Experimental Neonatal Respiratory Failure Induced by a Monoclonal Antibody to the Hydrophobic Surfactant-Associated Protein SP-B

Robertson, Bengt; Kobayashi, Tsutomu; Ganzuka, M.; Grossmann, Gertie; Li, Wenzhi; Suzuki, Yuzuru

doi:10.1203/00006450-199109000-00007

Cited by 89 publications

(41 citation statements)

References 6 publications

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“…In vivo experiments in preterm rabbits [265] and selective blocking of SP-B [267] did confirm the significance of this protein. Recently, Nogee and co-workers described a frame shift mutation in the SP-B cDNA [223], which resulted in children unable to produce SP-B.…”

Section: Promotion Of Phospholipid Insertion Into the Air-liquid Intementioning

confidence: 70%

The Pulmonary Surfactant System: Biochemical and Clinical Aspects

Creuwels

Golde

Haagsman

1997

Lung

283

188

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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.

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Section: Promotion Of Phospholipid Insertion Into the Air-liquid Intementioning

confidence: 70%

The Pulmonary Surfactant System: Biochemical and Clinical Aspects

Creuwels

Golde

Haagsman

1997

Lung

283

188

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“…Isolated genetic deficiency of SP-B in humans produces progressive respiratory failure (Nogee et al, 1993) and knockout of the SP-B gene in mice likewise produces respiratory distress (Clark et al, 1995). Loss of surfactant activity and respiratory failure is also observed after blocking of SP-B with monoclonal antibodies Robertson et al, 1991). Today SP-B is the only surfactant protein for which there is direct evidence for a vital respiratory function.…”

Section: Structures Interactions and Dynamics In Relation To Functiomentioning

confidence: 99%

Molecular Structures and Interactions of Pulmonary Surfactant Components

Johansson

Curstedt

1997

European Journal of Biochemistry

273

217

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The dominating functional property of pulmonary surfactant is to reduce the surface tension at the alveolar aidliquid interface, and thereby prevent the lungs from collapsing at the end of expiration. In addition, the system exhibits host-defense properties. Insufficient amounts of pulmonary surfactant in premature infants causes respiratory distress syndrome, a serious threat which nowadays can be effectively treated by airway instillation of surfactant preparations. Surfactant is a mixture of many molecular species, mainly phospholipids and specific proteins, surfactant protein A (SP-A), SP-B, SP-C and SP-D. SP-A and SP-D are water-soluble and belong to the collectins, a family of large multimeric proteins which structurally exhibit collagenousAectin hybrid properties and functionally are Caz+-dependent carbohydrate binding proteins involved in innate host-defence functions. SP-A and SP-D also bind lipids and SP-A is involved in organization of alveolar surfactant phospholipids. SP-B belongs to another family of proteins, which includes also lipid-interacting polypeptides with antibacterial and lytic properties. SP-B is a 17.4-kDa homodimer and each subunit contains three intrachain disulphides and has been proposed to contain four amphipathic helices oriented pairwise in an antiparallel fashion. SP-A, SP-B and SP-D all have been detected also in the gastrointestinal tract. SP-C, in contrast, appears to be a unique protein with extreme structural and stability properties and to exist exclusively in the lungs. SP-C is a lipopeptide containing covalently linked palmitoyl chains and is folded into a 3.7-nm a-helix with a central 2.3-nm all-aliphatic part, making it perfectly suited to interact in a transmembranous way with a fluid bilayer composed of dipalmitoylglycerophosphocholine, the main component of surfactant. Homozygous genetic deficiency of proSP-B causes lethal respiratory distress soon after birth and is associated with aberrant processing of the precursor of SP-C. This review focuses on the chemical composition, structures and interactions of the pulmonary surfactant, in particular the associated proteins.

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“…Surfactant protein B is important for the formation of the active surfactant surface film (Schürch et al, 1998) and is essential for normal lung function (Robertson et al, 1991). Surfactant protein B knock out mice show disruption of surfactant film and function and die from respiratory failure (Clark et al, 1995(Clark et al, , 1997.…”

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confidence: 99%

Surfactant protein B gene variations enhance susceptibility to squamous cell carcinoma of the lung in German patients

Seifart

Plagens

et al. 2002

Br J Cancer

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Genetic factors are thought to influence the risk for lung cancer. Since pulmonary surfactant mediates the response to inhaled carcinogenic substances, candidate genes may be among those coding for pulmonary surfactant proteins. In the present matched case -control study a polymorphism within intron 4 of the gene coding for surfactant specific protein B was analysed in 357 individuals. They were divided into 117 patients with lung cancer (40 patients with small cell lung cancer, 77 patients with non small cell lung cancer), matched controls and 123 healthy individuals. Surfactant protein B gene variants were analysed using specific PCR and cloned surfactant protein B sequences as controls. The frequency of the intron 4 variation was similar in both control groups (13.0% and 9.4%), whereas it was increased in the small cell lung cancer group (17.5%) and the non small cell lung cancer group (16.9%). The gene variation was found significantly more frequently in patients with squamous cell carcinoma (25.0%, P=0.016, odds ratio=3.2, 95%CI=1.24 -8.28) than in the controls. These results indicate an association of the surfactant protein B intron 4 variants and/or its flanking loci with mechanisms that may enhance lung cancer susceptibility, especially to squamous cell carcinoma of the lung.

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Experimental Neonatal Respiratory Failure Induced by a Monoclonal Antibody to the Hydrophobic Surfactant-Associated Protein SP-B

Cited by 89 publications

References 6 publications

The Pulmonary Surfactant System: Biochemical and Clinical Aspects

The Pulmonary Surfactant System: Biochemical and Clinical Aspects

Molecular Structures and Interactions of Pulmonary Surfactant Components

Surfactant protein B gene variations enhance susceptibility to squamous cell carcinoma of the lung in German patients

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