Age-related changes in molecular organization of type I collagen in tendon as probed by polarized SHG and Raman microspectroscopy

Gulick, Laurence Van; Saby, Charles; Morjani, Hamid; Beljebbar, A.

doi:10.1038/s41598-019-43636-2

Cited by 36 publications

(33 citation statements)

References 59 publications

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“…10a presents the primary structure of type I collagen showing the amino acid motif (Gly-X-Y), where X represents the proline (pro) and Y represents hydroxyproline (HyPro) respectively. [58][59][60] Fig. 10b ensures that the presence of hydrogen bonding between -CONHin the collagen brils of the IESM lattice structure.…”

Section: Mechanism Of the Proposed Sensor Arraymentioning

confidence: 97%

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Inner egg shell membrane based bio-compatible capacitive and piezoelectric function dominant self-powered pressure sensor array for smart electronic applications

2020

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Section: Mechanism Of the Proposed Sensor Arraymentioning

confidence: 97%

“…The change in the thickness of the IESM is predominant due to the porous nature of the micro-brils and proteins present in the IESM. 57,58 The cross-sectional SEM images in Fig. 9a and b show the comprehensive picture of the porous structure of the IESM.…”

Section: Mechanism Of the Proposed Sensor Arraymentioning

confidence: 99%

Inner egg shell membrane based bio-compatible capacitive and piezoelectric function dominant self-powered pressure sensor array for smart electronic applications

2020

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“…Chang et al have shown that in a 2D collagen coating model, an increase of type I collagen rigidity rendered NSCLC cells A549 more resistant to erlotinib (8). Previous studies from our group have shown that age-related modifications of type I collagen were linked to an increase of its rigidity (17,18), and could modulate tumor cells behavior when used in a more physiological 3D model. Since lung carcinoma cells are confronted to a collagen rich microenvironment, we decided to investigate the effect of collagen aging on the toxicity of erlotinib on A549 and BZR cells by determining the IC 50 of erlotinib in adult and old collagen, for both cell lines.…”

Section: Collagen Aging Promotes Lung Cancer Cells Resistance To Erlomentioning

confidence: 90%

Type I Collagen Aging Increases Expression and Activation of EGFR and Induces Resistance to Erlotinib in Lung Carcinoma in 3D Matrix Model

et al. 2020

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Type I collagen is the major structural component of lung stroma. Because of its long half-life, type I collagen undergoes post-translational modifications such as glycation during aging process. These modifications have been shown to impact the structural organization of type I collagen fibers. In the present work we evaluated the impact of collagen aging on lung carcinoma cells response to erlotinib-induced cytotoxicity and apoptosis, and on Epidermal Growth Factor Receptor (EGFR) expression and phosphorylation. To this end, experiments were performed in 2D and 3D matrix models established from type I collagen extracted from adult (10 weeks-old) and old (100 weeksold) rat's tail tendons. Our results show that old collagen induces a significant increase in EGFR expression and phosphorylation when compared to adult collagen in 3D matrix but not in 2D coating. Such modification was associated to an increase in the IC 50 of erlotinib in the presence of old collagen and a lower sensitivity to drug-induced apoptosis. These data suggest that collagen aging confers resistance to the cytotoxic and apoptotic effects of therapies targeting EGFR kinase function in lung carcinoma. Moreover, our data underline the importance of the 3D matrix environment in this process.

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“…Here, human and bovine bone generated stronger background fluorescence than synthetic HAp. Demineralised bovine bone, despite exhibiting the most intense background fluorescence, displayed many of the characteristic spectral features associated with type-I collagen 13,25,26 , both before and after baseline subtraction.…”

Section: Discussionmentioning

confidence: 99%

Towards refining Raman spectroscopy-based assessment of bone composition

Shah

2020

Sci Rep

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Various compositional parameters are derived using intensity ratios and integral area ratios of different spectral peaks and bands in the Raman spectrum of bone. The $$\nu $$ ν 1-, $$\nu $$ ν 2-,$$\nu $$ ν 3-, $$\nu $$ ν 4 PO43−, and $$\nu_{1} $$ ν 1 CO32− bands represent the inorganic phase while amide I, amide III, Proline, Hydroxyproline, Phenylalanine, δ(CH3), δ(CH2), and $$\nu $$ ν (C–H) represent the organic phase. Here, using high-resolution Raman spectroscopy, it is demonstrated that all PO43− bands of bone either partially overlap with or are positioned close to spectral contributions from the organic component. Assigned to the organic component, a shoulder at 393 cm−1 compromises accurate estimation of $$\nu $$ ν 2 PO43− integral area, i.e., phosphate/apatite content, with implications for apatite-to-collagen and carbonate-to-phosphate ratios. Another feature at 621 cm−1 may be inaccurately interpreted as $$\nu $$ ν 4 PO43− band broadening. In the 1020–1080 cm−1 range, the ~ 1047 cm−1$$\nu $$ ν 3 PO43− sub-component is obscured by the 1033 cm−1 Phenylalanine peak, while the ~ 1076 cm−1$$\nu $$ ν 3 PO43− sub-component is masked by the $$\nu $$ ν 1 CO32− band. With $$\nu $$ ν 1 PO43− peak broadening, $$\nu $$ ν 2 PO43− integral area increases exponentially and individual peaks comprising the $$\nu $$ ν 4 PO43− band merge together. Therefore, $$\nu $$ ν 2 PO43− and $$\nu $$ ν 4 PO43− band profiles are sensitive to changes in mineral crystallinity.

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Age-related changes in molecular organization of type I collagen in tendon as probed by polarized SHG and Raman microspectroscopy

Cited by 36 publications

References 59 publications

Inner egg shell membrane based bio-compatible capacitive and piezoelectric function dominant self-powered pressure sensor array for smart electronic applications

Inner egg shell membrane based bio-compatible capacitive and piezoelectric function dominant self-powered pressure sensor array for smart electronic applications

Type I Collagen Aging Increases Expression and Activation of EGFR and Induces Resistance to Erlotinib in Lung Carcinoma in 3D Matrix Model

Towards refining Raman spectroscopy-based assessment of bone composition

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