Lung collagen heterogeneity. Synthesis of type I and type III collagen by rabbit and human lung cells in culture.

Hance, Allan J.; Bradley, Kathryn H.; Crystal, Ronald G.

doi:10.1172/jci108250

Cited by 62 publications

(13 citation statements)

References 19 publications

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“…However, the recognition of collagen by lymphocytes from patients with fibrotic lung disease is not very specific; they do not distinguish between type I collagen of different species (human, rabbit) or different organs (lung, skin). Since prior studies have shown these type I collagens to be very similar (3,4,(26)(27)(28)(29), this cross-reactivity is not surprising.…”

Section: Discussionmentioning

confidence: 61%

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Pathogenic mechanisms in pulmonary fibrosis: collagen-induced migration inhibition factor production and cytotoxicity mediated by lymphocytes.

Kravis¹,

Ahmed²,

Brown³

et al. 1976

J. Clin. Invest.

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110

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A B S T R A C T The universal features of the histopathology of fibrotic lung disease are derangement of parenchymal collagen and infiltration of the parenchyma with chronic inflammatory cells. To determine if this cellular reaction might be associated with autoimmunity to a constituent of the alveolar interstitium, peripheral blood lymphocytes were exposed to human type I collagen in vitro and evaluated for the production of migration inhibition factor and cytotoxicity. Data from 18 patients with idiopathic pulmonary fibrosis, 8 patients with pulmonary fibrosis other than idiopathic pulmonary fibrosis, 12 patients with nonfibrotic lung disease, and 9 normals demonstrated that circulating lymphocytes from more than 94% of patients with fibrotic lung disease take part in processes where the recognition of collagen results in migration inhibition factor production and lysis of collagen-coated sheep red blood cells. These collagen-induced cell-mediated phenomena are obviated with human T-lymphocyte antiserum. Collagen-induced migration inhibition factor production and cytotoxicity were found in less than 20%/o of patients with nonfibrotic disease and were not found in normals. Qualitatively, there was no organ (lung, skin) or species (human, rabbit) Send

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Section: Discussionmentioning

confidence: 61%

“…This is suggested by data demonstrating that: (a) collagen is bound to membranes of fibroblasts (41); (b) human lung fibroblasts synthesize type I collagen (28); and (c) antibodies to collagen are cytotoxic to fibroblasts in culture (42)(43)(44).…”

mentioning

confidence: 99%

Pathogenic mechanisms in pulmonary fibrosis: collagen-induced migration inhibition factor production and cytotoxicity mediated by lymphocytes.

Kravis¹,

Ahmed²,

Brown³

et al. 1976

J. Clin. Invest.

Self Cite

110

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show abstract

“…4 Though [14C]-valine was specifically employed to detect the synthesis of elastin by the lung cells in culture, no radiactive band corresponding to proelastin or tropoelastin could be discerned in these cultures.29 Thus the guinea pig lung fibroblasts did not appear to synthesize any elastin under the conditions employed.…”

Section: Discussionmentioning

confidence: 97%

Biochemical Characterization of Collagens and of a Non-Collagenous Protein Synthesized by Guinea Pig Lung Fibroblasts in Culture

Bashey

Herold

Jimenez

1983

Connective Tissue Research

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Employing various radioactive amino acids, protein biosynthesis by guinea pig lung fibroblasts has been studied in monolayer culture. The cells were shown to synthesize and secrete several collagenous and noncollagenous proteins. The biosynthesized macromolecules have been characterized employing molecular sieve and ion exchange chromatography (DEAE-cellulose column), SDS-polyacrylamide gel electrophoresis, and enzymatic digestion. It was found that the guinea pig lung fibroblasts synthesized mainly type I procollagen molecules which appeared in the media in various stages of cleavage. The intact procollagen molecules and the various processed products were identified by their electrophoretic migration in SDS-polyacrylamide slab gels and further characterized by 1) elution position on SDS-agarose columns under reducing conditions; 2) hydroxyproline content; 3) change in elution position on SDS-agarose after pepsin digestion; 4) chromatographic separation on DEAE-cellulose columns and electrophoretic mobility of the various peaks; and 5) susceptibility to collagenase digestion. Slab gel electrophoresis under non-reducing conditions of aliquots of culture media after limited pepsin digestion indicated the presence of disulfide-bonded type III collagen alpha-chains. In addition, the lung fibroblasts synthesized a non-collagenous protein composed of two disulfide-bonded chains. The individual chains appeared to have a molecular weight of approximately 220,000 when examined under reducing conditions. This protein has been identified as fibronectin based on its molecular weight, its resistance to collagenase attack, its susceptibility to protease digestion and its precipitation with specific antisera to fibronectin.

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“…About 40% of lung cells are fibroblasts, which are the main producer of type I and III collagens (Hance et al, 1976). As cellular senescence of fibroblasts impairs the secretion of collagenous proteins due to the immediate intracellular collagen degradation (Martin et al, 1990;Shivakumar et al, 2003), an increased number of senescent fibroblasts can, at least in part, explain the lower biosynthesis of fibrillar collagens in the old mouse lung.…”

Section: Discussionmentioning

confidence: 99%

Age‐related expression, enzymatic solubility and modification with advanced glycation end‐products of fibrillar collagens in mouse lung

Rolewska

Al‐Robaiy

Santos

et al. 2013

Experimental Gerontology

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Lung collagen heterogeneity. Synthesis of type I and type III collagen by rabbit and human lung cells in culture.

Abstract: A B S T R A CThe existence of 40 cell types and the insolubility of lung collagen increase the complexity of identifying the types of collagen in lung and the cells responsible for the synthesis of each type. The techniques described here should eventually lead to a complete description of

Cited by 62 publications

References 19 publications

Pathogenic mechanisms in pulmonary fibrosis: collagen-induced migration inhibition factor production and cytotoxicity mediated by lymphocytes.

Pathogenic mechanisms in pulmonary fibrosis: collagen-induced migration inhibition factor production and cytotoxicity mediated by lymphocytes.

Biochemical Characterization of Collagens and of a Non-Collagenous Protein Synthesized by Guinea Pig Lung Fibroblasts in Culture

Age‐related expression, enzymatic solubility and modification with advanced glycation end‐products of fibrillar collagens in mouse lung

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