2022
DOI: 10.1016/j.bbadis.2021.166279
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Identification of remodeled collagen fibers in tumor stroma by FTIR Micro-spectroscopy: A new approach to recognize the colon carcinoma

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Cited by 10 publications
(5 citation statements)
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“…In particular, the absorption values of cancerous cells were larger than those of healthy ones and the differences were statistically significant. Such a result is in good agreement with that reported by S. De Santis et al regarding FTIR microspectroscopy of collagen from human colon specimens which was surgically removed after diagnosis of adenocarcinoma [44]: they found larger FTIR spectral signals from malignant tissue than normal tissue in the amide III spectral range [44]. Even B. Brozen-Pluska reported that protein-related peaks in the Raman spectra of Caco-2 cells were characterized by greater intensities with respect to the corresponding peaks in the Raman spectra of noncancerous colon cells [45].…”
Section: Dong Et Al Regarding Colon Tissuesupporting
confidence: 93%
“…In particular, the absorption values of cancerous cells were larger than those of healthy ones and the differences were statistically significant. Such a result is in good agreement with that reported by S. De Santis et al regarding FTIR microspectroscopy of collagen from human colon specimens which was surgically removed after diagnosis of adenocarcinoma [44]: they found larger FTIR spectral signals from malignant tissue than normal tissue in the amide III spectral range [44]. Even B. Brozen-Pluska reported that protein-related peaks in the Raman spectra of Caco-2 cells were characterized by greater intensities with respect to the corresponding peaks in the Raman spectra of noncancerous colon cells [45].…”
Section: Dong Et Al Regarding Colon Tissuesupporting
confidence: 93%
“…The amide III is characterized by three main signals (1291, 1241, and 1998 cm −1 ) associated with CN stretching, NH bending, CC stretching, and CH bending vibrations. The band at 1241 cm −1 showed the highest intensity and is related to the NH group involved in hydrogen bonds with CO of the adjacent α ‐chain 77 …”
Section: Resultsmentioning
confidence: 99%
“…In showed the highest intensity and is related to the N H group involved in hydrogen bonds with C O of the adjacent α-chain. 77 A study on the comparative composition of PVA, PCL, and PCL-Col_1/PVA core-shell fibers was carried out by using FTIR spectroscopy. The infrared spectra of these materials presented in Figure 6 show the characteristic bands for pristine collagen, PVA, PCL, and PCL-Col_1/PVA (before and after release/degradation in saline solution at 37 C for 28 days).…”
Section: Core-shell Fiber Chemical Composition Assessmentmentioning
confidence: 99%
“…Conversely, in OP osteoporotic samples, two sets of spectra were identified representative of collagen‐rich areas (OP+) and collagen‐poor ones (OP–) (named respectively OP+ cortical, OP+ trabecular, OP– cortical and OP– trabecular, based on the region of interest). The analysis of the average IR spectra, reported in Figure 4 both in absorbance (continuous colored lines) and second derivative mode (dotted black lines), highlighted the following bands: ~1340 cm −1 (CH 2 wagging of proline side chains) 29 , 30 ;~1320 cm −1 (a‐helix secondary structures) 31 , 32 ; ~1284 cm −1 and ~1240 cm −1 , (collagen triple helix) 33 ; ~1264 cm −1 (random secondary structures), 33 ~1204 cm −1 (amino acids lateral chains) 34 and ~ 1160 cm −1 (C‐OH moiety of carbohydrates). 18 , 35 , 36 …”
Section: Resultsmentioning
confidence: 99%
“…Conversely, in OP osteoporotic samples, two sets of spectra were identified representative of collagen-rich areas (OP+) and collagen-poor ones (OP-) (named respectively OP+ cortical, OP+ trabecular, OP-cortical and OP-trabecular, based on the region of interest). The analysis of the average IR spectra, reported in Figure 4 both in absorbance (continuous colored lines) and second derivative mode (dotted black lines), highlighted the following bands: ~1340 cm À1 (CH 2 wagging of proline side chains) 29,30 ;~1320 cm À1 (a-helix secondary structures) 31,32 ; ~1284 cm À1 and ~1240 cm À1 , (collagen triple helix) 33 ; ~1264 cm À1 (random secondary structures), 33 ~1204 cm À1 (amino acids lateral chains) 34 and ~1160 cm À1 (C-OH moiety of carbohydrates). 18,35,36 The following band area ratios diagnostic for collagen composition and structure were calculated and statistically analyzed (Figure 5): Coll/Tot (total collagen), 1340/1160 (collagen's proline), 1320/1160 (a-helices), 1284/1160 (triple helices), 1264/1160 (random structures), 1240/1160 (triple helices), 1204/1160 (amino acids' lateral chains), and Random/Folded (calculated as the ratio between the areas of the 1264 cm À1 band and the sum of the areas of the bands at 1320, 1284 -, and 1240 cm À1 ).…”
Section: Type I Collagen Structure and Localization Were Altered In D...mentioning
confidence: 94%