Macromolecular organization of natural and recombinant lung surfactant protein SP 28–36

Voss, Tilman; Eistetter, Harald; Schäfer, Klaus; Engel, Jürgen

doi:10.1016/0022-2836(88)90448-2

Cited by 245 publications

(110 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…1A. At neutral pH, spectra were characterized by a shoulder at 220 nm and a strong negative extreme at 207 nm as previously reported (24,40). The change of pH from 7.2 to 4.5 led to a change in the shape of SP-A spectrum and markedly reduced the contribution of the 207-nm minimum to the spectrum.…”

Section: Reversible Ph-dependent Change Of the Secondary Structure Ofsupporting

confidence: 49%

Effect of Acidic pH on the Structure and Lipid Binding Properties of Porcine Surfactant Protein A

Ruano

Pérez‐Gil

Casals

1998

Journal of Biological Chemistry

View full text Add to dashboard Cite

Pulmonary surfactant protein A (SP-A) is synthesized by type II cells and stored intracellularly in secretory granules (lamellar bodies) together with surfactant lipids and hydrophobic surfactant proteins B and C (SP-B and SP-C).We asked whether the progressive decrease in pH along the exocytic pathway could influence the secondary structure and lipid binding and aggregation properties of porcine SP-A. Conformational analysis from CD spectra of SP-A at various pH values indicated that the percentage of ␣-helix progressively decreased and that of ␤-sheet increased as the pH was reduced. The protein underwent a marked self-aggregation at mildly acidic pH in the presence of Ca 2؉, conditions thought to resemble those existing in the trans-Golgi network. Protein aggregation was greater as the pH was reduced. We also found that both neutral and acidic vesicles either with or without SP-B or SP-C bound to SP-A at acidic pH as demonstrated by co-migration during centrifugation. However, the binding of acidic but not neutral vesicles to SP-A led to 1) a striking change in the CD spectra of the protein, which was interpreted as a decrease of the level of SP-A self-aggregation, and 2) a protection of the protein from endoproteinase Glu-C degradation at pH 4.5. SP-A massively aggregated acidic vesicles but poorly aggregated neutral vesicles at acidic pH. Aggregation of dipalmitoylphosphatidylcholine (DPPC) vesicles either with or without SP-B and/or SP-C strongly depended on pH, being progressively decreased as the pH was reduced and markedly increased when pH was shifted back to 7.0. At the pH of lamellar bodies, SP-A-induced aggregation of DPPC vesicles containing SP-B or a mixture of SP-B and SP-C was very low, although SP-A bound to these vesicles. These results indicate that 1) DPPC binding and DPPC aggregation are different phenomena that probably have different SP-A structural requirements and 2) aggregation of membranes induced by SP-A at acidic pH is critically dependent on the presence of acidic phospholipids, which affect protein structure, probably preventing the formation of large aggregates of protein.Pulmonary surfactant is a mixture of approximately 80% phospholipids, 10% other lipids, and 5-10% surfactant-specific proteins that lines the alveolar space and is essential for breathing (for reviews, see Refs. 1-3). The alveolar type II cell is the sole cell type in the lung that produces all components of pulmonary surfactant. The surfactant apolipoproteins (SP-A, 1 SP-B, and SP-C) and all of the surfactant phospholipids are stored intracellularly in lamellar bodies and are secreted as a complex (4 -7). The release of surfactant to the alveolar lumen occurs by exocytosis of lamellar body content in response to secretagogue stimulation (8, 9). The regulated secretory pathway of the type II cell is atypical because the lamellar body not only functions as a classic secretory granule, but it also intersects with the endocytic pathway (10, 11). Like the storage granules in other secretory cells, lamellar bodies ha...

show abstract

Section: Reversible Ph-dependent Change Of the Secondary Structure Ofsupporting

confidence: 49%

Effect of Acidic pH on the Structure and Lipid Binding Properties of Porcine Surfactant Protein A

Ruano

Pérez‐Gil

Casals

1998

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Chemical and electron microscopy studies of SP-A [30] mannan binding protein [15] (Thiel, S. and Timpl, R., unpublished electron microscopy data) and conglutinin [ 16,3 l] have shown that they have the same distinct divisions of collagen-like and globular amino acid sequences in peptide chains between 24 and 65 kDa ( fig.2) and similar overall macromolecular organisation. SP-A is difficult to distinguish from Clq when viewed in the electron microscope, the MBP also shows marked similarity to Clq but appears to be mainly found as extended tetramers and trimers rather than as a close-packed hexamer, while conglutinin is organised in a more flexible 'spider-like' structure ( fig.3).…”

Section: Structural Similarities Between the Collagen-like Soluble Lementioning

confidence: 99%

Structures and functions associated with the group of mammalian lectins containing collagen‐like sequences

1989

View full text Add to dashboard Cite

The number of proteins found in body fluids and at cell surfaces, which are known to display carbohydrate-binding properties, continues to increase rapidly. In these proteins, in addition to a domain associated with lectin properties, one or more, non-lectin domains are present. It is possible that binding of sugar residues by the lectin domain may be important in triggering a variety of recognition and clearance mechanisms via the non-lectin domains. The group of lectins containing collagen-like sequences may provide some insight into structure/function relationships of the different domains in view of the well defined structures already available for several of these molecules.

show abstract

“…The interruption in the collagen-like repeating sequence after the 13th triplet introduces a flexible kink in the collagen rod. After this interruption, the trimers are no longer bundled, but they bend outward from the central axis into six directions [338]. The carboxyl-terminal region (divided into a neck region and the CRD) is composed of 148-residues, forming a C-type lectin domain [67,68].…”

Section: Structure Of Sp-amentioning

confidence: 99%

The Pulmonary Surfactant System: Biochemical and Clinical Aspects

Creuwels

Golde

Haagsman

1997

Lung

283

188

View full text Add to dashboard Cite

Abstract. This article starts with a brief account of the history of research on pulmonary surfactant. We will then discuss the morphological aspects and composition of the pulmonary surfactant system. We describe the hydrophilic surfactant proteins A and D and the hydrophobic surfactant proteins B and C, with focus on the crucial roles of these proteins in the dynamics, metabolism, and functions of pulmonary surfactant. Next we discuss the major disorders of the surfactant system. The final part of the review will be focused on the potentials and complications of surfactant therapy in the treatment of some of these disorders. It is our belief that increased knowledge of the surfactant system and its functions will lead to a more optimal composition of the exogenous surfactants and, perhaps, widen their applicability to treatment of surfactant disorders other than neonatal respiratory distress syndrome.Key words: Surfactant protein-Pulmonary surfactant-Respiratory distress syndrome. HistoryResearch on surfactant goes back to 1929 when von Neergaard published the first paper about the difference in pressure needed to inflate lungs with air or with liquid [333]. He found that the pressure necessary for filling the lungs with air was higher than when the lungs were filled with liquid. To explain this result he stated that the alveoli were stabilized by lowering the naturally high surface tension of the air/water interface. In 1946 Thannhauser and co-workers reported that lung tissue has a remarkably high content of the lipid dipalmityl lecithin (current name, dipalmitoylphosphatidylcholine)Offprint requests to: Henk P. Haagsman.

show abstract

Macromolecular organization of natural and recombinant lung surfactant protein SP 28–36

Cited by 245 publications

References 31 publications

Effect of Acidic pH on the Structure and Lipid Binding Properties of Porcine Surfactant Protein A

Effect of Acidic pH on the Structure and Lipid Binding Properties of Porcine Surfactant Protein A

Structures and functions associated with the group of mammalian lectins containing collagen‐like sequences

The Pulmonary Surfactant System: Biochemical and Clinical Aspects

Contact Info

Product

Resources

About