Studies on the Collagen and Elastin Content of the Human Lung*†

Pierce, John A.; Hocott, Joe B.

doi:10.1172/jci104030

Cited by 114 publications

(52 citation statements)

References 6 publications

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“…It has been shown that steroids can stimulate collagen biasynthesia in the l u n~ (18). This effect might be mediated by steroid receptors since such receptors have been described in rat lung cytosol (17).…”

Section: Discussionmentioning

confidence: 97%

Androgen Receptors and Metabolism in Cultured Human Fetal Fibroblasts

et al. 1980

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Testosterone metabolism and dihydrotestosterone (DHT) receptor activity were studied in fibroblasts cultured fram genital and non-genital tissues of 8-to 22-week old human fetuses.AS early a s the eighth week of gestation. DHT receptar activity was detected in non-genital skin. The binding capacity (Bma,) was greater in genital skin fibroblasts (mean + SD -474 + 32 moles x lO-18/ug DNA) than non-genital skin (mean + SD = 124 fb2 moles C10-181ug DNA). DHT receptor binding (Bmax) was found in fibroblasts derived from testes (112 moles x 10-18lug DNA), but not intestine ( < 10 moles x l~-~~/ u g DNA). The DHT receptor activity of fetal skin fibroblasts of genital origin was similar to that of fibroblasts derived fram the foreskin of normal newborns. DHT receptors from fetal and newborn fibroblast cultures had similar sedimentation coefficients in sucrose density gradient centrifugation, but there were small differences in their relative affinities for 17%-estradiol and cypraterone.Low, but detectable 5a-reductase activity was observed at 8 weeks gestation in non-genital skin fibroblasts and was present in fibroblasts from a variety of tissues of older fetuses, including testes, kidneys and lung.. The highest 5o-reductase activity of 210 pgthourlug DNA was found in fibroblasts cultured from clitoral tissue from 8 10-week old fetus. In all but one specimen, the 5o-reduced products were either DHT or 5o-androstanedione.The demanstratian of 5a-reductase activity and specific DHT receptors in fetal tissues suggests that the intracellular mechanism for androgen action is present in the fetus, similar to that after birth. SPECULATIONWe have observed the conversion of testosterone into dihydrotestosterone (DHT) as well as DHT binding to a specific receptor in human fibroblasts cultured from a variety of tissue8 of fetal origin as early a s 8 weeks gestation. It is speculated that the concentration of testosterone, the rate of formation of DHT and the concentration of androgen receptors each play a role in the differentiation of the external genitalia.

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Section: Discussionmentioning

confidence: 97%

Androgen Receptors and Metabolism in Cultured Human Fetal Fibroblasts

et al. 1980

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“…The ECM of the lung is dominated by type I collagen fibrils and elastic fibres (Pierce and Hocott 1960). Most studies of the ageing lung have failed to identify any change in collagen content (Escolar et al 1997;Lang et al 1994;Pierce and Hocott 1960;Takubo et al 1999;Yamamoto et al 2003), although age-related increases have been observed in both rodent (Goldstein 1982;Huang et al 2007) and human systems (Derrico et al 1989).…”

Section: Pulmonarymentioning

confidence: 99%

“…Most studies of the ageing lung have failed to identify any change in collagen content (Escolar et al 1997;Lang et al 1994;Pierce and Hocott 1960;Takubo et al 1999;Yamamoto et al 2003), although age-related increases have been observed in both rodent (Goldstein 1982;Huang et al 2007) and human systems (Derrico et al 1989). Similarly, the concentration of elastin and/or elastic fibres in human and rodent lungs has been reported to remain unchanged (Andreotti et al 1983;Takubo et al 1999;Yamamoto et al 2003), to increase (Escolar et al 1994(Escolar et al , 1997Fitzpatrick and Hospelhorn 1962;Pierce and Hocott 1960) and to decrease with age (Derrico et al 1989;Huang et al 2007). There are three potential explanations for the lack of a consensus regarding changes in ECM composition in the ageing lung.…”

Section: Pulmonarymentioning

confidence: 99%

“…1). They are major components of the extracellular matrix (ECM) in dynamic tissues such as blood vessels (Davis 1993), skin (Braverman and Fonferko 1982) and the lungs (Pierce and Hocott 1960). This tissue distribution, combined with the low modulus of elasticity and high resilience of elastin (Gosline et al 2002), allows elastic fibres to complement the tensile strength of fibrillar collagens (Kielty et al 2002).…”

Section: Introductionmentioning

confidence: 99%

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Tissue elasticity and the ageing elastic fibre

Sherratt

2009

AGE

270

189

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The ability of elastic tissues to deform under physiological forces and to subsequently release stored energy to drive passive recoil is vital to the function of many dynamic tissues. Within vertebrates, elastic fibres allow arteries and lungs to expand and contract, thus controlling variations in blood pressure and returning the pulmonary system to a resting state. Elastic fibres are composite structures composed of a cross-linked elastin core and an outer layer of fibrillin microfibrils. These two components perform distinct roles; elastin stores energy and drives passive recoil, whilst fibrillin microfibrils direct elastogenesis, mediate cell signalling, maintain tissue homeostasis via TGFβ sequestration and potentially act to reinforce the elastic fibre. In many tissues reduced elasticity, as a result of compromised elastic fibre function, becomes increasingly prevalent with age and contributes significantly to the burden of human morbidity and mortality. This review considers how the unique molecular structure, tissue distribution and longevity of elastic fibres pre-disposes these abundant extracellular matrix structures to the accumulation of damage in ageing dermal, pulmonary and vascular tissues. As compromised elasticity is a common feature of ageing dynamic tissues, the development of strategies to prevent, limit or reverse this loss of function will play a key role in reducing age-related morbidity and mortality.

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“…Collagen is the most abundant protein in lung, composing about 20% of the dry weight of the adult human lung (2)(3)(4)(5). This collagen is distributed throughout the lung, including the tracheobronchial tree, blood vessels, and the alveolar interstitium.…”

Section: Introductionmentioning

confidence: 99%