Literature DB >> 11923100

Torpor-associated fluctuations in surfactant activity in Gould's wattled bat.

Jonathan R Codd1, Samuel Schürch, Christopher B Daniels, Sandra Orgeig.   

Abstract

The primary function of pulmonary surfactant is to reduce the surface tension (ST) created at the air-liquid interface in the lung. Surfactant is a complex mixture of lipids and proteins and its function is influenced by physiological parameters such as metabolic rate, body temperature and breathing. In the microchiropteran bat Chalinolobus gouldii these parameters fluctuate throughout a 24 h period. Here we examine the surface activity of surfactant from warm-active and torpid bats at both 24 degrees C and 37 degrees C to establish whether alterations in surfactant composition correlate with changes in surface activity. Bats were housed in a specially constructed bat room at Adelaide University, at 24 degrees C and on a 8:16 h light:dark cycle. Surfactant was collected from bats sampled during torpor (25<T(b)<28 degrees C), and while active (T(b)>35 degrees C). Alterations in the lipid composition of surfactant occur with changes in the activity cycle. Most notable is an increase in surfactant cholesterol (Chol) with decreases in body temperature [Codd et al., Physiol. Biochem. Zool. 73 (2000) 605-612]. Surfactant from active bats was more surface active at higher temperatures, indicated by lower ST(min) and less film area compression required to reach ST(min) at 37 degrees C than at 24 degrees C. Conversely, surfactant from torpid bats was more active at lower temperatures, indicated by lower ST(min) and less area compression required to reach ST(min) at 24 degrees C than at 37 degrees C. Alterations in the Chol content of bat surfactant appear to be crucial to allow it to achieve low STs during torpor.

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Year:  2002        PMID: 11923100     DOI: 10.1016/s1388-1981(01)00185-8

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  5 in total

1.  Palmitoylation of pulmonary surfactant protein SP-C is critical for its functional cooperation with SP-B to sustain compression/expansion dynamics in cholesterol-containing surfactant films.

Authors:  Florian Baumgart; Olga L Ospina; Ismael Mingarro; Ignacio Rodríguez-Crespo; Jesús Pérez-Gil
Journal:  Biophys J       Date:  2010-11-17       Impact factor: 4.033

2.  Combined and independent action of proteins SP-B and SP-C in the surface behavior and mechanical stability of pulmonary surfactant films.

Authors:  David Schürch; Olga L Ospina; Antonio Cruz; Jesús Pérez-Gil
Journal:  Biophys J       Date:  2010-11-17       Impact factor: 4.033

Review 3.  Leptin integrates vertebrate evolution: from oxygen to the blood-gas barrier.

Authors:  J S Torday; F L Powell; C G Farmer; S Orgeig; H C Nielsen; A J Hall
Journal:  Respir Physiol Neurobiol       Date:  2010-01-21       Impact factor: 1.931

4.  Pulmonary surfactant protein SP-C counteracts the deleterious effects of cholesterol on the activity of surfactant films under physiologically relevant compression-expansion dynamics.

Authors:  Leticia Gómez-Gil; David Schürch; Erik Goormaghtigh; Jesús Pérez-Gil
Journal:  Biophys J       Date:  2009-11-18       Impact factor: 4.033

5.  The Molecular Apgar Score: A Key to Unlocking Evolutionary Principles.

Authors:  John S Torday; Heber C Nielsen
Journal:  Front Pediatr       Date:  2017-03-20       Impact factor: 3.418

  5 in total

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