Hydrophobic proteins of lamellated osmiophilic bodies isolated from pig lung

Phizackerley, P. J. R.; Town, M.-H.; Newman, G. E.

doi:10.1042/bj1830731

Cited by 114 publications

(56 citation statements)

References 35 publications

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“…Phizackerley and co-workers were the first to describe the presence of hydrophobic surfactant proteins [253]. Two hydrophobic surfactant proteins are known: SP-B and SP-C.…”

Section: Hydrophobic Surfactant Proteinsmentioning

confidence: 99%

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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“…Phizackerley and co-workers were the first to describe the presence of hydrophobic surfactant proteins [253]. Two hydrophobic surfactant proteins are known: SP-B and SP-C.…”

Section: Hydrophobic Surfactant Proteinsmentioning

confidence: 99%

The Pulmonary Surfactant System: Biochemical and Clinical Aspects

Creuwels

Golde

Haagsman

1997

Lung

283

188

View full text Add to dashboard Cite

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“…The presence of two hydrophobic, low molecular weight apoproteins in mammalian pulmonary surfactant has been shown (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18)(19), and cDNA clones have been isolated that predict the amino acid sequences of their precursor molecules (3-5, 10, 15). The importance of these apoproteins, termed SP-B and SP-C (20) in the ability of natural or synthetic surfactants to be able to reduce surface tension at the epithelial air/liquid interface in the lung has been the subject of several recent papers (2,7,10,11,(13)(14)(15)(17)(18)(19)(21)(22)(23).…”

Section: Preparation Ofpurified Sp-b Monomer Dimer and Oligomersmentioning

confidence: 99%

The Use of Synthetic Peptides in the Formation of Biophysically and Biologically Active Pulmonary Surfactants

et al. 1991

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ABSTRACf. Synthetic pulmonary surfactants consisting of mixtures of phospholipids with synthetic peptides based on the amino acid sequence of human surfactant apoprotein SP-B were prepared. These surfactants were analyzed for their ability to lower surface tension on a pulsating bubble surfactometer and for their capacity to improve lung compliance and increase alveolar expansion in a fetal rabbit model of surfactant deficiency. The data demonstrate that several peptides, ranging from 17 to 45 residues in length, matching the carboxy-terminal sequence of the SP-B protein, when appropriately recombined with the phospholipids dipalmitoylphosphatidylcholine and phosphatidylglycerol (3:1), are capable of producing a synthetic surfactant with biophysical and biologicactivity approaching that of human surfactant derived from amniotic fluid. (Pediatr Res 29: 460-465, 1991) Abbreviations DPPC, dipalmitoylphosphatidylcholine lA, iodoacetic acid PG, phosphatidylglycerol PL, phospholipid SP, surfactant protein or swine, or synthetic lipids, generally in combination with SPBand SP-C (7, 10, 11, 13-15, 17-19, 21-23, 27), are being evaluated for their potential use in surfactant replacement therapies.Our previous studies (10) and those of Curstedt et al. (2), and Yu and Possmayer (19), suggested that when recombined with PL, SP-B resulted in greater surface tension lowering and biologic activity than did SP-C. For this reason, we decided to focus our attention on this protein. SP-B, also called SP-18 (4, 10), SPL(Phe) (3), PSP-B (5), and SAP-6-14 (7,16,17,23), has been shown to be a disulfide-linked dimer of two identical polypeptides of approximately 9000 D having an amino terminal sequence of phe-pro-ile-pro-leu-pro-tyr-(human) (3, 5, 10). Data based on amino acid compositions (10) and fast atom bombardment mass spectroscopy (unpublished observations) have led us to conclude that human SP-B is 80-81 residues in length. The sequence is shown in Figure I.To investigate the mechanisms by which SP-B protein augments the surfactant capacity of PL, peptides were synthesized that conform to portions of the native sequence of this protein. These peptides could be combined with PL to reconstitute the biophysical and biologic activities of natural surfactant. We report here the results of studies, using the pulsating bubble surfactometer to measure the capacity of these synthetic surfactants to lower surface tension at an air/liquid interface and the fetal rabbit model to determine their ability to increase lung compliance and alveolar expansion. MATERIALS AND METHODS Preparation ofpurified SP-B monomer, dimer, and oligomers.SP-B was isolated from human amniotic fluid surfactant ad escribed previously (10). One hundred J.Lg of SP-B, in a volume of 206 J.LL methanol, were incubated with 5.14 mg DTT (Sigma Chemical Co, St. Louis, MO) in 17 J.LL methanol, for 1 h at 37°C. Analysis of 2 J.LL on SDS-PAGE showed the SP-B to be approximately 70% reduced as noted by a shift in band position from 18000 D to approximately 9000 D. The SP-B/...

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“…The Ide.ntIty of several extremely hydrophobic, small molecular weIght pro.teins wa~most clearly described by Phizackerly et al (10) studymg porcme surfactant. Two distinct small molecular weight proteins w~re rece~tly isolated from rat surfactant (17).…”

mentioning

confidence: 90%

“…Ether/ethanol extracts containing SAP-6 were evaporated to near dryness and redissolved in chloroform. Purification of SAP-6 then proceeded essentially as described by Phizackerley et al (10). The dried residue was dissolved in chloroform and applied to a BioSil-HA column (2.5 x 40 cm, Bio-Rad, Richmond, CA) equilibrated in chloroform.…”

Section: Purification Of Hydrophobic Proteins From Surfactant and Surmentioning

confidence: 99%

“…Mam~~ian pulmon~ry surfactant is composed primarily of phospholIpIds~nd ass?cIat~d proteins, Two major protein groups h~ve been prevIOusly IdentIfied: a surfactant-associated glycoprotem of 3~-40,000 daltons first described by King and Clements (1), hereI~called .SAP-35 and smaller molecular weight proteins det~cted m a v~net~of mammalian surfactants (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12). ClarificatIon of the IdentIty and nature of the various surfactantassociated proteins has been incomplete.…”

mentioning

confidence: 99%

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