8 results on '"Eklouh-Molinier, Christophe"'
Search Results
2. Genetic architecture and genomic selection of fatty acid composition predicted by Raman spectroscopy in rainbow trout.
- Author
-
Blay, Carole, Haffray, Pierrick, D'Ambrosio, Jonathan, Prado, Enora, Dechamp, Nicolas, Nazabal, Virginie, Bugeon, Jérôme, Enez, Florian, Causeur, David, Eklouh-Molinier, Christophe, Petit, Vincent, Phocas, Florence, Corraze, Geneviève, and Dupont-Nivet, Mathilde
- Subjects
RAINBOW trout ,RAMAN spectroscopy ,GENETIC variation ,DOCOSAHEXAENOIC acid ,FISH oils ,EICOSAPENTAENOIC acid ,GENETIC correlations ,UNSATURATED fatty acids - Abstract
Background: In response to major challenges regarding the supply and sustainability of marine ingredients in aquafeeds, the aquaculture industry has made a large-scale shift toward plant-based substitutions for fish oil and fish meal. But, this also led to lower levels of healthful n−3 long-chain polyunsaturated fatty acids (PUFAs)—especially eicosapentaenoic (EPA) and docosahexaenoic (DHA) acids—in flesh. One potential solution is to select fish with better abilities to retain or synthesise PUFAs, to increase the efficiency of aquaculture and promote the production of healthier fish products. To this end, we aimed i) to estimate the genetic variability in fatty acid (FA) composition in visceral fat quantified by Raman spectroscopy, with respect to both individual FAs and groups under a feeding regime with limited n-3 PUFAs; ii) to study the genetic and phenotypic correlations between FAs and processing yields- and fat-related traits; iii) to detect QTLs associated with FA composition and identify candidate genes; and iv) to assess the efficiency of genomic selection compared to pedigree-based BLUP selection. Results: Proportions of the various FAs in fish were indirectly estimated using Raman scattering spectroscopy. Fish were genotyped using the 57 K SNP Axiom™ Trout Genotyping Array. Following quality control, the final analysis contained 29,652 SNPs from 1382 fish. Heritability estimates for traits ranged from 0.03 ± 0.03 (n-3 PUFAs) to 0.24 ± 0.05 (n-6 PUFAs), confirming the potential for genomic selection. n-3 PUFAs are positively correlated to a decrease in fat deposition in the fillet and in the viscera but negatively correlated to body weight. This highlights the potential interest to combine selection on FA and against fat deposition to improve nutritional merit of aquaculture products. Several QTLs were identified for FA composition, containing multiple candidate genes with indirect links to FA metabolism. In particular, one region on Omy1 was associated with n-6 PUFAs, monounsaturated FAs, linoleic acid, and EPA, while a region on Omy7 had effects on n-6 PUFAs, EPA, and linoleic acid. When we compared the effectiveness of breeding programmes based on genomic selection (using a reference population of 1000 individuals related to selection candidates) or on pedigree-based selection, we found that the former yielded increases in selection accuracy of 12 to 120% depending on the FA trait. Conclusion: This study reveals the polygenic genetic architecture for FA composition in rainbow trout and confirms that genomic selection has potential to improve EPA and DHA proportions in aquaculture species. [ABSTRACT FROM AUTHOR]
- Published
- 2021
- Full Text
- View/download PDF
3. In vivo confocal Raman microspectroscopy of the human skin: highlighting of spectral markers associated to aging via a research of correlation between Raman and biometric mechanical measurements.
- Author
-
Eklouh-Molinier, Christophe, Gaydou, Vincent, Froigneux, Emmanuel, Barlier, Pascale, Couturaud, Virginie, Manfait, Michel, and Piot, Olivier
- Subjects
RAMAN spectroscopy ,BIOMETRIC identification ,SKIN aging ,STRAINS & stresses (Mechanics) ,ELASTICITY - Abstract
Skin plays a protective role against the loss of water and external aggression, including mechanical stresses. These crucial functions are ensured by different cutaneous layers, particularly the stratum corneum (SC). During aging, the human skin reveals some apparent modifications of functionalities such as a loss of elasticity. Our investigations aimed at demonstrating that Raman microspectroscopy, as a label-free technique with a high molecular specificity, is efficient to assess in vivo the molecular composition of the skin and the alterations underwent during aging. Our approach was based on a search for correlation between Raman data collected on healthy female volunteers of different ages (from 21 to 70 years old) by means of a remote confocal Raman and skin firmness measurements used as a reference method. Raman and biometric data were then submitted to a partial least square (PLS)-based data processing. Our experiments demonstrated the potential of Raman microspectroscopy to provide an objective in vivo assessment of the skin 'biological age' that can be very different from the 'chronological age' of the person. In addition, Raman features sensitive to the elasticity and the fatigability of the SC were highlighted. Thereafter, calibration transfer functions were constructed to show the possibility to compare the results obtained during two distinct measurement campaigns conducted with two Raman probes of the same conception. This approach could lead to several interesting prospects, in particular by objectifying the effects of dermocosmetic products on the superficial layers of the skin and by accessing some underlying molecular mechanisms. [ABSTRACT FROM AUTHOR]
- Published
- 2015
- Full Text
- View/download PDF
4. Investigating the relationship between changes in collagen fiber orientation during skin aging and collagen/water interactions by polarized-FTIR microimaging.
- Author
-
Eklouh-Molinier, Christophe, Happillon, Teddy, Bouland, Nicole, Fichel, Caroline, Diébold, Marie-Danièle, Angiboust, Jean-François, Manfait, Michel, Brassart-Pasco, Sylvie, and Piot, Olivier
- Subjects
COLLAGEN ,CYTOSKELETAL proteins ,HELICAL structure ,HYDROGEN bonding interactions ,FOURIER transform infrared spectroscopy ,MACROMOLECULES - Abstract
Upon chronological aging, human skin undergoes structural and molecular modifications, especially at the level of type I collagen. This macromolecule is one of the main dermal structural proteins and presents several age-related alterations. It exhibits a triple helical structure and assembles itself to form fibrils and fibers. In addition, water plays an important role in stabilizing the collagen triple helix by forming hydrogen-bonds between collagen residues. However, the influence of water on changes of dermal collagen fiber orientation with age has not been yet understood. Polarized-Fourier Transform Infrared (P-FTIR) imaging is an interesting biophotonic approach to determine in situ the orientation of type I collagen fibers, as we have recently shown by comparing skin samples of different ages. In this work, P-FTIR spectral imaging was performed on skin samples from two age groups (35- and 38-year-old on the one hand, 60- and 66-year-old on the other hand), and our analyses were focused on the effect of H
2 O/D2 O substitution. Spectral data were processed with fuzzy C-means (FCM) clustering in order to distinguish different orientations of collagen fibers. We demonstrated that the orientation was altered with aging, and that D2 O treatment, affecting primarily highly bound water molecules, is more marked for the youngest skin samples. Collagen-bound water-related spectral markers were also highlighted. Our results suggest a weakening of water/collagen interactions with age. This non-destructive and label-free methodology allows us to understand better the importance of bound water in collagen fiber orientation alterations occurring with skin aging. Obtaining such structural information could find benefits in dermatology as well as in cosmetics. [ABSTRACT FROM AUTHOR]- Published
- 2015
- Full Text
- View/download PDF
5. Probing single-tumor cell interactions with different-age type I collagen networks by synchrotron-based Fourier transform infrared microspectroscopy.
- Author
-
Guilbert, Marie, Eklouh-Molinier, Christophe, Wehbe, Katia, Sulé.-Suso, Josep, Ying Yang, Cinque, Gianfelice, Jeannesson, Pierre, and Sockalingum, Ganesh D.
- Subjects
FOURIER transform infrared spectroscopy ,CANCER cells ,COLLAGEN ,AGING - Abstract
We report here on a first study using synchrotron radiation-based Fourier transform infrared microspectroscopy and imaging to investigate HT1080 human fibrosarcoma cells grown onto different-aged type I collagen networks. Spectral images were analyzed with k-means and fuzzy C-means (FCM) clustering algorithms. K-means delineated tumor cells from their surrounding collagen networks and the latter as a function of age mainly due to specific changes in the sugar absorption region. The FCM analysis gave a better nuance of the spectral images. A progression of the biochemical information was observed upon going from the cellular compartments to the pericellular contact regions and to the intact collagens of the different age groups. Two spectral markers based on sugar and protein bands via the intensity ratio (I
1032 /I1655 ) and band area ratio (Asugar /Aamide II), showed an increase in advanced glycation endproducts (AGEs) with age. A clear-separation of the three age groups was obtained for spectra originating from the peripheral contact areas mainly due to changes in protein band intensities. The above-described markers decreased to constant levels for the three conditions indicating a masking of the biochemical information. These results hold promises to better understand the impact of age on tumor progression processes while highlighting new markers of the tumor cell invasion front. [ABSTRACT FROM AUTHOR]- Published
- 2014
- Full Text
- View/download PDF
6. Interest of polarized FT-IR imaging to characterize the collagen network in human skin.
- Author
-
Eklouh-Molinier, Christophe, Nguyen, The Thuong, Sebiskveradze, David, Feru, Jezabel, Bouland, Nicole, Terryn, Christine, Manfait, Michel, Brassart-Pasco, Sylvie, and Piot, Olivier
- Subjects
FOURIER transform infrared spectroscopy ,COLLAGEN ,CANCER invasiveness ,POLARIZATION spectroscopy ,K-means clustering ,DERMATOLOGY ,FUZZY clustering technique - Abstract
BACKGROUND: During pathological and/or physiological processes, such as tumoral progression or aging, human skin undergoes molecular and structural changes mainly due to alterations of dermal structural proteins such as type I collagen. These modifications in dermis are probably due to collagen fibers rearrangement and reorientation which have not been thoroughly studied up to now. FT-IR (Fourier transform infrared) microspectroscopy associated to polarization measurement appears as an interesting method to determine in situ the alignment of type I collagen fibers.OBJECTIVE: In this paper, two different clustering algorithms were applied to determine different layers in human skin. Besides, we used polarized FT-IR imaging to evaluate the molecular organization of dermal collagen.METHODS: To do this, a cryosection of skin from 48-year-old woman was analyzed. Acquired FT-IR images were firstly processed using K-means and fuzzy C-means (FCM). FCM was chosen on polarized FT-IR images in order to highlight the molecular orientation of dermal collagen fibrils. The ratio of Amide I/Amide II bands integrated intensities was computed in order to assess the orientation of collagen fibrils.RESULTS AND CONCLUSION: This methodology permitted to reveal the potential of polarized FT-IR microspectroscopy for the characterization of type I collagen network in human skin. Our approach could help to find innovative applications in dermatology as well as in cosmetics. [ABSTRACT FROM AUTHOR]
- Published
- 2014
- Full Text
- View/download PDF
7. Changes of skin collagen orientation associated with chronological aging as probed by polarized-FTIR micro-imaging.
- Author
-
Nguyen, The Thuong, Eklouh-Molinier, Christophe, Sebiskveradze, David, Feru, Jezabel, Terryn, Christine, Manfait, Michel, Brassart-Pasco, Sylvie, and Piot, Olivier
- Subjects
COLLAGEN ,CHRONOLOGY ,AGING ,IMAGING systems ,MORPHOLOGY - Abstract
During chronological skin aging, alterations in dermal structural proteins cause morphological modifications. Modifications are probably due to collagen fiber (type I collagen) rearrangement and reorientation with aging that have not been researched until now. FTIR microspectroscopy appears as an interesting method to study protein structure under normal and pathological conditions. Associated with a polarizer, this vibrational technique permits us to probe collagen orientation within skin tissue sections, by computing the ratio of integrated intensities of amide I and amide II bands. In this study, we used the polarized-FTIR imaging to evaluate molecular modifications of dermal collagen during chronological aging. The data processing of polarized infrared data revealed that type I collagen fibers become parallel to the skin surface in aged skin dermis. Our approach could find innovative applications in dermatology as well as in cosmetics. [ABSTRACT FROM AUTHOR]
- Published
- 2014
- Full Text
- View/download PDF
8. Freezing Weakens the Barrier Function of Reconstructed Human Epidermis as Evidenced by Raman Spectroscopy and Percutaneous Permeation.
- Author
-
Dancik, Yuri, Kichou, Hichem, Eklouh-Molinier, Christophe, Soucé, Martin, Munnier, Emilie, Chourpa, Igor, and Bonnier, Franck
- Subjects
RAMAN spectroscopy ,EPIDERMIS ,PRINCIPAL components analysis ,FREEZING ,AQUEOUS solutions - Abstract
The development and characterization of reconstructed human epidermis (RHE) is an active area of R&D. RHE can replace animal tissues in pharmaceutical, toxicological and cosmetic sciences, yielding scientific and ethical advantages. RHEs remain costly, however, due to consumables and time required for their culture and a short shelf-life. Storing, i.e., freezing RHE could help reduce costs but to date, little is known on the effects of freezing on the barrier function of RHE. We studied such effects using commercial EpiSkin™ RHE stored at −20, −80 and −150 °C for 1 and 10 weeks. We acquired intrinsic Raman spectra in the stratum corneum (SC) of the RHEs as well as spectra obtained following topical application of resorcinol in an aqueous solution. In parallel, we quantified the effects of freezing on the permeation kinetics of resorcinol from time-dependent permeation experiments. Principal component analyses discriminated the intrinsic SC spectra and the spectra of resorcinol-containing RHEs, in each case on the basis of the freezing conditions. Permeation of resorcinol through the frozen RHE increased 3- to 6-fold compared to fresh RHE, with the strongest effect obtained from freezing at −20 °C for 10 weeks. Due to the extensive optimization and standardization of EpiSkin™ RHE, the effects observed in our work may be expected to be more pronounced with other RHEs. [ABSTRACT FROM AUTHOR]
- Published
- 2020
- Full Text
- View/download PDF
Catalog
Discovery Service for Jio Institute Digital Library
For full access to our library's resources, please sign in.