A detailed analysis will be performed of the glycoprotein components of respiratory mucus. The major secretory macromolecule is responsible for maintenance of the reheologic properties of the mucus and apparently provides a vehicle whereby airway lipid components may be passively cleaned from the respiratory tract. Purification of the glycoprotein can be achieved by taking advantage of its high molecular weight (exclusion chromatography) and high buoyant density (density gradient centrifugation). Lipid removal by solvent extraction yields substantially homogeneous preparations from which the saccharide components can be completely removed by alkali catalyzed elimination in the presence of sodium borohydride. The oligosaccharides are clustered along the polypeptide chain and range in the size from 2-14 sugars. The attachment is via galactosamine to seryl or threonyl residues which comprise approximately one-half of the amino acids in the sugar rich domain. The macrostructure of the glycoprotein is maintained, in part, by disulfide cross links whose cleavage results in a substantial reduction in molecular weight. Lipid binding specificity and stoichiometry as well as the role of the disulfide bridges in exhibited physical properties will be examined.

National Institute of Health (NIH)
National Heart, Lung, and Blood Institute (NHLBI)
Research Project (R01)
Project #
Application #
Study Section
Physiological Chemistry Study Section (PC)
Project Start
Project End
Budget Start
Budget End
Support Year
Fiscal Year
Total Cost
Indirect Cost
Pennsylvania State University
Schools of Medicine
United States
Zip Code
Verma, M; Baraniuk, J; Blass, C et al. (1999) CFTR antisense phosphorothioate oligodeoxynucleotides (S-ODns) induce tracheo-bronchial mucin (TBM) mRNA expression in human airway mucosa. Glycoconj J 16:7-11
Verma, M; Blass, C; Davidson, E A (1997) Upregulation of the tracheobronchial mucin gene involves cyclic AMP response elements. Indian J Biochem Biophys 34:118-23
Verma, M; Blass, C; Davidson, E A (1996) Tracheo-bronchial mucin gene expression as detected by in situ hybridization. Glycobiology 6:141-5
Verma, M; Murthy, V V; Mathew, S et al. (1996) Promoter of the canine tracheobronchial mucin gene. Glycoconj J 13:797-807
Verma, M; Olnes, M J; Kurl, R N et al. (1995) Primary structure of the canine U1 snRNA. Gene 154:255-7
Culp, D J; Lee, D K; Penney, D P et al. (1992) Cat tracheal gland cells in primary culture. Am J Physiol 263:L264-75
Ringler, N J; Selvakumar, R; Woodward, H D et al. (1988) Protein components of human tracheobronchial mucin: partial characterization of a closely associated 65-kilodalton protein. Biochemistry 27:8056-63
Woodward, H D; Ringler, N J; Selvakumar, R et al. (1987) Deglycosylation studies on tracheal mucin glycoproteins. Biochemistry 26:5315-22
Ringler, N J; Selvakumar, R; Woodward, H D et al. (1987) Structure of canine tracheobronchial mucin glycoprotein. Biochemistry 26:5322-8
Bhavanandan, V P; Hegarty, J D (1987) Identification of the mucin core protein by cell-free translation of messenger RNA from bovine submaxillary glands. J Biol Chem 262:5913-7

Showing the most recent 10 out of 11 publications