@article{leiner_newman_li_walsh_khosla_sannes_2006, title={Heparin and fibroblast growth factors affect surfactant protein gene expression in type II cells}, volume={35}, DOI={10.1165/rcmb.2006-01590C}, number={5}, journal={American Journal of Respiratory Cell and Molecular Biology}, author={Leiner, K. A. and Newman, D. and Li, C. M. and Walsh, E. and Khosla, J. and Sannes, P. L.}, year={2006}, pages={611–618} }
 @article{newman_li_simmons_khosla_sannes_2004, title={Heparin affects signaling pathways stimulated by fibroblast growth factor-1 and-2 in type II cells}, volume={287}, ISSN={["1522-1504"]}, DOI={10.1152/ajplung.00284.2003}, abstractNote={Undersulfation of the basement membrane matrix of alveolar type II (AT2) cells compared with that of neighboring type I cells is believed to account for some of the known morphological and functional differences between these pneumocytes. Heparin, a model for sulfated components of basement membrane matrices, is known to inhibit fibroblast growth factor (FGF)-2-stimulated DNA synthesis as well as gene expression of FGF-2 and its receptor in AT2 cells. To determine whether these end points result from specific effects of heparin on FGF-related signaling pathways, isolated rat AT2 cells were treated with 100 ng/ml FGF-1 or FGF-2 in the presence of up to 500 μg/ml heparin. In addition, experiments were done on cells grown in the presence of 20 mM sodium chlorate (sulfation inhibitor). High-dose heparin reduced FGF-1- or FGF-2-stimulated phosphorylation of mitogen-activated protein kinase kinases (MEK1/2), p44/42 mitogen-activated protein kinases (MAPK/ERK1/2), stress-activated protein kinase/c-Jun NH2-terminal kinase, Akt/protein kinase B, and p90RSK. FGF-2-stimulated signaling was more sensitive to heparin's effects than was signaling stimulated by FGF-1. Heparin had an additive effect on the reduced [3H]thymidine incorporation in FGF-2-treated AT2 cells caused by inhibition of the MEK/ERK pathway by the MEK inhibitor PD-98059. The data suggest that heparin's known capacity to alter DNA synthesis and, possibly, other biological end points is realized via cross talk between multiple signaling pathways.}, number={1}, journal={AMERICAN JOURNAL OF PHYSIOLOGY-LUNG CELLULAR AND MOLECULAR PHYSIOLOGY}, author={Newman, DR and Li, CM and Simmons, R and Khosla, J and Sannes, PL}, year={2004}, month={Jul}, pages={L191–L200} }
 @article{li_newman_cesta_tompkins_khosla_sannes_2003, title={Modulation of fibroblast growth factor expression and signal transduction in type II cells}, volume={123}, ISSN={["0012-3692"]}, DOI={10.1378/chest.123.3_suppl.429S}, abstractNote={repair and wound healing. PDGFs are synthesized and secreted by most inflammatory cell types present within the milieu of the asthmatic airway. We have previously reported that airway fibroblasts from severe asthmatics produce more type I procollagen in response to PDGF stimulation as compared to patients with mild asthma and normal control subjects; therefore, we hypothesized that the enhanced responsiveness to PDGFs in patients with severe asthma is linked to an increased expression of PDGF receptors. In an ongoing study, 5 subjects with severe asthma, 10 subjects with mild-to-moderate asthma, and 6 normal control subjects underwent bronchoscopy with endobronchial biopsy. Biopsies were placed in Dulbecco’s modified Eagle’s serum supplemented with fetal bovine serum (10%), streptomycin (100 g/mL), penicillin (10,000 U/mL), and gentamicin (100 g/mL), and cultured until fibroblast growth was established at 50% confluency (approximately 8 to 20 days). Immunostaining with vimentin (Dako; Carpenteria, CA), Ab-1 (Calbiochem; San Diego, CA) and -smooth muscle actin (Dako) confirmed fibroblast identity. To determine baseline fibroblast expression of PDGF receptors (PDGFRs) [PDGFRand PDGFR], we developed a sandwich enzyme-linked immunosorbent assay for these receptors that quantifies receptor protein levels in fibroblast cell lysates. Receptor protein levels were expressed in nanograms per 100 g of total cell protein. There were no significant differences in baseline expression of PDGFRbetween the groups (severe, 7.6 ng/100 g protein; mild to moderate, 12.50 ng/100 g protein; normal control, 11.33 ng/100 g protein; p 0.35). However, there was a significantly greater baseline expression of PDGFRin the severe asthmatic group, as compared to both the mild/moderate asthmatic and normal control groups (severe, 15.20 ng/100 g protein; mild-to-moderate, 13.30 ng/100 g protein; normal control, 3.67 ng/100 g protein; p 0.0024). Our data suggests that airway fibroblasts from severe asthmatics may be of a synthetic phenotype, with altered capabilities in collagen production, as compared to those from patients with mild-to-moderate asthma and normal control subjects, and this may be driven by an increased expression of PDGFR. Modulation of Fibroblast Growth Factor Expression and Signal Transduction in Type II Cells*}, number={3}, journal={CHEST}, author={Li, CM and Newman, D and Cesta, M and Tompkins, L and Khosla, J and Sannes, PL}, year={2003}, month={Mar}, pages={429S–429S} }
 @article{pagan_khosla_li_sannes_2002, title={Effect of growth factor-fibronectin matrix interaction on rat type II cell adhesion and DNA synthesis}, volume={28}, ISSN={["0190-2148"]}, DOI={10.1080/019021402753462013}, abstractNote={Type II cells attach, migrate, and proliferate on a provisional fibronectin-rich matrix during alveolar wall repair after lung injury. The combination of cell-substratum interactions via integrin receptors and exposure to local growth factors are likely to initiate the signals required for cell proliferation, differentiation, reepithelialization, and ultimate restoration of the alveolar wall structure. Accordingly, primary cultured type II cells have been shown to bind fibronectin, in part through the α 5 β 1 integrin, and to respond to growth factors that induce type II cell proliferation, such as fibroblast growth factor 1 (FGF-1). The purpose of this study was to determine whether or not FGF-1 modifies type II cell attachment to fibronectin, and if together they affect DNA synthesis. Attachment assays showed that FGF-1 treatment enhanced type II cell adhesion to fibronectin. This effect correlated with an increase in β 1 integrin cell surface expression, and with the formation of cytoskeletal stabilizing structures such as lamellipodial extensions and stress fibers. FGF-1 also induced an increase in thymidine in corporation into DNA. Together FGF-1 and fibronectin appear to promote adhesion, cytoskeletal organization, and in creased DNA synthesis, and in this way influence cell-substratum interactions and signaling during alveolar repair.}, number={2}, journal={EXPERIMENTAL LUNG RESEARCH}, author={Pagan, I and Khosla, J and Li, CM and Sannes, PL}, year={2002}, month={Mar}, pages={69–84} }
 @article{li_newman_khosla_sannes_2002, title={Heparin inhibits DNA synthesis and gene expression in alveolar type II cells}, volume={27}, ISSN={["1535-4989"]}, DOI={10.1165/rcmb.2002-0002OC}, abstractNote={Responses of isolated type II alveolar cells to fibroblast growth factors (FGF) have been shown to be sensitive to the level of sulfation in extracellular matrix (ECM) substrata. These observations may reflect the specific in situ distribution and level of sulfation of ECM within the alveolar basement membranes (ABM) associated with type II cells. The goal of this study was to determine if the model sulfated ECM heparin modified DNA synthesis and gene expression by type II cells in a concentration dependent-manner. Isolated rat type II cells were exposed to different concentrations of heparin (0.005-500 micro g/ml) in serum-free medium for 1-3 d with or without FGF-1 or FGF-2. The effects of heparin were examined by [(3)H]thymidine incorporation into DNA, total cell protein, cell number, and selected gene expression. Results indicated that heparin inhibited [(3)H]thymidine uptake in a concentration-dependent manner. Total protein, cell number, and FGF-2 protein expression and mRNA of FGF-1, -2, and FGF receptor-2 detected by reverse transcriptase-polymerase chain reaction were decreased by heparin. These results demonstrate that sulfated molecules in the ABM may play important regulatory role(s) in selected type II cell activities during normal cell homeostasis, turnover, and repair after lung injury.}, number={3}, journal={AMERICAN JOURNAL OF RESPIRATORY CELL AND MOLECULAR BIOLOGY}, author={Li, CM and Newman, D and Khosla, J and Sannes, PL}, year={2002}, month={Sep}, pages={345–352} }
 @article{li_khosla_hoyle_sannes_2001, title={Transforming growth factor-beta(1) modifies fibroblast growth factor-2 production in type II cells}, volume={120}, ISSN={["0012-3692"]}, DOI={10.1378/chest.120.1_suppl.S60}, abstractNote={Transforming growth factor (TGF)-β 1 is an inflammatory cytokine that plays multiple roles in pulmonary fibrosis. In vascular epithelium, it has been shown to regulate production and activity of fibroblast growth factor (FGF)-2, a potent type II cell mitogen in the lung. Such a relationship could have important consequences in prefibrotic change in the lung alveolus, where reepithelialization of alveolar surfaces is crucial. The goal of this study was to determine if FGF-2 production by alveolar type II cells is modulated by TGF-β 1 or FGF-1, another type II cell mitogen. Isolated rat type II cells were exposed to 0 to 40 ng/mL of TGF-β 1 or 0 to 500 ng/mL of FGF-1 in serum-free medium for 1 to 3 days. Using a specific immunoassay, significant increases in FGF-2 protein in type II cell lysates were achieved after 1 day of exposure to 100 ng/mL of FGF-1 and after 3 days of treatment with 8 ng/mL of TGF-β 1 . Similarly, transcripts for FGF-2 were dramatically increased with TGF-β 1 or FGF-1, as were those for FGF receptor (FGFR)-1. These interactions were dramatically effected by the addition of heparin, a model sulfated extracellular matrix (ECM). Heparin as low as 0.01 mg/mL significantly downregulated expression of TGF-β 1 and FGF-1–stimulated FGF-2 and FGFR-1. These results demonstrate important regulatory links between FGF-2, sulfated ECMs, and both TGF-β 1 and FGF-1, which could contribute to the modulation of normal cell turnover, development, and repair processes attendant to fibrosis in the lung.}, number={1}, journal={CHEST}, author={Li, CM and Khosla, J and Hoyle, P and Sannes, PL}, year={2001}, month={Jul}, pages={60S–61S} }
 @article{li_khosla_pagan_hoyle_sannes_2000, title={TGF-beta 1 and fibroblast growth factor-1 modify fibroblast growth factor-2 production in type II cells}, volume={279}, ISSN={["1040-0605"]}, DOI={10.1152/ajplung.2000.279.6.l1038}, abstractNote={ Fibroblast growth factor (FGF)-2, which stimulates DNA synthesis by type II cells in the lung, has been shown to be regulated by transforming growth factor (TGF)-β1, an important inflammatory cytokine, in vascular epithelium. The goal of this study was to determine if FGF-2 production by alveolar type II cells is modulated by TGF-β1 or FGF-1, which also stimulates DNA synthesis by type II cells. Isolated rat type II cells were exposed to 0–40 ng/ml of TGF-β1 or 0–500 ng/ml of FGF-1 in serum-free medium for 1–5 days. With a specific immunoassay, significant increases of FGF-2 protein in type II cell lysates to levels above those in control cells were achieved after 1 day of exposure to 100 ng/ml of FGF-1 and after 3 days of treatment with 8 ng/ml of TGF-β1. Similarly, transcripts for FGF-2 were dramatically increased above those in control cells with TGF-β1 or FGF-1, as were those for FGF receptor-1. These results demonstrate important regulatory links between FGF-2 and both TGF-β1 and FGF-1 in the alveolar epithelium that could contribute to the regulation of normal cell turnover, development, and the repair processes after injury in the lung. }, number={6}, journal={AMERICAN JOURNAL OF PHYSIOLOGY-LUNG CELLULAR AND MOLECULAR PHYSIOLOGY}, author={Li, CM and Khosla, J and Pagan, I and Hoyle, P and Sannes, PL}, year={2000}, month={Dec}, pages={L1038–L1046} }
 @article{li_joshee_adler_cheng_1999, title={Development of monoclonal antibodies against bovine mucin core 2 beta 6 N-acetylglucosaminyltransferase}, volume={16}, ISSN={["1573-4986"]}, DOI={10.1023/A:1007030223118}, abstractNote={Molecular cloning techniques have been used to produce abundant amounts of recombinant glycosyltransferases for biochemical studies. We recently cloned a cDNA which encoded bovine mucin core 2 beta6N-acetylglucosaminyl transferase (C2TF). Poly-histidine-C2TF fusion protein was generated from the cloned cDNA in the E. coli Xpress system and used to produce monoclonal antibodies (MAbs). We obtained seven hybridomas which secreted MAbs against bovine C2TF in mouse ascites with titers ranging from 1:1280 to 1:40960 as assessed by immunofluorescence assay (IF). Isotyping revealed that all seven MAbs were IgG (4 IgG1, 2 IgG2b and 1 IgG2a). The affinity constants (M(-1)) for these MAbs range from 5.4 x 10(7) to 1.2 x 10(9). These MAbs recognized bovine C2TF in tissue sections and on Western blottings. Six of these MAbs reacted with human core 2-M enzyme and one with both core 2-L and core 2-M enzymes on Western blottings. Therefore, these antibodies should be useful for further study of bovine and human core 2 enzymes.}, number={9}, journal={GLYCOCONJUGATE JOURNAL}, author={Li, CM and Joshee, N and Adler, KB and Cheng, PW}, year={1999}, month={Sep}, pages={555–562} }
 @inbook{fischer_li_li_choe_wright_rochelle_adler_1998, title={Intracellular regulation of airway mucin secretion.}, booktitle={Cilia, mucus and mucociliary interactions}, author={Fischer, B. M. and Li, C. and Li, H. and Choe, N. and Wright, D. T. and Rochelle, L. G. and Adler, K. B.}, year={1998}, pages={143–151} }
 @article{li_adler_cheng_1998, title={Mucin biosynthesis: Molecular cloning and expression of bovine lung mucin core 2 N-acetylglucosaminyltransferase cDNA}, volume={18}, ISSN={["1044-1549"]}, DOI={10.1165/ajrcmb.18.3.2593}, abstractNote={A cDNA clone containing a 2,150-bp insert was isolated from a bovine lung lambdagt10 cDNA library by cross-species hybridization using a DNA probe generated by polymerase chain reaction (PCR) employing a human cDNA that encodes mucin core 2 beta6-N-acetylglucosaminyltransferase (hC2TF) as the template. The bovine cDNA (bcDNA) insert was devoid of 220 bp of the 5' portion of the C2TF open reading frame (ORF), as predicted from the human counterpart. Southern blotting analysis suggested that the coding region of this C2TF gene is in one exon. To construct a full-length bovine C2TF (bC2TF) cDNA, a genomic DNA fragment containing the 5' portion of the ORF of the bC2TF gene was cloned from a lambdaEMBL bovine genomic DNA library and ligated to the 5' end of the cloned cDNA insert. DNA sequence analysis showed that the complete ORF of bC2TF gene was 1,281 bp in length, which corresponds to a polypeptide of 427 amino acids. Catalytically active bC2TF was expressed in sf21 insect cells infected with recombinant baculovirus containing the ORF of the bC2TF gene. The recombinant bC2TF catalyzed the synthesis of core 2, but not core 4 and blood group I structures. Western blotting analysis showed that the recombinant bC2TF migrated with the same mobility (approximately 55 kD) as the native bovine tracheal C2TF. Immunohistochemical analysis showed that in bovine trachea, the bC2TF was present at the surface epithelium and in the submucosal glands, with the latter being the major site of distribution.}, number={3}, journal={AMERICAN JOURNAL OF RESPIRATORY CELL AND MOLECULAR BIOLOGY}, author={Li, CM and Adler, KB and Cheng, PW}, year={1998}, month={Mar}, pages={343–352} }
 @article{sannes_khosla_li_pagan_1998, title={Sulfation of extracellular matrices modifies growth factor effects on type II cells on laminin substrata}, volume={275}, ISSN={["1040-0605"]}, DOI={10.1152/ajplung.1998.275.4.l701}, abstractNote={The alveolar basement membrane contains a variety of extracellular matrix (ECM) molecules, including laminin and sulfated glycosaminoglycans of proteoglycans. These mixtures exist within microdomains of differing levels of sulfate, which may specifically interact to be key determinants of the known capacity of the type II cell to respond to certain growth factors. Isolated type II cells were exposed to either acidic fibroblast growth factor (FGF-1), basic fibroblast growth factor (FGF-2), or keratinocyte growth factor (KGF; FGF-7) on culture wells precoated with laminin alone or in combination with chondroitin sulfate (CS), high-molecular-weight heparin, or their desulfated forms. Desulfated heparin significantly elevated FGF-1- and FGF-2-stimulated DNA synthesis, whereas desulfated CS and N-desulfated heparin elevated FGF-7-stimulated DNA synthesis by type II cells on laminin substrata. When FGF-1 was mixed into the various test matrix substrata, DNA synthesis was significantly increased in all cases. These results demonstrated that decreased levels of sulfate in ECM substrata act to upregulate responses to heparin-binding growth factors by alveolar epithelial cells on laminin substrata.}, number={4}, journal={AMERICAN JOURNAL OF PHYSIOLOGY-LUNG CELLULAR AND MOLECULAR PHYSIOLOGY}, author={Sannes, PL and Khosla, J and Li, CM and Pagan, I}, year={1998}, month={Oct}, pages={L701–L708} }
 @inbook{wright_li_fischer_yagaloff_adler_1997, title={Interactions between oxidant gases and airway epithelial cells; in vitro in vivo correlations.}, booktitle={Correlations between in vitro and in vivo investigations in inhalation toxicology.}, author={Wright, D. T. and Li, C. M. and Fischer, B. M. and Yagaloff, K. and Adler, K. B.}, year={1997}, pages={216–229} }
 @article{adler_li_li_choe_fischer_1997, title={Intracellular regulation of mucin secretion.}, journal={Proceedings of the International Congress on Cilia, Mucus and Mucociliary Interations.}, author={Adler, K. B. and Li, C. M. and Li, H. F. and Choe, N. and Fischer, B. M.}, year={1997}, pages={15} }
 @article{cheng_li_adler_1997, title={Molecular cloning and expression of a mucin core 2 N-acetylglucosaminyltransferase cDNA.}, volume={155}, journal={American Journal of Respiratory and Critical Care Medicine}, author={Cheng, P. W. and Li, C. M. and Adler, K. B.}, year={1997}, pages={A434} }
 @article{adler_wright_li_li_choe_rochell_fischer_1996, title={Nitric oxide: A key signaling molecule regulating airway mucin secretion.}, volume={9}, journal={Proceedings of the 9th World Congress on Bronchology & World Congress on Bronchoesophagology.}, author={Adler, K. B. and Wright, D. T. and Li, C. and Li, H. and Choe, N. and Rochell, L. G. and Fischer, B. M.}, year={1996}, pages={S060} }
 @article{wright_fischer_li_rochelle_akley_adler_1996, title={Oxidant stress stimulates mucin secretion and PLG in airway epithelium via a nitric oxide-dependent mechanism}, volume={271}, ISSN={["1040-0605"]}, DOI={10.1152/ajplung.1996.271.5.l854}, abstractNote={ Reactive oxygen species (ROS) have been implicated in the pathogenesis of a wide variety of respiratory diseases. We investigated mechanisms of ROS-induced mucin secretion by guinea pig tracheal epithelial (GPTE) cells in primary culture, and ROS-induced activation of the second messenger-producing enzyme phospholipase C (PLC), in GPTE cells and in a virally transformed cell line (BEAS-2B) derived from human bronchial epithelium. Mucin secretion was measured by a monoclonal antibody-based enzyme-linked immunosorbent assay, and PLC activation was assessed by anion exchange chromatography. ROS generated enzymatically by xanthine oxidase (XO, 500 microM) in the presence of purine (500 microM) enhanced release of mucin by GPTE cells and activated PLC in GPTE and BEAS cells. Hypersecretion of mucin and activation of PLC in response to purine + XO appeared to occur via an intracellular pathway(s) dependent on endogenously produced nitric oxide and possibly intracellularly generated oxidants. Both responses could be blocked or attenuated by preincubation of the cells with NG-monomethyl-L-arginine, an inhibitor of the enzyme nitric oxide synthase, or with dimethylthiourea, a compound that can react with a variety of intracellular oxidant species. Reactive nitrogen species generated chemically also stimulated secretion of mucin and activated PLC via a mechanism dependent (at least in part) on intracellular oxidant-mediated process(es). The results suggest that intracellularly generated radical species of nitrogen and oxygen may be important modulators of the response of airway epithelial cells to external oxidant stress. }, number={5}, journal={AMERICAN JOURNAL OF PHYSIOLOGY-LUNG CELLULAR AND MOLECULAR PHYSIOLOGY}, author={Wright, DT and Fischer, BM and Li, CM and Rochelle, LG and Akley, NJ and Adler, KB}, year={1996}, month={Nov}, pages={L854–L861} }
 @article{fischer_wright_li_li_cohn_akley_adler_1995, title={Endogenously-generated nitric oxide (NO) may be a key signaling molecule in hypersecretion of mucin by guinea pig tracheal epithelial (GPTE) cells in vitro.}, volume={151}, journal={American Journal of Respiratory and Critical Care Medicine}, author={Fischer, B. M. and Wright, D. T. and Li, H. and Li, C. M. and Cohn, L. A. and Akley, N. J. and Adler, K. B.}, year={1995}, pages={A337} }
 @article{wright_li_fischer_akley_adler_1995, title={Reactive nitrogen species (RNS) stimulate secretion of mucin by primary cultures of guinea pig tracheal epithelial (GPTE) cells.}, volume={151}, journal={American Journal of Respiratory and Critical Care Medicine}, author={Wright, D. T. and Li, C. M. and Fischer, B. M. and Akley, N. J. and Adler, K. B.}, year={1995}, pages={A337} }
 @article{adler_wright_fischer_cohn_li_li_choe_akley_1994, title={Effects of oxidant stress on airway epithelial cells in vitro.}, volume={8}, journal={FASEB Journal}, author={Adler, K. B. and Wright, D. T. and Fischer, B. M. and Cohn, L. A. and Li, C. and Li, H. and Choe, N. H. and Akley, N. J.}, year={1994}, pages={A896} }
 @article{wright_cohn_li_fischer_li_adler_1994, title={Interactions of oxygen radicals with airway epithelium.}, volume={102}, DOI={10.1289/ehp.94102s1085}, abstractNote={Reactive oxygen species (ROS) have been implicated in the pathogenesis of numerous disease processes. Epithelial cells lining the respiratory airways are uniquely vulnerable regarding potential for oxidative damage due to their potential for exposure to both endogenous (e.g., mitochondrial respiration, phagocytic respiratory burst, cellular oxidases) and exogenous (e.g., air pollutants, xenobiotics, catalase negative organisms) oxidants. Airway epithelial cells use several nonenzymatic and enzymatic antioxidant mechanisms to protect against oxidative insult. Nonenzymatic defenses include certain vitamins and low molecular weight compounds such as thiols. The enzymes superoxide dismutase, catalase, and glutatione peroxidase are major sources of antioxidant protection. Other materials associated with airway epithelium such as mucus, epithelial lining fluid, and even the basement membrane/extracellular matrix may have protective actions as well. When the normal balance between oxidants and antioxidants is upset, oxidant stress ensues and subsequent epithelial cell alterations or damage may be a critical component in the pathogenesis of several respiratory diseases. Oxidant stress may profoundly alter lung physiology including pulmonary function (e.g., forced expiratory volumes, flow rates, and maximal inspiratory capacity), mucociliary activity, and airway reactivity. ROS may induce airway inflammation; the inflammatory process may serve as an additional source of ROS in airways and provoke the pathophysiologic responses described. On a more fundamental level, cellular mechanisms in the pathogenesis of ROS may involve activation of intracellular signaling enzymes including phospholipases and protein kinases stimulating the release of inflammatory lipids and cytokines. Respiratory epithelium may be intimately involved in defense against, and pathophysiologic changes invoked by, ROS.}, number={11}, journal={Environmental Health Perspectives. Supplements}, author={Wright, D. T. and Cohn, L. A. and Li, H. and Fischer, B. M. and Li, C. M. and Adler, K. B.}, year={1994}, pages={85–90} }
 @article{li_cheng_adler_1994, title={PRODUCTION AND CHARACTERIZATION OF MONOCLONAL-ANTIBODIES AGAINST GUINEA-PIG TRACHEAL MUCINS}, volume={13}, ISSN={["0272-457X"]}, DOI={10.1089/hyb.1994.13.281}, abstractNote={Thirty-five hybridomas that secrete mouse monoclonal antibodies (MAb) against guinea pig (G.P.) tracheal mucins were established. The MAbs were characterized immunologically, biochemically, and immunohistochemically at both light and electron microscopic levels. Isotyping of the MAbs revealed 14 to be IgM, 13 IgG1, 3 IgG2, and 5 IgG3. The MAbs demonstrated various patterns of binding in immunoblots against mucins derived from G.P. tracheal explants. This suggested the presence of "subpopulations" of G.P. tracheal mucins with specific MAbs binding to different epitopes on the mucin molecules. Periodate oxidation indicated that 33 of the 35 MAbs recognized carbohydrate epitopes on the mucin molecules. Ten of the MAbs also reacted with both bovine and ferret tracheal mucins, while 7 and 6 MAbs bound only to bovine and ferret tracheal mucins, respectively. The generated MAbs should be useful for immunomeasurement of mucin secretion in vivo (e.g., in bronchoalveolar or airway lavage fluid) and in vitro (e.g., cell and organ cultures) from cells of guinea pig and (with certain MAbs) bovine and ferret origin.}, number={4}, journal={HYBRIDOMA}, author={LI, CM and CHENG, PW and ADLER, KB}, year={1994}, month={Aug}, pages={281–287} }