Notes

Thus, cell-mediated degradation of collagen is an essential process that promotes resolution of fibrosis, and impairment in this process contributes to Conflict of interest statement: Conflict of interest: The authors have declared Isolation and characterization of collagen from the skin of Brama australis
Chemistry of Biomaterials and Cosmetics, ul. collagen supplement , 87-100 Toruń, Poland. Chemistry of Biomaterials and Cosmetics, ul. Gagarina 7, 87-100 Toruń, Poland.Collagen was extracted from the skin of Brama australis, the fish from warm-water sea. The yield of collagen from skin of B.

australis was about 1% on a wet weight basis of raw material. The isolated protein was confirmed as collagen by different physico-chemical techniques such as: FTIR, SDS-PAGE, and amino acid analysis. The denaturation temperature (T(d)) of obtained collagen was found to be 24°C, what is promising as an advantage for cosmetic application. According to the electrophoretic pattern, collagen consisted of two different α-chains (α1 and α2) and was classified as type I collagen. Although T(d) of obtained collagen is higher than 20 °C it is still far from T(d) of Impaired balance of type I and type III procollagen mRNA in cultured fibroblasts Institute of Pathology, Technical University of Aachen, Aachen, Germany.Rhanjit]; Rene, Peter Merten [corrected to Mertens, Peter Rene].BACKGROUND: Recent findings of an impaired protein ratio of type I to type III procollagen showed a disturbed collagen metabolism in incisional hernia development.

We analyzed the type I and type III procollagen messenger RNA to investigate whether these findings represent the altered extracellular matrix or a primary defect at the transcriptional level.METHODS: We examined cultured skin fibroblasts of patients with incisional or recurrent incisional hernia in comparison with those without any previous incision (control) and those with a skin scar without clinical appearance of a hernia (scar). Immunohistochemical detection of a lowered protein ratio of type I and type III collagen in the hernia skin tissue leads to mRNA expression analysis. The procollagen mRNA and the ratio of type I to type III procollagen mRNA are detected by reverse transcriptase-polymerase chain reaction and Northern blot analysis, the collagens type I and III by Western blot analysis.RESULTS: Reverse transcriptase-polymerase chain reaction revealed an increase of type I procollagen mRNA in the incisional and recurrent hernia (00 +/- 04 and 19 +/- 04, respectively) compared with stable scar (04 +/- 02) or healthy tissue (03 +/- 01). The obvious rise of type III procollagen mRNA to 43 +/- 04 for incisional, 62 +/- 03 for recurrent hernia, 29 +/- 04 for stable scar, and 12 +/- 03 for the healthy tissue showed a significantly decreased ratio of type I to type III procollagen mRNA in the hernia patients as compared with the controls (P <1). By Western blot analysis, an increase of type I and type III collagen protein and a significant rise in the corresponding ratio in the recurrent hernia group were detected.


CONCLUSIONS: The altered synthesis of type I and type III collagen in cultured skin fibroblasts suggests a disorder of collagen metabolism, at least in patients with recurrent hernia. Hence, a basically impaired wound healing process is likely to contribute to the unsatisfactory results of incisional Genotypic and phenotypic analysis of 34 cases of inherited junctional epidermolysis bullosa caused by COL17A1 mutations.Dermatology, Referral Center for Genodermatoses, Centre Hospitalier Removal of collagen three-dimensional scaffold bubbles utilizing a vacuum of Nanjing Medical University, Changzhou City, Jiangsu Province, China.Nanjing Medical University, Changzhou City, Jiangsu Province, China.of Nanjing Medical University, Changzhou City, Jiangsu Province, China. The process of generating type I/II collagen scaffolds is fraught with bubble formation, which can interfere with the three-dimensional structure of the scaffold. Herein, we applied low-temperature vacuum freeze-drying to remove mixed air bubbles under negative pressure.

Type I and II rubber sponges were acid-solubilized via acid lysis and enzymolysis. Thereafter, vacuum negative pressure was applied to remove bubbles, and the cover glass press method was applied to shape the type I/II original scaffold. Vacuum negative pressure was applied for a second time to remove any residual bubbles. Subsequent application of carbamide/N-hydroxysuccinimide cross-linked the scaffold. The traditional method was used as the control group. The structure and number of residual bubbles and pore sizes of the two scaffolds were compared. Based on Purchase today between the pressure and the number of residual bubbles, a curve was created, and the time of ice formation was calculated.

The bubble content of the experimental group was significantly lower than that of the control group (P < 05). The pore diameter of the type I/II collagen scaffold was higher in the experimental group than in the control group. The time of icing effect of type I and II collagen solution was 1364 ± 56 and 1440 ± 65 s, respectively. The experimental scaffold had a more regular structure with actively proliferating chondrocytes that possessed adherent pseudopodia.

Website: http://en.wikipedia.org/wiki/Collagen