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Thomas F E Barth - One of the best experts on this subject based on the ideXlab platform.
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loss of Collagen Type iv in rheumatoid synovia and cytokine effect on the Collagen Type iv gene expression in fibroblast like synoviocytes from rheumatoid arthritis
Virchows Archiv, 2001Co-Authors: N Rinaldi, M Willhauck, D Weis, B Brado, P Kern, M Lukoschek, M Schwarzeywill, Thomas F E BarthAbstract:Collagen Type IV is a structural matrix protein which contributes to the structural organization of the synovia. In order to characterize the distribution of this protein in synovia with chronic synovitis, Collagen Type IV was detected by immunochemistry in normal synovia and in synovia from patients with osteoarthritis (OA) and rheumatoid arthritis (RA). A decrease of Collagen Type IV was observed in synovial layers of rheumatoid synovia, which statistically correlated with the grade of inflammation and with the thickness of the synovial layer. In vitro, we found no differences in the gene expression of Collagen Type IV in cultures of fibroblast-like synoviocytes (FLS) derived from OA and RA using a reverse-transcriptase polymerase chain reaction. Nevertheless, we observed a downregulating effect of tumor necrosis factor-alpha and interleukin (IL)-1beta on the gene expression of Collagen Type IV only in FLS isolated from patients with RA. The effect of IL-1beta was dose dependent. In summary, we observed an inflammation-associated decrease of Collagen Type IV in the synovial layer of rheumatoid synovia. Inflammatory cytokines may play a role in regulating the synthesis of Collagen Type IV in the rheumatoid process in vivo.
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Loss of Collagen Type IV in rheumatoid synovia and cytokine effect on the Collagen Type-IV gene expression in fibroblast-like synoviocytes from rheumatoid arthritis.
Virchows Archiv, 2001Co-Authors: N Rinaldi, M Willhauck, D Weis, B Brado, P Kern, M Lukoschek, M. Schwarz-eywill, Thomas F E BarthAbstract:Collagen Type IV is a structural matrix protein which contributes to the structural organization of the synovia. In order to characterize the distribution of this protein in synovia with chronic synovitis, Collagen Type IV was detected by immunochemistry in normal synovia and in synovia from patients with osteoarthritis (OA) and rheumatoid arthritis (RA). A decrease of Collagen Type IV was observed in synovial layers of rheumatoid synovia, which statistically correlated with the grade of inflammation and with the thickness of the synovial layer. In vitro, we found no differences in the gene expression of Collagen Type IV in cultures of fibroblast-like synoviocytes (FLS) derived from OA and RA using a reverse-transcriptase polymerase chain reaction. Nevertheless, we observed a downregulating effect of tumor necrosis factor-α and interleukin (IL)-1β on the gene expression of Collagen Type IV only in FLS isolated from patients with RA. The effect of IL-1β was dose dependent. In summary, we observed an inflammation-associated decrease of Collagen Type IV in the synovial layer of rheumatoid synovia. Inflammatory cytokines may play a role in regulating the synthesis of Collagen Type IV in the rheumatoid process in vivo.
Narayan C. Mishra - One of the best experts on this subject based on the ideXlab platform.
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surface modification of nanofibrous polycaprolactone gelatin composite scaffold by Collagen Type i grafting for skin tissue engineering
Materials Science and Engineering: C, 2014Co-Authors: Sneh Gautam, Amit Kumar Dinda, Pravin D. Potdar, Chia-fu Chou, Narayan C. MishraAbstract:Abstract In the present study, a tri-polymer polycaprolactone (PCL)/gelatin/Collagen Type I composite nanofibrous scaffold has been fabricated by electrospinning for skin tissue engineering and wound healing applications. Firstly, PCL/gelatin nanofibrous scaffold was fabricated by electrospinning using a low cost solvent mixture [chloroform/methanol for PCL and acetic acid (80% v/v) for gelatin], and then the nanofibrous PCL/gelatin scaffold was modified by Collagen Type I (0.2–1.5 wt.%) grafting. Morphology of the Collagen Type I-modified PCL/gelatin composite scaffold that was analyzed by field emission scanning electron microscopy (FE-SEM), showed that the fiber diameter was increased and pore size was decreased by increasing the concentration of Collagen Type I. Fourier transform infrared (FT-IR) spectroscopy and thermogravimetric (TG) analysis indicated the surface modification of PCL/gelatin scaffold by Collagen Type I immobilization on the surface of the scaffold. MTT assay demonstrated the viability and high proliferation rate of L929 mouse fibroblast cells on the Collagen Type I-modified composite scaffold. FE-SEM analysis of cell-scaffold construct illustrated the cell adhesion of L929 mouse fibroblasts on the surface of scaffold. Characteristic cell morphology of L929 was also observed on the nanofiber mesh of the Collagen Type I-modified scaffold. Above results suggest that the Collagen Type I-modified PCL/gelatin scaffold was successful in maintaining characteristic shape of fibroblasts, besides good cell proliferation. Therefore, the fibroblast seeded PCL/gelatin/Collagen Type I composite nanofibrous scaffold might be a potential candidate for wound healing and skin tissue engineering applications.
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surface modification of nanofibrous polycaprolactone gelatin composite scaffold by Collagen Type i grafting for skin tissue engineering
Materials Science and Engineering: C, 2014Co-Authors: Sneh Gautam, Amit Kumar Dinda, Pravin D. Potdar, Chia-fu Chou, Narayan C. MishraAbstract:Abstract In the present study, a tri-polymer polycaprolactone (PCL)/gelatin/Collagen Type I composite nanofibrous scaffold has been fabricated by electrospinning for skin tissue engineering and wound healing applications. Firstly, PCL/gelatin nanofibrous scaffold was fabricated by electrospinning using a low cost solvent mixture [chloroform/methanol for PCL and acetic acid (80% v/v) for gelatin], and then the nanofibrous PCL/gelatin scaffold was modified by Collagen Type I (0.2–1.5 wt.%) grafting. Morphology of the Collagen Type I-modified PCL/gelatin composite scaffold that was analyzed by field emission scanning electron microscopy (FE-SEM), showed that the fiber diameter was increased and pore size was decreased by increasing the concentration of Collagen Type I. Fourier transform infrared (FT-IR) spectroscopy and thermogravimetric (TG) analysis indicated the surface modification of PCL/gelatin scaffold by Collagen Type I immobilization on the surface of the scaffold. MTT assay demonstrated the viability and high proliferation rate of L929 mouse fibroblast cells on the Collagen Type I-modified composite scaffold. FE-SEM analysis of cell-scaffold construct illustrated the cell adhesion of L929 mouse fibroblasts on the surface of scaffold. Characteristic cell morphology of L929 was also observed on the nanofiber mesh of the Collagen Type I-modified scaffold. Above results suggest that the Collagen Type I-modified PCL/gelatin scaffold was successful in maintaining characteristic shape of fibroblasts, besides good cell proliferation. Therefore, the fibroblast seeded PCL/gelatin/Collagen Type I composite nanofibrous scaffold might be a potential candidate for wound healing and skin tissue engineering applications.
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Surface modification of nanofibrous polycaprolactone/gelatin composite scaffold by Collagen Type I grafting for skin tissue engineering.
Materials Science and Engineering: C, 2013Co-Authors: Sneh Gautam, Amit Kumar Dinda, Pravin D. Potdar, Chia-fu Chou, Narayan C. MishraAbstract:In the present study, a tri-polymer polycaprolactone (PCL)/gelatin/Collagen Type I composite nanofibrous scaffold has been fabricated by electrospinning for skin tissue engineering and wound healing applications. Firstly, PCL/gelatin nanofibrous scaffold was fabricated by electrospinning using a low cost solvent mixture [chloroform/methanol for PCL and acetic acid (80% v/v) for gelatin], and then the nanofibrous PCL/gelatin scaffold was modified by Collagen Type I (0.2-1.5wt.%) grafting. Morphology of the Collagen Type I-modified PCL/gelatin composite scaffold that was analyzed by field emission scanning electron microscopy (FE-SEM), showed that the fiber diameter was increased and pore size was decreased by increasing the concentration of Collagen Type I. Fourier transform infrared (FT-IR) spectroscopy and thermogravimetric (TG) analysis indicated the surface modification of PCL/gelatin scaffold by Collagen Type I immobilization on the surface of the scaffold. MTT assay demonstrated the viability and high proliferation rate of L929 mouse fibroblast cells on the Collagen Type I-modified composite scaffold. FE-SEM analysis of cell-scaffold construct illustrated the cell adhesion of L929 mouse fibroblasts on the surface of scaffold. Characteristic cell morphology of L929 was also observed on the nanofiber mesh of the Collagen Type I-modified scaffold. Above results suggest that the Collagen Type I-modified PCL/gelatin scaffold was successful in maintaining characteristic shape of fibroblasts, besides good cell proliferation. Therefore, the fibroblast seeded PCL/gelatin/Collagen Type I composite nanofibrous scaffold might be a potential candidate for wound healing and skin tissue engineering applications.
N Rinaldi - One of the best experts on this subject based on the ideXlab platform.
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loss of Collagen Type iv in rheumatoid synovia and cytokine effect on the Collagen Type iv gene expression in fibroblast like synoviocytes from rheumatoid arthritis
Virchows Archiv, 2001Co-Authors: N Rinaldi, M Willhauck, D Weis, B Brado, P Kern, M Lukoschek, M Schwarzeywill, Thomas F E BarthAbstract:Collagen Type IV is a structural matrix protein which contributes to the structural organization of the synovia. In order to characterize the distribution of this protein in synovia with chronic synovitis, Collagen Type IV was detected by immunochemistry in normal synovia and in synovia from patients with osteoarthritis (OA) and rheumatoid arthritis (RA). A decrease of Collagen Type IV was observed in synovial layers of rheumatoid synovia, which statistically correlated with the grade of inflammation and with the thickness of the synovial layer. In vitro, we found no differences in the gene expression of Collagen Type IV in cultures of fibroblast-like synoviocytes (FLS) derived from OA and RA using a reverse-transcriptase polymerase chain reaction. Nevertheless, we observed a downregulating effect of tumor necrosis factor-alpha and interleukin (IL)-1beta on the gene expression of Collagen Type IV only in FLS isolated from patients with RA. The effect of IL-1beta was dose dependent. In summary, we observed an inflammation-associated decrease of Collagen Type IV in the synovial layer of rheumatoid synovia. Inflammatory cytokines may play a role in regulating the synthesis of Collagen Type IV in the rheumatoid process in vivo.
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Loss of Collagen Type IV in rheumatoid synovia and cytokine effect on the Collagen Type-IV gene expression in fibroblast-like synoviocytes from rheumatoid arthritis.
Virchows Archiv, 2001Co-Authors: N Rinaldi, M Willhauck, D Weis, B Brado, P Kern, M Lukoschek, M. Schwarz-eywill, Thomas F E BarthAbstract:Collagen Type IV is a structural matrix protein which contributes to the structural organization of the synovia. In order to characterize the distribution of this protein in synovia with chronic synovitis, Collagen Type IV was detected by immunochemistry in normal synovia and in synovia from patients with osteoarthritis (OA) and rheumatoid arthritis (RA). A decrease of Collagen Type IV was observed in synovial layers of rheumatoid synovia, which statistically correlated with the grade of inflammation and with the thickness of the synovial layer. In vitro, we found no differences in the gene expression of Collagen Type IV in cultures of fibroblast-like synoviocytes (FLS) derived from OA and RA using a reverse-transcriptase polymerase chain reaction. Nevertheless, we observed a downregulating effect of tumor necrosis factor-α and interleukin (IL)-1β on the gene expression of Collagen Type IV only in FLS isolated from patients with RA. The effect of IL-1β was dose dependent. In summary, we observed an inflammation-associated decrease of Collagen Type IV in the synovial layer of rheumatoid synovia. Inflammatory cytokines may play a role in regulating the synthesis of Collagen Type IV in the rheumatoid process in vivo.
Romana A. Nowak - One of the best experts on this subject based on the ideXlab platform.
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Leuprolide acetate-treated leiomyomas retain their relative overexpression of Collagen Type I and Collagen Type III messenger ribonucleic acid.
Journal of the Society for Gynecologic Investigation, 1998Co-Authors: Elizabeth A. Stewart, Alan R. Rhoades, Romana A. NowakAbstract:OBJECTIVE To evaluate the levels of mRNA for the extracellular matrix proteins Collagen Type I, Collagen Type III, and fibronectin in leiomyomas and myometrium obtained from women treated with GnRH-agonist (GnRH-a) and to examine steroid hormone regulation of these proteins using an in vitro explant culture system. METHODS Northern blot analysis of mRNA was obtained from hysterectomy specimens at the time of surgery or after 48 hours of in vitro steroid treatment. A portion of the tissue was processed for RNA, and the remaining tissue was used to establish explant cultures. Extracellular matrix/alpha-tubulin ratio was computed for each band, and within each experiment the lowest ratio was standardized to a value of one densitometry unit to allow for comparison among experiments. RESULTS There is a relative overexpression of both Collagen Type I and Collagen Type III mRNAs but not fibronectin in leiomyomas compared to myometrium from the same uteri of women treated with GnRH-a. CONCLUSION Leiomyomas obtained from women treated with GnRH-a show an up-regulation of Collagens Type I and Type III similar to that seen in leiomyomas obtained from women in the proliferative phase of their menstrual cycles.
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Increased expression of messenger RNA for Collagen Type I, Collagen Type III, and fibronectin in myometrium of pregnancy.
Obstetrics and gynecology, 1995Co-Authors: Elizabeth A. Stewart, Amy E. Floor, Prachee Jain, Romana A. NowakAbstract:Objective: To determine the expression of the extracellular matrix proteins Collagen Type I, Collagen Type III, and fibronectin by immunohistochemistry, and the messenger RNA (mRNA) for these proteins by Northern blot analysis in the myometrium of pregnancy compared with myometrium from normal premenopausal women. Methods: Myometrial tissue was obtained from seven pregnant women undergoing elective cesarean delivery and eight nonpregnant premenopansal women undergoing hysterectomy. Tissue was paraffin embedded and processed for RNA. Antibodies to Collagen Type I, Collagen Type III, and fibronectin were used to examine protein expression by immunohistochemistry. Complimentary DNA probes for the same proteins were used to examine mRNA expression by Northern blot analysis. Results: Increased staining was seen for all three proteins in the myometrium of pregnancy. Densitometric analysis of Northern blots showed increased levels of Collagen Type I mRNA ( P P P Conclusion: There is increased expression of both protein and mRNA for Collagen Type I, Collagen Type III, and fibronectin in the myometrium of pregnancy.
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relative overexpression of Collagen Type i and Collagen Type iii messenger ribonucleic acids by uterine leiomyomas during the proliferative phase of the menstrual cycle
The Journal of Clinical Endocrinology and Metabolism, 1994Co-Authors: Elizabeth A. Stewart, Andrew J Friedman, Kimberly Peck, Romana A. NowakAbstract:Uterine leiomyomas contain abundant quantities of extracellular matrix (ECM). We characterized the localization of three ECM proteins, Collagen Type I, Collagen Type III, and fibronectin, in leiomyomas and adjacent normal myometrium. We further examined the expression of messenger ribonucleic acid (mRNA) levels for these proteins from 1) women who were in various stages of the menstrual cycle and 2) multiple leiomyomas from the same patient. Immunohistochemical staining showed that fibronectin was localized primarily around individual smooth muscle cells (SMC). Collagen Type I was distributed across the ECM and also in the cytoplasm of SMC. Collagen Type III was found primarily in the ECM. Leiomyomas showed more intense staining for Collagen Types I and III than corresponding normal myometrium. Northern blot and densitometric analysis showed that both Collagen Type I and III mRNAs were consistently elevated in leiomyomas relative to the adjacent myometrium in patients who were in the proliferative phase o...
M Lukoschek - One of the best experts on this subject based on the ideXlab platform.
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loss of Collagen Type iv in rheumatoid synovia and cytokine effect on the Collagen Type iv gene expression in fibroblast like synoviocytes from rheumatoid arthritis
Virchows Archiv, 2001Co-Authors: N Rinaldi, M Willhauck, D Weis, B Brado, P Kern, M Lukoschek, M Schwarzeywill, Thomas F E BarthAbstract:Collagen Type IV is a structural matrix protein which contributes to the structural organization of the synovia. In order to characterize the distribution of this protein in synovia with chronic synovitis, Collagen Type IV was detected by immunochemistry in normal synovia and in synovia from patients with osteoarthritis (OA) and rheumatoid arthritis (RA). A decrease of Collagen Type IV was observed in synovial layers of rheumatoid synovia, which statistically correlated with the grade of inflammation and with the thickness of the synovial layer. In vitro, we found no differences in the gene expression of Collagen Type IV in cultures of fibroblast-like synoviocytes (FLS) derived from OA and RA using a reverse-transcriptase polymerase chain reaction. Nevertheless, we observed a downregulating effect of tumor necrosis factor-alpha and interleukin (IL)-1beta on the gene expression of Collagen Type IV only in FLS isolated from patients with RA. The effect of IL-1beta was dose dependent. In summary, we observed an inflammation-associated decrease of Collagen Type IV in the synovial layer of rheumatoid synovia. Inflammatory cytokines may play a role in regulating the synthesis of Collagen Type IV in the rheumatoid process in vivo.
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Loss of Collagen Type IV in rheumatoid synovia and cytokine effect on the Collagen Type-IV gene expression in fibroblast-like synoviocytes from rheumatoid arthritis.
Virchows Archiv, 2001Co-Authors: N Rinaldi, M Willhauck, D Weis, B Brado, P Kern, M Lukoschek, M. Schwarz-eywill, Thomas F E BarthAbstract:Collagen Type IV is a structural matrix protein which contributes to the structural organization of the synovia. In order to characterize the distribution of this protein in synovia with chronic synovitis, Collagen Type IV was detected by immunochemistry in normal synovia and in synovia from patients with osteoarthritis (OA) and rheumatoid arthritis (RA). A decrease of Collagen Type IV was observed in synovial layers of rheumatoid synovia, which statistically correlated with the grade of inflammation and with the thickness of the synovial layer. In vitro, we found no differences in the gene expression of Collagen Type IV in cultures of fibroblast-like synoviocytes (FLS) derived from OA and RA using a reverse-transcriptase polymerase chain reaction. Nevertheless, we observed a downregulating effect of tumor necrosis factor-α and interleukin (IL)-1β on the gene expression of Collagen Type IV only in FLS isolated from patients with RA. The effect of IL-1β was dose dependent. In summary, we observed an inflammation-associated decrease of Collagen Type IV in the synovial layer of rheumatoid synovia. Inflammatory cytokines may play a role in regulating the synthesis of Collagen Type IV in the rheumatoid process in vivo.