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. 1981 Feb 1;193(2):447–457. doi: 10.1042/bj1930447

Characterization of collagenous and non-collagenous peptides of a glycoprotein isolated from alveoli of patients with alveolar proteinosis.

S N Bhattacharyya
PMCID: PMC1162626  PMID: 6796047

Abstract

A glycoprotein of Mr 62 000 was isolated from lung lavage material of patients with alveolar proteinosis. The glycoprotein was found to contain (per molecule) 72 residues of glycine, 5 residues of hydroxyproline, 3 molecules of sialic acid, 4.9 molecules of mannose, 4.0 molecules of galactose, 0.9 molecule of fucose and 7.0 molecules of N-acetylglucosamine. Limited pepsin digestion of the glycoprotein resulted in six peptides, three of which contained hydroxyproline and nearly 30% glycine, and two of which contained all the carbohydrate present in the glycoprotein of Mr 62 000. The three peptides containing hydroxyproline and with high content of glycine contained a repeating -Gly-X-Y-sequence in the peptide chain. Partial amino acid-sequence analyses on the peptides derived from the digestion of the alveolar glycoprotein with various proteolytic enzymes indicate that this glycoprotein is characterized by the presence of alternating collagenous and non-collagenous regions in the same polypeptide chain.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bhattacharyya S. N., Lynn W. S. Isolation and characterization of a pulmonary glycoprotein from human amniotic fluid. Biochim Biophys Acta. 1978 Dec 20;537(2):329–335. doi: 10.1016/0005-2795(78)90516-0. [DOI] [PubMed] [Google Scholar]
  2. Bhattacharyya S. N., Lynn W. S. Structural characterization of a glycoprotein isolated from alveoli of patients with alveolar proteinosis. J Biol Chem. 1979 Jun 25;254(12):5191–5198. [PubMed] [Google Scholar]
  3. Bhattacharyya S. N., Lynn W. S. Structural studies on the oligosaccharides of a glycoprotein isolated from alveoli of patients with alveolar proteinosis. J Biol Chem. 1977 Feb 25;252(4):1172–1180. [PubMed] [Google Scholar]
  4. Bhattacharyya S. N., Lynn W. S. Studies on structural relationship between two glycoproteins isolated from alveoli of patients with alveolar proteinosis. Biochim Biophys Acta. 1977 Sep 27;494(1):150–161. doi: 10.1016/0005-2795(77)90143-x. [DOI] [PubMed] [Google Scholar]
  5. Bhattacharyya S. N., Passero M. A., DiAugustine R. P., Lynn W. S. Isolation and characterization of two hydroxyproline-containing glycoproteins from normal animal lung lavage and lamellar bodies. J Clin Invest. 1975 May;55(5):914–920. doi: 10.1172/JCI108020. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Bhattacharyya S. N., Passero M. A., Lynn W. S. Isolation and characterization of subunits of human Clq. Biochim Biophys Acta. 1974 Apr 11;342(2):343–350. doi: 10.1016/0005-2795(74)90089-0. [DOI] [PubMed] [Google Scholar]
  7. Bhattacharyya S. N., Rose M. C., Lynn M. G., MacLeod C., Alberts M., Lynn W. S. Isolation and characterization of a unique glycoprotein from lavage of chicken lungs and lamellar organelles. Am Rev Respir Dis. 1976 Nov;114(5):843–850. doi: 10.1164/arrd.1976.114.5.843. [DOI] [PubMed] [Google Scholar]
  8. Bhattacharyya S. N., Sahu S., Lynn W. S. Structural studies on a glycoprotein isolated from alveoli of patients with alveolar proteinosis. Biochim Biophys Acta. 1976 Mar 18;427(1):91–106. doi: 10.1016/0005-2795(76)90288-9. [DOI] [PubMed] [Google Scholar]
  9. Clark C. C., Kefalides N. A. Carbohydrate moieties of procollagen: incorporation of isotopically labeled mannose and glucosamine into propeptides of procollagen secreted by matrix-free chick embryo tendon cells. Proc Natl Acad Sci U S A. 1976 Jan;73(1):34–38. doi: 10.1073/pnas.73.1.34. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Clark C. C., Kefalides N. A. Localization and partial composition of the oligosaccharide units on the propeptide extensions of type I procollagen. J Biol Chem. 1978 Jan 10;253(1):47–51. [PubMed] [Google Scholar]
  11. Crouch E., Sage H., Bornstein P. Structural basis for apparent heterogeneity of collagens in human basement membranes: type IV procollagen contains two distinct chains. Proc Natl Acad Sci U S A. 1980 Feb;77(2):745–749. doi: 10.1073/pnas.77.2.745. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Furuto D. K., Miller E. J. Isolation of a unique collagenous fraction from limited pepsin digests of human placental tissue. Characterization of one of the constituent polypeptide chains. J Biol Chem. 1980 Jan 10;255(1):290–295. [PubMed] [Google Scholar]
  13. Hudson B. G., Spiro R. G. Fractionation of glycoprotein components of the reduced alkylated renal glomerular basement membrane. J Biol Chem. 1972 Jul 10;247(13):4239–4247. [PubMed] [Google Scholar]
  14. Kylstra J. A., Rausch D. C., Hall K. D., Spock A. Volume-controlled lung lavage in the treatment of asthma, bronchiectasis, and mucoviscidosis. Am Rev Respir Dis. 1971 May;103(5):651–665. doi: 10.1164/arrd.1971.103.5.651. [DOI] [PubMed] [Google Scholar]
  15. Levine M. J., Spiro R. G. Isolation from glomerular basement membrane of a glycopeptide containing both asparagine-linked and hydroxylysine-linked carbohydrate units. J Biol Chem. 1979 Sep 10;254(17):8121–8124. [PubMed] [Google Scholar]
  16. ROSEN S. H., CASTLEMAN B., LIEBOW A. A. Pulmonary alveolar proteinosis. N Engl J Med. 1958 Jun 5;258(23):1123–1142. doi: 10.1056/NEJM195806052582301. [DOI] [PubMed] [Google Scholar]
  17. Ramirez J. Pulmonary alveolar proteinosis. Treatment by massive bronchopulmonary lavage. Arch Intern Med. 1967 Feb;119(2):147–156. doi: 10.1001/archinte.119.2.147. [DOI] [PubMed] [Google Scholar]
  18. Reid K. B. A collagen-like amino acid sequence in a polypeptide chain of human C1q (a subcomponent of the first component of complement). Biochem J. 1974 Jul;141(1):189–203. doi: 10.1042/bj1410189. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Reid K. B. Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement. Biochem J. 1979 May 1;179(2):367–371. doi: 10.1042/bj1790367. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Reid K. B. Isolation, by partial pepsin digestion, of the three collagen-like regions present in subcomponent Clq of the first component of human complement. Biochem J. 1976 Apr 1;155(1):5–17. doi: 10.1042/bj1550005. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Rosenberry T. L., Richardson J. M. Structure of 18S and 14S acetylcholinesterase. Identification of collagen-like subunits that are linked by disulfide bonds to catalytic subunits. Biochemistry. 1977 Aug 9;16(16):3550–3558. doi: 10.1021/bi00635a008. [DOI] [PubMed] [Google Scholar]
  22. Sato T., Spiro R. G. Studies on the subunit composition of the renal glomerular basement membrane. J Biol Chem. 1976 Jul 10;251(13):4062–4070. [PubMed] [Google Scholar]
  23. Schwartz D., Chin-Quee T., Veis A. Characterization of bovine anterior-lens-capsule basement-membrane collagen. 1. Pepsin susceptibility, salt precipitation and thermal gelation: a property of non-collagen component integrity. Eur J Biochem. 1980 Jan;103(1):21–27. doi: 10.1111/j.1432-1033.1980.tb04284.x. [DOI] [PubMed] [Google Scholar]
  24. Spiro R. G. Studies on the renal glomerular basement membrane. Nature of the carbohydrate units and their attachment to the peptide portion. J Biol Chem. 1967 Apr 25;242(8):1923–1932. [PubMed] [Google Scholar]

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