@article{li_martin_minnicozzi_greenfeder_fine_pettersen_chorley_adler_2001, title={Enhanced expression of mucin genes in a guinea pig model of allergic asthma}, volume={25}, ISSN={["1535-4989"]}, DOI={10.1165/ajrcmb.25.5.4485}, abstractNote={The ovalbumin (OVA)-sensitized guinea pig is often used as an animal model of asthma and airway hyperreactivity. A characteristic lesion of asthma is excessive production of mucin in the airways. Mechanistic studies of this lesion in guinea pigs have been limited due to lack of mucin gene probes for this species. The aim of the present study was to clone the cDNAs encoding two major airway mucins (Muc2 and Muc5ac) from the guinea pig, and investigate mucin gene expression in lungs of sensitized animals in response to antigen challenge. We isolated and sequenced two cDNA fragments coding for the sequences located within the carboxyl-terminal cysteine-rich region of guinea pig Muc2 and Muc5ac mucins. Comparison of cloned cDNAs with those from other species revealed high degrees of sequence identity and conservation of all cysteine residues in deduced primary sequences. Based on the resultant sequence information, we also designed oligonucleotide primers for specific detection of guinea-pig Muc2 and Muc5ac steady-state mRNA levels via reverse transcriptase/ polymerase chain reaction (RT-PCR). Levels of both Muc2 and Muc5ac mRNA in lungs of OVA-sensitized guinea pigs increased significantly by 30 min after an acute exposure to 0.3% OVA. In addition, levels of eotaxin mRNA also increased in these tissues, but the increases were not significant until 2 h after challenge. Correspondingly, the number of eosinophils in bronchoalveolar lavage fluid did not increase until 4 h postchallenge. Results of these studies suggest that the OVA-sensitized guinea pig responds to allergic challenge with enhanced expression of genes (e.g., eotaxin, Muc2, and Muc5ac) that likely play a role in increased airway inflammation and mucin overproduction, and enhanced mucin gene expression appears to occur before eosinophil infiltration.}, number={5}, journal={AMERICAN JOURNAL OF RESPIRATORY CELL AND MOLECULAR BIOLOGY}, author={Li, YH and Martin, LD and Minnicozzi, M and Greenfeder, S and Fine, J and Pettersen, CA and Chorley, B and Adler, KB}, year={2001}, month={Nov}, pages={644–651} }
 @article{olivry_fine_dunston_chasse_tenorio_monteiro-riviere_chen_woodley_1998, title={Canine epidermolysis bullosa acquisita: circulating autoantibodies target the aminoterminal noncollagenous (NC1) domain of collagen VII in anchoring fibrils}, volume={9}, ISSN={["0959-4493"]}, url={http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000073123800004&KeyUID=WOS:000073123800004}, DOI={10.1046/j.1365-3164.1998.00067.x}, abstractNote={The classification of autoimmune blistering skin diseases is based on the skin antigen(s) targeted by pathogenic autoantibodies. In humans and dogs, there is increasing evidence that autoimmune subepidermal bullous diseases represent different nosological entities. This study establishes the existence of the canine equivalent of epidermolysis bullosa acquisita (EBA) in humans. Canine EBA, like the inflammatory variant of its human counterpart, is characterized by spontaneous vesicles arising from an inflammatory eruption. Dermo‐epidermal separation occurs in association with neutrophilic infiltration in the superficial dermis. Tissue‐fixed and circulating IgA and IgG autoantibodies specific for the lower basement membrane zone can be detected by immunofluorescence methods. Using immunoelectron microscopy, autoantibodies are shown to target the distal end of anchoring fibrils in the sublamina densa. ELISA and immunoblotting utilizing eukaryotically expressed recombinant collagen VII subdomains confirm that the circulating autoantibodies are specific for the aminoterminal globular non‐collagenous NC1 domain of type VII collagen.}, number={1}, journal={VETERINARY DERMATOLOGY}, author={Olivry, T and Fine, JD and Dunston, SM and Chasse, D and Tenorio, AP and Monteiro-Riviere, NA and Chen, M and Woodley, DT}, year={1998}, month={Mar}, pages={19–31} }
 @article{zhang_fine_monteiro-riviere_1998, title={Uncein may be a potential target for sulfur mustard alkylation}, volume={8}, ISSN={["1051-7235"]}, url={http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000074183400004&KeyUID=WOS:000074183400004}, DOI={10.1080/105172398243014}, abstractNote={Severe blister formation in theepidermal and dermal junction is one of the characteristic cutaneous lesions caused by bis-2-chloroethyl sulfide (sulfur mustard, HD), a bifunctional alkylating agent. Uncein is a newly discovered anchoring filament-associated antigen that has been shown to be undetectable in all forms of junctional epidermolysis bullosa, therefore suggesting its role in maintaining the integrity of the epidermal-dermal basement membrane zone. To test uncein as a potential target for HD alkylation in HD-induced vesication, uncein was biosynthetically labeled with 35 S-methionine and purified by immunoprecipitation with a 19-DEJ-1 monoclonal antibody from the medium of normal human keratinocyte (NHEK) cultures. The 3 5 S-labeled uncein was incubated with 50 muL of 10.0 mg/mL of HD in ethanol (ETOH) or ETOH, which served as the control in 50 mM Tris-Cl buffer (pH 7.4) for 2 h. In addition, 10.0 mg/mL of HD was incubated with uncein pretreated with 3 mM sodium thiosulfate, an HD scavenger. Unce...}, number={1}, journal={TOXICOLOGY METHODS}, author={Zhang, ZL and Fine, JD and Monteiro-Riviere, NA}, year={1998}, pages={27–36} }