermore, that MnSOD is a target of nitration during the inflammatory response. In addition, through microsequencing analyses, nitrated albumin--apparent in both control and EIU eyes--was identified. Positive immunostaining of nitrated proteins was seen in the ciliary epithelium, inflammatory cells, and protein exudate of eyes from rats injected with endotoxin. Incubation of nitrotyrosine immunoprecipitates from the iris and ciliary body (ICB) with a polyclonal antibody against MnSOD revealed that nitrated MnSOD was present only in the ICB of EIU rats. When the total activity of the enzyme was examined, it was observed that despite the presence of nitrated MnSOD, activity was increased relative to control. Analysis of MnSOD mRNA and protein from the ICB of both groups demonstrated an increase in mRNA expression and consequently a three- to five-fold increase in MnSOD protein in EIU rats as compared to control rats. Further examination of MnSOD protein expression through immunohistochemistry noted enhanced immunostaining in the ciliary epithelium of eyes of EIU rats. Additional investigation of a 70 kDa band apparent in nitrotyrosine immunoprecipitates from the ICB of control and EIU rats revealed that the plasma protein albumin is nitrated as well. This protein is present as a result of the breakdown of the blood-aqueous barrier during inflammation. In summary, two endogenous nitration targets, albumin and MnSOD, were identified. Nitrated MnSOD appears to be specifically targeted to the ICB during inflammation, underscoring the importance of the interface in EIU. Furthermore, the expression and activity of the enzyme is increased in the ICB during EIU, perhaps regulating reactive nitrogen species produced within the cells. This study implicates ONOO(-) in the pathogenesis of EIU and imparts the putative role MnSOD plays in disease resolution.}, number={4}, journal={EXPERIMENTAL EYE RESEARCH}, author={Pittman, KM and MacMillan-Crow, LA and Peters, BP and Allen, JB}, year={2002}, month={Apr}, pages={463–471} }
 @article{sannes_khosla_peters_1997, title={Biosynthesis of sulfated extracellular matrices by alveolar type II cells increases with time in culture}, volume={273}, ISSN={["1040-0605"]}, DOI={10.1152/ajplung.1997.273.4.l840}, abstractNote={The aim of this study was to determine the extent to which sulfate incorporated into biosynthesized basement membrane (BM) components increased as isolated type II cells progress toward a more type I cell-like phenotype from 7 to 21 days in culture. Specific sulfate cytochemistry, using high iron diamine, showed that type I-like cells in 21-day cultures deposited a more highly sulfated extracellular matrix. Biosynthetic labeling experiments using [35S]cysteine or [35S]sulfate as precursors confirmed the increased capacity of 21-day type I-like cells to biosynthesize sulfated BM components compared with type II-like cells in 7-day cultures, including a novel sulfated laminin. These biochemical changes in sulfation of BM components coincide with the established phenotypic transition from type II to type I cells during prolonged culture. More importantly, the data suggest that regulation of sulfation constitutes a potential mechanism by which type I and type II cells alter their environment in such a manner as to stabilize phenotype and modulate responses to growth factors.}, number={4}, journal={AMERICAN JOURNAL OF PHYSIOLOGY-LUNG CELLULAR AND MOLECULAR PHYSIOLOGY}, author={Sannes, PL and Khosla, J and Peters, BP}, year={1997}, month={Oct}, pages={L840–L847} }
 @article{zhang_peters_monteiroriviere_1995, title={ASSESSMENT OF SULFUR MUSTARD INTERACTION WITH BASEMENT-MEMBRANE COMPONENTS}, volume={11}, ISSN={["1573-6822"]}, url={http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:A1995RM25300003&KeyUID=WOS:A1995RM25300003}, DOI={10.1007/bf00767494}, abstractNote={Bis-2-chloroethyl sulfide (sulfur mustard, HD) is a bifunctional alkylating agent which causes severe vesication characterized by slow wound healing. Our previous studies have shown that the vesicant HD disrupts the epidermal-dermal junction at the lamina lucida of the basement membrane. The purpose of this study was to examine whether HD directly modifies basement membrane components (BMCs), and to evaluate the effect of HD on the cell adhesive activity of BMCs. EHS laminin was incubated with [14C]HD, and extracted by gel filtration. Analysis of the [14C]HD-conjugated laminin fraction by a reduced sodium dodecyl sulfate-polyacrylaminde gel electrophoresis (SDS-PAGE) revealed the incorporation of radioactivity into both laminin subunits and a laminin trimer resistant to dissociation in reduced SDS-PAGE sample buffer, suggesting direct alkylation and cross-linking of EHS laminin by [14C]HD. Normal human foreskin epidermal keratinocytes were biosynthetically labeled with [35S]cysteine. 35S-labeled laminin isoforms, Ae.B1e.B2e. laminin and K.B1e.B2e. laminin (using the nomenclature of Engel), fibronectin, and heparan sulfate proteoglycan were isolated by immunoprecipitation from the cell culture medium, treated with HD or ethanol as control, and then analyzed by SDS-PAGE. On reduced SDS gels, these three BMCs not treated with HD showed the typical profile of dissociated subunits. However, HD treatment caused the appearance of higher molecular weight bands indicative of cross-linking of subunits within these BMCs. The HD scavengers sodium thiosulfate and cysteine prevented the cross-linking of BMC subunits by HD. Finally, tissue culture dishes coated with laminin or fibronectin were treated with HD or ethanol as a control, and human keratinocytes were plated on the BMC-coated surfaces. After 20 h of incubation, it was observed that cell adhesion was decreased significantly on the BMC-coated surfaces treated with HD. As expected, the preincubation of HD with cysteine diminished the HD inhibition of cell adhesion. Thus, HD alkylates adhesive macromolecules of the basement membrane zone and inhibits their cell adhesive activity. These findings support the hypothesis that the alkylation of basement membrane components by HD destabilizes the epidermal-dermal junction in the process of HD-induced vesication. The failure of the HD-alkylated BMCs to support the attachment of keratinocytes might also contribute to the slow reepithelialization of the wound site which is characteristic of HD-induced blistering.}, number={2}, journal={CELL BIOLOGY AND TOXICOLOGY}, author={ZHANG, Z and PETERS, BP and MONTEIRORIVIERE, NA}, year={1995}, month={Apr}, pages={89–101} }
 @article{king_peters_a._1994, title={Matrix molecules of the epidermal basement membrane as targets for chemical vesication with lewisite}, volume={126}, journal={Toxicology and Applied Pharmacology}, author={King, J. R. and Peters, B. P. and A., Monteiro-Riviere N.}, year={1994}, pages={164–173} }
 @article{vaden_page_peters_cline_riviere_1993, title={Development and characterization of an isolated and perfused tumor and skin preparation for evaluation of drug disposition}, volume={53}, journal={Cancer Research}, author={Vaden, S. L. and Page, R. L. and Peters, B. P. and Cline, J. M. and Riviere, J. E.}, year={1993}, pages={101–105} }
 @article{sannes_peters_adler_1991, title={Specific interactions with extracellular matrix may influence epithelial repair mechanisms in the pulmonary alveolus.}, volume={99}, journal={Chest}, author={Sannes, P. and Peters, B. and Adler, K.}, year={1991}, pages={70S–71} }
 @article{adler_peters_krunkosky_sannes_1990, title={Interactions between extracellular matrix, airway and alveolar epithelium: alterations in fibrosis and possible pathogenetic significance.}, volume={6}, journal={Proceedings of the Sixth International Colloquium Pulmonary Fibrosis.}, author={Adler, K. B. and Peters, B. P. and Krunkosky, T. and Sannes, P. L.}, year={1990}, pages={39} }
 @article{sannes_peters_adler_1990, title={Specific interactions with extracellular matrix may influence epithelial repair mechanisms in the pulmonary alveolus.}, volume={30}, journal={Proceedings of the 30th Aspen Lung Conference.}, author={Sannes, P. and Peters, B. and Adler, K.}, year={1990}, pages={24} }