Studies on structural relationship between two glyco-proteins isolated from alveoli of patients with alveolar proteinosis

Bhattacharyya, Sambhu N.; Lynn, William S.

doi:10.1016/0005-2795(77)90143-x

Cited by 36 publications

(31 citation statements)

References 28 publications

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“…The oligosaccharides present in the glycoproteins were of the high-mannose-type. The molecular weights of these labelled proteins were similar to the collagen-like and complex type glycoproteins isolated from lung lavage material of patients with alveolar proteinosis (Bhattacharyya & Lynn, 1977a,b, 1979, 1980aBhattacharyya, 1981) as well as from lung lavage of normal rabbit (Bhattacharyya & Lynn, 1980b).…”

Section: Discussionmentioning

confidence: 53%

“…The profiles on the left show radioactivity in slices of the gels whose photographs are shown on the right (after staining with Coomassie Blue). The migration of standard proteins (myosin H-chain, phosphorylase b, bovine serum albumin, ovalbumin, achymotrypsinogen, fi-lactoglobulin and cytochrome c) and alveolar glycoprotein (M, 80000, 62000 and 36000; Bhattacharyya et al, 1976;Bhattacharyya & Lynn, 1977a are indicated by arrows. Abbreviation used: B.B., Bromophenol Blue.…”

Section: Reversibility Of Inhibition Of Biosynthesis Of Oligosaccharimentioning

confidence: 99%

“…Glycoproteins containing asparagine-linked complex oligosaccharides have been found to be present in lavage material isolated from lungs of patients with alveolar proteinosis (Bhattacharyya & Lynn, 1977a,b) as well as from lung lavage of normal animals (Bhattacharyya & Lynn, 1980b). The biosynthesis of these glycoproteins has not been explored yet.…”

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confidence: 99%

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Effects of bleomycin and methylprednisolone on the biosynthesis of oligosaccharide-lipids and glycoproteins in lung

Mohapatra¹,

Lynn²,

Bhattacharyya³

1983

Biochemical Journal

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Tissues from rabbit lung were found to incorporate radioactivity from [3H]mannose into the oligosaccharide of a polar lipid soluble in chloroform/methanol/water (10:10:3, by vol.). Only one oligosaccharide-lipid was formed and the composition of the radiolabelled carbohydrate moiety was Glc3Man9(GlcNAc)2. An antitumour antibiotic, bleomycin, and an anti-inflammatory steroid, methylprednisolone, partially inhibited the incorporation of [3H]mannose into oligosaccharide-lipids and in addition resulted in the production of two new components, Man5(GlcNAc)2 and Man2(GlcNAc)2. Sodium dodecyl sulphate/polyacrylamide-gel electrophoresis of the glycoproteins synthesized from the oligosaccharide-lipid intermediates showed labelled components with Mr greater than 200000, 130000, 80000 and 62000. The addition of the drugs resulted in the same pattern with the addition of a new component of Mr 36000. Endoglucosaminidase H-treatment of the glycopeptides isolated from the Pronase-digested glycoproteins indicated that the oligosaccharide units in the glycoproteins were of the high-mannose-type.

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Section: Discussionmentioning

confidence: 53%

Section: Reversibility Of Inhibition Of Biosynthesis Of Oligosaccharimentioning

confidence: 99%

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Effects of bleomycin and methylprednisolone on the biosynthesis of oligosaccharide-lipids and glycoproteins in lung

Mohapatra¹,

Lynn²,

Bhattacharyya³

1983

Biochemical Journal

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“…It was not clear whether this anomaly was due to inaccessibility of some methionine residues leading to incomplete digestion, or to structural properties intrinsic to the peptides that produce a lower mobility on SDS/polyacrylamide-gel electrophoresis than predicted from mass alone. Peptides produced after CNBr cleavage of alveolar-proteinosis-patient PSAP described by others appeared closer in estimated Mr to those predicted from the gene structure (Bhattacharyya & Lynn, 1977). However, amino acid composition and N-terminal analysis of those peptides did not correlate with the data from gene structure as it is now known.…”

Section: Discussionmentioning

confidence: 65%

“…In addition to the 32000-36000-Mr protein(s), other non-serum proteins with Mr values of 60000-62000 have been described in human surfactant (Bhattacharyya & Lynn, 1977;Bhattacharyya, 1981;Phelps et al, 1984;Kuroki et al, 1985).…”

Section: Introductionmentioning

confidence: 99%

Structural characteristics and intermolecular organization of human pulmonary-surfactant-associated proteins

Crawford¹,

Mecham²,

Sage³

1986

Biochemical Journal

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The structural relationships and intermolecular organization among the proteins associated with pulmonary surfactant are largely unknown. We studied the pulmonary-surfactant-associated proteins in the bronchoalveolar lavage fluid obtained from a patient with the clinical syndrome of alveolar proteinosis. The major proteins with Mr values of 32,000-36,000 and 62,000 formed thiol-dependent complexes (Mr greater than 400,000) with intermolecular disulphide bonds present in the collgenase-sensitive domains of these proteins. In contrast, other proteins, which were collagenase-insensitive, formed thiol-dependent oligomers that were not covalently linked to the major proteins. The associations of these proteins in the surfactant of a normal individual were similar. By amino acid analysis, two-dimensional peptide mapping and bacterial-collagenase digestion the 32,000-36,000-Mr and 62,000-Mr proteins were nearly identical. Differences in CNBr cleavage products suggested that the larger of the proteins was formed by non-disulphide, covalent, cross-links in the collagenase-sensitive domains of the 32,000-36,000-Mr proteins. Thus the evidence suggested that the lipid-associated proteins of Mr 32,000-36, 000 contained both disulphide and non-disulphide cross-links in the collagen-like N-terminal region of the proteins and form higher-Mr complexes. This organization may support the three-dimensional conformation of surfactant in the alveolar space.

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Ultrastructural, histochemical, and freeze‐fracture evaluation of multilamellated structures in human pulmonary alveolar proteinosis

et al. 1987

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Ultrastructural, histochemical, and freeze-fracture studies of material recovered by bronchoalveolar lavage from patients with pulmonary alveolar proteinosis revealed four types (A, B, C, and D) of multilamellated structures (MS). Type A, the major component, consisted of concentric, trilaminar structures which were composed of two electron-dense layers and a central lucent layer (5.7-7.5 nm in overall width) alternating with wider (25-30 nm) electron-lucent intervening layers. Type B MS were formed by concentric lamellae with a 5-5.3-nm periodicity. Type C MS were composed of wavy, electron-dense lamellae with a 4-4.5-nm periodicity. Type D MS were conglomerated masses of intricately arranged double or triple electron-dense layers (7.5-13.5 nm wide) alternating with wider (30-40-nm) electron-lucent layers. The electron-dense lamellae of type A, type C, and type D MS were stained with ruthenium red, the Thiéry method, and concanavalin A, indicating the presence of carbohydrate components. Freeze-fracture studies revealed smooth inner and outer surfaces in type A MS, with the fracture planes passing through the central parts of the trilaminar structures; the intervening layers contained 10-nm particles, which probably are proteins. Type B MS had smooth surfaces, and type C MS had slightly particulate surfaces; while type D MS showed tubular or polygonal structures, 350 nm wide, with rows of particles 7-8 nm in diameter. It is concluded that type A and type D MS contain proteins and carbohydrates, probably in the form of glycoproteins, as well as phospholipids, and are related to tubular myelin. Type B and type C MS are considered to contain mainly phospholipids; type C MS are also considered to contain carbohydrates and to be related to lamellar bodies of type II alveolar epithelial cells.

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Studies on structural relationship between two glyco-proteins isolated from alveoli of patients with alveolar proteinosis

Cited by 36 publications

References 28 publications

Effects of bleomycin and methylprednisolone on the biosynthesis of oligosaccharide-lipids and glycoproteins in lung

Effects of bleomycin and methylprednisolone on the biosynthesis of oligosaccharide-lipids and glycoproteins in lung

Structural characteristics and intermolecular organization of human pulmonary-surfactant-associated proteins

Ultrastructural, histochemical, and freeze‐fracture evaluation of multilamellated structures in human pulmonary alveolar proteinosis

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