The postnatal growth of the rat lung. I. Morphometry

Burri, Peter H.; Dbalý, J; Weibel, Ewald R.

doi:10.1002/ar.1091780405

Cited by 442 publications

(315 citation statements)

References 41 publications

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“…Lung development has been divided into four stages: glandular, canalicular, saccular and, finally, alveolar (Burri & Weibel, 1977). The development of alveoli from saccules is a postnatal phenomenon, which is accompanied by marked morphological changes, a changing ratio of cell types and rapid lung growth.…”

Section: Discussionmentioning

confidence: 99%

“…Secondary septal outgrowth occurs between the tip and base; elastin frequently appears beneath the tip of newly formed alveolar septa and elastic fibres may play a prominent role in this restructuring of lung (Burri & Weibel, 1977). Two types of interstitial fibroblast have been described in the neonatal rat lung: one appeared at the tip of new septa and appeared to be engaged in the synthesis and secretion of elastin; the other type of fibroblast, which is lipid rich, occurred at the base of the septa (Vaccaro & Brody, 1978).…”

Section: Discussionmentioning

confidence: 99%

“…Even though birth is such a critical event for the lung, considerable maturation of the lung occurs postnatally in humans (Boyden & Tompsett, 1965), dogs (Boyden & Tompsett, 1961), rats (Burni et al, 1974) and probably most mammals. The postnatal anatomical development of the rat lung has received extensive study (Burri, 1974;Burri et al, 1974;Hodson, 1977).…”

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confidence: 99%

“…We have investigated the activities of lung lectin and acetylcholinesterase during postnatal lung development. We have also monitored the amounts of elastin during this period of alveolarization, since morphological studies have closely linked the appearance of elastin with the process of alveolar septation (Loosli & Potter, 1959;Burri & Weibel, 1977;Vaccaro & Brody, 1978 (Bradford, 1976). Lectin activity was determined by both haemagglutination and asialo-orosomucoidfragment binding, as described by Powell (1980).…”

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confidence: 99%

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Postnatal development of rat lung. Changes in lung lectin, elastin, acetylcholinesterase and other enzymes

Powell

Whitney

1980

Biochemical Journal

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The development of rat lung from a primitive gas-exchange organ to the mature respiratory organ is in large part a postnatal phenomenon that has been well characterized by morphological and morphometric methods. The alveolarization of the lung is achieved during the first 3 weeks of life. Cholinergic innervation of rat lung also appears postnatally. We have monitored the presence or activity of several proteins during postnatal rat lung development. Newborn-rat lung contains negligible amounts of acetylcholinesterase, but the specific activity of acetylcholinesterase reaches adult values by postnatal day 10-11. Neonatal-rat lung does not contain significant amounts of ,B-galactoside-binding protein [Powell (1980) Biochem. J. 187, 123-1291. The activity of this endogenous lung lectin was apparent at about day 6, was maximal between days 10 and 13 before declining 8-10-fold to reach adult values. Elastin has been implicated from morphological evidence as critical to lung restructuring. We have quantified the amount of desmosine and isodesmosine per g wet wt. of lung. The concentration of elastin, by this criterion, was low and stationary until postnatal day 7; a dramatic increase in elastin concentration occurred between days 10 and 20, when adult values were reached. The peak of lung-lectin activity was coincident with the maturation of acetylcholinesterase and the beginning of rapid elastin cross-linking. The specific activities of angiotensin-converting enzyme, carbonic anhydrase, choline kinase and glucose 6-phosphate dehydrogenase were also monitored.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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confidence: 99%

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Postnatal development of rat lung. Changes in lung lectin, elastin, acetylcholinesterase and other enzymes

Powell

Whitney

1980

Biochemical Journal

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“…Third, to optimize the gas exchange, the double layered capillary networks of all septa are reduced to a single layered one (microvascular maturation, postnatal days 14 -21 in mice; Burri, 1974;Amy et al, 1977;Zeltner and Burri, 1987;Schittny and Burri, 2003;RothKleiner et al, 2005). According to the model of postnatal lung development proposed by Burri et al (Burri, 1974Schittny and Burri, 2003), the formation of new alveolar septa requires the existence of a double layered capillary network within the preexisting septa. As a consequence, after completion of microvascular maturation, further alveolarization should be precluded due to the missing of the second capillary layer.…”

Section: Introductionmentioning

confidence: 99%

Developmental alveolarization of the mouse lung

Mund

Stampanoni

Schittny

2008

Developmental Dynamics

159

171

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Postnatal lung development is not well characterized in mice, especially the time point when alveolarization is completed. Using the total length and the length density of the free septal edge as measured for the formation of new septa, we followed alveolarization throughout postnatal lung development (days 2-125). Furthermore, the alveolar surface area was estimated. The formation of new septa was observed until day 36. Approximately 10% of the septa present in adult mice were formed prenatally by branching morphogenesis, ϳ50% were generated postnatally before and ϳ40% after maturation of the alveolar microvasculature. Approximately 5% of the alveolar surface area present during adulthood was present before alveolarization started, ϳ55% was formed during alveolarization (days 4 -36) and ϳ40% afterward due to growth processes. We conclude that alveolarization continues until young adulthood and that the maturation of the alveolar microvasculature does not preclude further alveolarization. Developmental Dynamics 237:2108 -2116, 2008.

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Cellular Retinoid-Binding Proteins

Ong¹

1987

Arch Dermatol

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A number of specific carrier proteins for members of the vitamin A family have been discovered. Two of these proteins bind all-trans-retinol and are found within cells important in vitamin A metabolism or function. These two proteins have considerable sequence homology and have been named cellular retinol-binding protein (CRBP) and cellular retinol-binding protein, type II (CRBP [II]). A third intracellular protein, cellular retinoic acid-binding protein (CRABP) also is structurally similar but binds only retinoic acid. Although retinol appears to be bound quite similarly by the two retinol-binding proteins, subtle differences are apparent that appear to be related to the different functions of the two proteins. That, coupled with the specific cellular locations of the two proteins, suggests their roles. Cellular retinol-binding protein appears to have several roles, including (1) delivering retinol to specific binding sites within the nucleus and (2) participating in the transepithelial movement of retinol across certain blood-organ barriers. In contrast, CRBP (II) appears to be involved in the intestinal absorption of vitamin A and, in particular, may direct retinol to a specific esterifying enzyme, resulting in the production of fatty acyl esters of retinol that are incorporated into chylomicrons for release to the lymph. Like CRBP, CRABP can deliver its ligand retinoic acid to specific binding sites within the nucleus, sites different from those for retinol. The nuclear binding of retinol and retinoic acid may be part of the mechanism by which vitamin A directs the state of differentiation of epithelial tissue.

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The postnatal growth of the rat lung. I. Morphometry

Cited by 442 publications

References 41 publications

Postnatal development of rat lung. Changes in lung lectin, elastin, acetylcholinesterase and other enzymes

Postnatal development of rat lung. Changes in lung lectin, elastin, acetylcholinesterase and other enzymes

Developmental alveolarization of the mouse lung

Cellular Retinoid-Binding Proteins

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