Abstract
An antibody (PGM2B) recognizing a pig gastric-mucin apoprotein reacts with the surface epithelium of pig gastric mucosa. Virtually no reactivity was observed over the mucin-producing cells in the glands, which were recognized by the GlcNAc-selective Griffonia simplicifolia II (GSA-II) lectin. Mucins from the glandular tissue of the cardiac region, corpus and antrum were purified using isopycnic density-gradient centrifugation in CsCl/guanidinium chloride. In the cardiac region, two major mucin populations at 1.5 and 1.4 g/ml were identified. The high-density population reacted preferentially with the PGM2B antibody and resembled mucins from the surface epithelium of this region, whereas the low-density population reacted strongly with the GSA-II lectin and appeared to originate from the glands. In the glandular tissue of corpus, a component with strong GSA-II lectin reactivity, which was distinctly different from the surface mucins from this region, was found at 1.4 g/ml, thus resembling the gland component from the cardiac region. Mucins from antrum glandular tissue contained at least two GSA-II lectin-reactive populations banding at 1.5 and 1.4 g/ml, respectively. Gland mucins from all regions were large oligomeric glycoproteins and heterogeneous with respect to charge properties, as shown by using rate-zonal centrifugation and ion-exchange HPLC, respectively. Gel chromatography of mucin glycopeptides showed that gland mucins from antrum and corpus contained significantly longer glycosylated domains than those from the surface mucosa. Thus, mucins from pig gastric glandular tissue comprise a number of large and oligomeric glycoproteins that differ from those from the surface epithelium in buoyant density, apoprotein structure and carbohydrate substitution.
Full Text
The Full Text of this article is available as a PDF (714.6 KB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Allen A., Flemström G., Garner A., Kivilaakso E. Gastroduodenal mucosal protection. Physiol Rev. 1993 Oct;73(4):823–857. doi: 10.1152/physrev.1993.73.4.823. [DOI] [PubMed] [Google Scholar]
- Bara J., Decaens C., Loridon-Rosa B., Oriol R. Immunohistological characterization of mucin epitopes by pre-treatment of gastro-intestinal sections with periodic acid. J Immunol Methods. 1992 Apr 27;149(1):105–113. doi: 10.1016/s0022-1759(12)80054-8. [DOI] [PubMed] [Google Scholar]
- Bara J., Gautier R., Le Pendu J., Oriol R. Immunochemical characterization of mucins. Polypeptide (M1) and polysaccharide (A and Leb) antigens. Biochem J. 1988 Aug 15;254(1):185–193. doi: 10.1042/bj2540185. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bara J., Gautier R., Mouradian P., Decaens C., Daher N. Oncofetal mucin M1 epitope family: characterization and expression during colonic carcinogenesis. Int J Cancer. 1991 Jan 21;47(2):304–310. doi: 10.1002/ijc.2910470222. [DOI] [PubMed] [Google Scholar]
- Bara J., Gautier R., Mouradian P., Decaens C., Daher N. Oncofetal mucin M1 epitope family: characterization and expression during colonic carcinogenesis. Int J Cancer. 1991 Jan 21;47(2):304–310. doi: 10.1002/ijc.2910470222. [DOI] [PubMed] [Google Scholar]
- Carlstedt I., Herrmann A., Hovenberg H., Lindell G., Nordman H., Wickström C., Davies J. R. 'Soluble' and 'insoluble' mucins--identification of distinct populations. Biochem Soc Trans. 1995 Nov;23(4):845–851. doi: 10.1042/bst0230845. [DOI] [PubMed] [Google Scholar]
- Carlstedt I., Lindgren H., Sheehan J. K., Ulmsten U., Wingerup L. Isolation and characterization of human cervical-mucus glycoproteins. Biochem J. 1983 Apr 1;211(1):13–22. doi: 10.1042/bj2110013. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Davies J. R., Hovenberg H. W., Lindén C. J., Howard R., Richardson P. S., Sheehan J. K., Carlstedt I. Mucins in airway secretions from healthy and chronic bronchitic subjects. Biochem J. 1996 Jan 15;313(Pt 2):431–439. doi: 10.1042/bj3130431. [DOI] [PMC free article] [PubMed] [Google Scholar]
- De Bolós C., Garrido M., Real F. X. MUC6 apomucin shows a distinct normal tissue distribution that correlates with Lewis antigen expression in the human stomach. Gastroenterology. 1995 Sep;109(3):723–734. doi: 10.1016/0016-5085(95)90379-8. [DOI] [PubMed] [Google Scholar]
- Devine P. L. A sensitive microplate assay for glycoproteins that utilizes an immunological digoxigenin-based detection system. Biotechniques. 1992 Feb;12(2):160–162. [PubMed] [Google Scholar]
- GAENSLER E. A., LINDGREN I. Open-circuit techniques for the measurement of ventilation; a review. Scand J Clin Lab Invest. 1955;7 (Suppl 20):19–38. [PubMed] [Google Scholar]
- Gerken T. A., Butenhof K. J., Shogren R. Effects of glycosylation on the conformation and dynamics of O-linked glycoproteins: carbon-13 NMR studies of ovine submaxillary mucin. Biochemistry. 1989 Jun 27;28(13):5536–5543. doi: 10.1021/bi00439a030. [DOI] [PubMed] [Google Scholar]
- Good A. H., Yau O., Lamontagne L. R., Oriol R. Serological and chemical specificities of twelve monoclonal anti-Lea and anti-Leb antibodies. Vox Sang. 1992;62(3):180–189. doi: 10.1111/j.1423-0410.1992.tb01195.x. [DOI] [PubMed] [Google Scholar]
- Ho S. B., Roberton A. M., Shekels L. L., Lyftogt C. T., Niehans G. A., Toribara N. W. Expression cloning of gastric mucin complementary DNA and localization of mucin gene expression. Gastroenterology. 1995 Sep;109(3):735–747. doi: 10.1016/0016-5085(95)90380-1. [DOI] [PubMed] [Google Scholar]
- Hovenberg H. W., Davies J. R., Carlstedt I. Different mucins are produced by the surface epithelium and the submucosa in human trachea: identification of MUC5AC as a major mucin from the goblet cells. Biochem J. 1996 Aug 15;318(Pt 1):319–324. doi: 10.1042/bj3180319. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hsu S. M., Raine L. Versatility of biotin-labeled lectins and avidin-biotin-peroxidase complex for localization of carbohydrate in tissue sections. J Histochem Cytochem. 1982 Feb;30(2):157–161. doi: 10.1177/30.2.7037937. [DOI] [PubMed] [Google Scholar]
- Ihida K., Suganuma T., Tsuyama S., Murata F. Glycoconjugate histochemistry of the rat fundic gland using Griffonia simplicifolia agglutinin-II during the development. Am J Anat. 1988 Jul;182(3):250–256. doi: 10.1002/aja.1001820306. [DOI] [PubMed] [Google Scholar]
- Inatomi T., Tisdale A. S., Zhan Q., Spurr-Michaud S., Gipson I. K. Cloning of rat Muc5AC mucin gene: comparison of its structure and tissue distribution to that of human and mouse homologues. Biochem Biophys Res Commun. 1997 Jul 30;236(3):789–797. doi: 10.1006/bbrc.1997.7051. [DOI] [PubMed] [Google Scholar]
- Jourdian G. W., Dean L., Roseman S. The sialic acids. XI. A periodate-resorcinol method for the quantitative estimation of free sialic acids and their glycosides. J Biol Chem. 1971 Jan 25;246(2):430–435. [PubMed] [Google Scholar]
- Karlsson N. G., Nordman H., Karlsson H., Carlstedt I., Hansson G. C. Glycosylation differences between pig gastric mucin populations: a comparative study of the neutral oligosaccharides using mass spectrometry. Biochem J. 1997 Sep 15;326(Pt 3):911–917. doi: 10.1042/bj3260911. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lohmander L. S., De Luca S., Nilsson B., Hascall V. C., Caputo C. B., Kimura J. H., Heinegard D. Oligosaccharides on proteoglycans from the swarm rat chondrosarcoma. J Biol Chem. 1980 Jul 10;255(13):6084–6091. [PubMed] [Google Scholar]
- Mollicone R., Bara J., Le Pendu J., Oriol R. Immunohistologic pattern of type 1 (Lea, Leb) and type 2 (X, Y, H) blood group-related antigens in the human pyloric and duodenal mucosae. Lab Invest. 1985 Aug;53(2):219–227. [PubMed] [Google Scholar]
- Nordman H., Davies J. R., Herrmann A., Karlsson N. G., Hansson G. C., Carlstedt I. Mucus glycoproteins from pig gastric mucosa: identification ofdifferent mucin populations from the surface epithelium. Biochem J. 1997 Sep 15;326(Pt 3):903–910. doi: 10.1042/bj3260903. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Oinuma T., Ide S., Kawano J., Suganuma T. Purification and immunohistochemistry of Griffonia simplicifolia agglutinin-II-binding mucus glycoprotein in rat stomach. Glycobiology. 1994 Aug;4(4):469–475. doi: 10.1093/glycob/4.4.469. [DOI] [PubMed] [Google Scholar]
- Ota H., Katsuyama T. Alternating laminated array of two types of mucin in the human gastric surface mucous layer. Histochem J. 1992 Feb;24(2):86–92. doi: 10.1007/BF01082444. [DOI] [PubMed] [Google Scholar]
- Sakamoto S., Watanabe T., Tokumaru T., Takagi H., Nakazato H., Lloyd K. O. Expression of Lewisa, Lewisb, Lewisx, Lewisy, siayl-Lewisa, and sialyl-Lewisx blood group antigens in human gastric carcinoma and in normal gastric tissue. Cancer Res. 1989 Feb 1;49(3):745–752. [PubMed] [Google Scholar]
- Sheehan J. K., Carlstedt I. Size heterogeneity of human cervical mucus glycoproteins. Studies performed with rate-zonal centrifugation and laser light-scattering. Biochem J. 1987 Aug 1;245(3):757–762. doi: 10.1042/bj2450757. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Shekels L. L., Lyftogt C., Kieliszewski M., Filie J. D., Kozak C. A., Ho S. B. Mouse gastric mucin: cloning and chromosomal localization. Biochem J. 1995 Nov 1;311(Pt 3):775–785. doi: 10.1042/bj3110775. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Thornton D. J., Howard M., Khan N., Sheehan J. K. Identification of two glycoforms of the MUC5B mucin in human respiratory mucus. Evidence for a cysteine-rich sequence repeated within the molecule. J Biol Chem. 1997 Apr 4;272(14):9561–9566. doi: 10.1074/jbc.272.14.9561. [DOI] [PubMed] [Google Scholar]
- Turner B. S., Bhaskar K. R., Hadzopoulou-Cladaras M., Specian R. D., LaMont J. T. Isolation and characterization of cDNA clones encoding pig gastric mucin. Biochem J. 1995 May 15;308(Pt 1):89–96. doi: 10.1042/bj3080089. [DOI] [PMC free article] [PubMed] [Google Scholar]