Age-dependent increase of human plasma fibronectin

Labat‐Robert, J.; Potazman, Jean-Pascal; Derouette, J.C.; Robert, L.

doi:10.1016/0309-1651(81)90213-7

Cited by 57 publications

(11 citation statements)

References 12 publications

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“…The possible role of fibronectin in these phenomena was excluded on the following evidence: (i) When total human plasma as well as highly purified human plasma fibronectin (17) were passed over a K-elastin-coupled Sepharose column, there was no retention of fibronectin. Similar experiments were performed using fibrous elastin-coupled Sepharose (18), again with the same negative results.…”

Section: Resultsmentioning

confidence: 99%

Inducible adhesion of mesenchymal cells to elastic fibers: elastonectin.

Hornebeck¹,

Tixier²,

Robert³

1986

Proc. Natl. Acad. Sci. U.S.A.

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The addition of highly purified elastic fibers to confluent human skin fibroblast or porcine aorta smooth muscle cell cultures resulted in a time-dependent, strong adhesion of the fibrils to the cell surface. The kinetics of adhesion was studied by video/time-lapse cinematography. After a 0.5-1 hr lag period, adhesion progressed to a maximum amount in 3-6 hr in the described conditions. Adhesion is strongly accelerated by the prior addition of soluble elastin peptides (K-elastin) to the cultures. Cycloheximide inhibits this induced adhesion. Adherent elastic fibers can be detached by treatment with elastase and trypsin but not with collagenase. The radioactive proteins adhering to elastic fibers, after a 6-hr incubation of the induced cultures in presence of [35S]methionine, were extracted and analyzed by NaDodSO4/PAGE. The proteins strongly adhering to the elastic fibers had apparent molecular sizes of about 120, 67, 60, and 45 kDa. Only the 120-kDa protein band showed a significant increase of its associated radioactivity in the induced cultures as compared to the noninduced cultures. We propose that the 120-kDa protein is responsible for the induced adhesion of mesenchymal cells to elastic fibers and designate it "elastonectin."In the past years, specific adhesive proteins that mediate cell attachment to the extracellular matrix have been identified and characterized. Fibronectin ensures the adhesion of mesenchymal cells to interstitial collagens and to some proteoglycans (1-4). Laminin is involved in the interaction between epithelial cells and basement membrane components, such as collagen type IV (5, 6). Elastin was originally considered to be an isotropic and inert constituent, but physicochemical studies have pointed to a more dynamic structure and to possible interactions with other connective tissue proteins (7,8). Elastin peptides were also shown to be able to interact with several other cell types (9, 10). Mecham et al. (11) studied the acquisition of chemotactic responsiveness to elastin peptides and the expression of the elastin phenotype by fetal bovine ligamentum fibroblasts during cell differentiation and showed that they were closely related events. Therefore, the investigation of whether specific protein(s) could mediate the adhesion of mesenchymal cells to elastic fibers was undertaken.In the present report, we have investigated the interactions between purified bovine ligamentum nuchae elastic fibers and human skin fibroblasts or pig aorta smooth muscle cells in culture and show that elastic fibers adhere strongly to both cell types. Fibronectin has been shown not to be involved in this process. Biosynthetic experiments carried out with human skin fibroblasts cultured in presence or absence of elastic fibers enabled us to carry out preliminary identification of an inducible protein closely associated with the added elastic fibers. We have designated this adhesive protein "elastonectin."MATERIAL AND METHODS Fibroblasts and smooth muscle cells were obtained from human dermis and porci...

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Section: Resultsmentioning

confidence: 99%

Inducible adhesion of mesenchymal cells to elastic fibers: elastonectin.

Hornebeck¹,

Tixier²,

Robert³

1986

Proc. Natl. Acad. Sci. U.S.A.

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“…The GO term clusters targeted included blood coagulation, chemokine and inflammatory pathways, axon guidance, peptidase activity, and apoptosis. The two main proteins in the blood coagulation cluster were fibrinogen and fibronectin, both previously shown to increase with age, and both related with a pro‐inflammatory state (Folsom et al., 1991; Labat‐Robert, Potazman, Derouette, & Robert, 1981). A second cluster included a number of peptidases, with substantial overlap with the blood coagulation cluster, and included SERPINF2, AHSG, SERPING1, SERPINA3, and TIMP1 suggesting that this second group of proteins taps into some different aspects of blood clotting pathways.…”

Section: Discussionmentioning

confidence: 99%

Plasma proteomic signature of age in healthy humans

Tanaka¹,

Biancotto²,

Moaddel³

et al. 2018

Aging Cell

377

396

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To characterize the proteomic signature of chronological age, 1,301 proteins were measured in plasma using the SOMAscan assay (SomaLogic, Boulder, CO, USA) in a population of 240 healthy men and women, 22–93 years old, who were disease‐ and treatment‐free and had no physical and cognitive impairment. Using a p ≤ 3.83 × 10−5 significance threshold, 197 proteins were positively associated, and 20 proteins were negatively associated with age. Growth differentiation factor 15 (GDF15) had the strongest, positive association with age (GDF15; 0.018 ± 0.001, p = 7.49 × 10−56). In our sample, GDF15 was not associated with other cardiovascular risk factors such as cholesterol or inflammatory markers. The functional pathways enriched in the 217 age‐associated proteins included blood coagulation, chemokine and inflammatory pathways, axon guidance, peptidase activity, and apoptosis. Using elastic net regression models, we created a proteomic signature of age based on relative concentrations of 76 proteins that highly correlated with chronological age (r = 0.94). The generalizability of our findings needs replication in an independent cohort.

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“…Another proteolytic fragment of fibronectin induced an increased synthesis of fibronectin and of TNFa release (Lopez-Armada et al 1997). We could show in our laboratory that fibronectin biosynthesis by fibroblasts (the tissue form of fibronectin), as well as by hepatocytes (circulating form in the blood plasma) increase with age (Labat- Robert et al 1981). Proteolytic activity in several tissues was also shown to increase with age as well as with passage number in cell cultures (Robert and Labat-Robert 1988).…”

Section: Proteolytic Generation Of Harmful Peptidesmentioning

confidence: 90%

Genetic, epigenetic and posttranslational mechanisms of aging

2010

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Gerontological experimentation is and was always strongly influenced by "theories". The early decades of molecular genetics inspired deterministic thinking, based on the "Central Dogma" (DNA --> RNA --> Proteins). With the progress of detailed knowledge of gene-function a much more complicated picture emerged. Regulation of gene-expression turned out to be a highly complicated process. Experimental gerontology produced over the last decades several "paradigms" incompatible with simple genetic determinism. The increasing number of such detailed experimental "facts" revealed the importance of epigenetic factors and of posttranslational modifications in the age-dependent decline of physiological functions. We shall present in this review a short but critical analysis of genetic and epigenetic processes applied to the interpretation of the more and more precisely elucidated experimental paradigms of aging followed by some of the most relevant aging-mechanisms at the post-translational level, the posttranslational modifications of proteins such as the Maillard reaction, the proteolytic production of harmful peptides and the molecular mechanisms of the aging of elastin with the role of the age-dependent uncoupling of the elastin receptor, as well as the loss of several other receptors. We insist also on the well documented influence of posttranslational modifications on gene expression and on the role of non-coding RNA-s. Altogether, these data replace the previous simplistic concepts on gene action as related to aging by a much more complicated picture, where epigenetic and posttranslational processes together with environmentally influenced genetic pathways play key-roles in aging and strongly influence gene expression.

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Age-dependent increase of human plasma fibronectin

Cited by 57 publications

References 12 publications

Inducible adhesion of mesenchymal cells to elastic fibers: elastonectin.

Inducible adhesion of mesenchymal cells to elastic fibers: elastonectin.

Plasma proteomic signature of age in healthy humans

Genetic, epigenetic and posttranslational mechanisms of aging

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