Low-dose prednisolone in early rheumatoid arthritis inhibits collagen type I degradation by matrix metalloproteinases as assessed by serum 1CTP--a possible mechanism for specific inhibition of radiological destruction

Most rheumatic diseases, including rheumatoid arthritis (RA), are characterized by immune disorders that affect antibody activity. In the present study, using Dot blot and ELISA assay, we showed that patients with rheumatic disease produced significantly more antibodies against lipopolysaccharide (LPS) P. mirabilis O3 compared to healthy donors (p < 0.05), and affinity purified antibodies against LPS O3 may cross-react with collagen type I. It was demonstrated that purified of antibodies isolated from RA patients sera, reacted stronger with the collagen than healthy donors (p = 0.015), and cross-reaction was correlated with level of anti-citrullinated peptide antibodies (r = 0.7, p = 0.003). Moreover, using six different lipopolysaccharides were demonstrated the significant correlations in sera reactivity among lysine-containing lipopolysaccharides observed in patients’ sera (p < 0.05). Using Attenuated Total Reflection Fourier Transform Infrared Spectroscopy (ATR-FTIR) it was shown that unique wavenumbers of sera spectra correlate with reactivity with lipopolysaccharides allowing distinguish patients from healthy blood donors. Antibodies adsorption by synthetic antigens shows that in patients’ group anti-LPS O3 antibodies can be adsorbed by both amides of galacturonic acid and lysine or threonine, which suggests less specificity of antibodies binding with non-carbohydrate LPS component. The observed correlations suggest that non-carbohydrate components of LPS may be an important epitope for less specific anti-LPS antibodies, which might lead to cross-reactions and affect disease development.

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Effect of a Collagen-Based Compound on Morpho-Functional Properties of Cultured Human Tenocytes

Cells ◽

10.3390/cells7120246 ◽

2018 ◽

Vol 7 (12) ◽

pp. 246 ◽

Cited By ~ 4

Author(s):

Filippo Randelli ◽

Alessandra Menon ◽

Alessio Giai Via ◽

Manuel Mazzoleni ◽

Fabio Sciancalepore ◽

...

Keyword(s):

Matrix Metalloproteinases ◽

Collagen Type ◽

Clinical Investigation ◽

Pain Syndrome ◽

Collagen Type I ◽

Type I ◽

Mrna Levels ◽

Collagen Turnover ◽

And Migration ◽

Proliferation And Migration

Background: Greater Trochanter Pain Syndrome (GTPS) is the main reason for recalcitrant lateral hip pain. Gluteus medius and minimus tendinopathy plays a key role in this setting. An injectable medical compound containing collagen type I (MD-Tissue, Guna) has been produced with the aim to counteract the physiological and pathological degeneration of tendons. In this study we aimed at characterizing the effect of this medical compound on cultured human gluteal tenocytes, focusing on the collagen turnover pathways, in order to understand how this medical compound could influence tendon biology and healing. Methods: Tenocytes were obtained from gluteal tendon fragments collected in eight patients without any gluteal tendon pathology undergoing total hip replacement through an anterior approach. Cell proliferation and migration were investigated by growth curves and wound healing assay, respectively. The expression of genes and proteins involved in collagen turnover were analysed by real-time PCR, Slot blot and SDS-zymography. Results: Our data show that tenocytes cultured on MD-Tissue, compared to controls, have increased proliferation rate and migration potential. MD-Tissue induced collagen type I (COL-I) secretion and mRNA levels of tissue inhibitor of matrix metalloproteinases (MMP)-1 (TIMP-1). Meanwhile, lysyl hydroxylase 2b and matrix metalloproteinases (MMP)-1 and -2, involved, respectively, in collagen maturation and degradation, were not affected. Conclusions: Considered as a whole, our results suggest that MD-Tissue could induce in tenocytes an anabolic phenotype by stimulating tenocyte proliferation and migration and COL-I synthesis, maturation, and secretion, thus favouring tendon repair. In particular, based on its effect on gluteal tenocytes, MD-Tissue could be effective in the discouraging treatment of GTPS. From now a rigorous clinical investigation is desirable to understand the real clinical potentials of this compound.

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Collagen type I, III and V differently modulate synthesis and activation of matrix metalloproteinases by cultured rabbit periosteal fibroblasts

Matrix Biology ◽

10.1016/s0945-053x(03)00035-0 ◽

2003 ◽

Vol 22 (3) ◽

pp. 217-227 ◽

Cited By ~ 19

Author(s):

Erica H.M. Kerkvliet ◽

Ineke C. Jansen ◽

Ton Schoenmaker ◽

Wouter Beertsen ◽

Vincent Everts

Keyword(s):

Matrix Metalloproteinases ◽

Collagen Type ◽

Collagen Type I ◽

Type I

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The Association of Gene Polymorphisms of Matrix Metalloproteinases (-9, -12 and -20) and Collagen Type I Degradation Products With the Remodeling of the Left Ventricle in Patients With Acute Myocardial Infarction

Kardiologiia ◽

10.18087/cardio.2018.3.10093 ◽

2018 ◽

Vol 17 (3) ◽

pp. 13-19

Author(s):

N. A. Sokolova ◽

◽

M. S. Danshova ◽

A. V. Govorin ◽

D. N. Zaytsev ◽

...

Keyword(s):

Myocardial Infarction ◽

Acute Myocardial Infarction ◽

Matrix Metalloproteinases ◽

Left Ventricle ◽

Gene Polymorphisms ◽

Collagen Type ◽

Degradation Products ◽

Collagen Type I ◽

Type I ◽

Matrix Metalloproteinases 9

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Ηλεκτροφυσιολογικές και ηλεκτροανατομικές ιδιότητες του δεξιού κόλπου σε ασθενείς με εμμένουσα κολπική μαρμαρυγή

10.12681/eadd/36485 ◽

2015 ◽

Author(s):

Χρήστος Γουδής

Keyword(s):

Matrix Metalloproteinases ◽

Matrix Metalloproteinase ◽

Collagen Type ◽

Collagen Type I ◽

Type I ◽

Tissue Inhibitor ◽

Matrix Metalloproteinase 1

Σκοπός: Η κολπική μαρμαρυγή σχετίζεται με παθολογικό κολπικό υπόστρωμα. Στην παρούσα μελέτη διερευνήθηκε αν ασθενείς με μονήρη εμμένουσα κολπική μαρμαρυγή και ασθενείς με εμμένουσα κολπική μαρμαρυγή και μη ισχαιμική διατατική μυοκαρδιοπάθεια παρουσιάζουν διαφορές στις ηλεκτροφυσιολογικές και ηλεκτροανατομικές ιδιότητες του δεξιού κόλπου και στους βιοχημικούς δείκτες των μεταβολών του κολλαγόνου. Επίσης διερευνήθηκε η σχέση μεταξύ των δυναμικών του δεξιού κόλπου και των βιοχημικών δεικτών μεταβολών του κολλαγόνου στις δύο ομάδες.Μέθοδοι: Δέκα ασθενείς με εμμένουσα μονήρη κολπική μαρμαρυγή και οκτώ ασθενείς με εμμένουσα κολπική μαρμαρυγή και μη ισχαιμική διατατική μυοκαρδιοπάθεια συμπεριλήφθηκαν στη μελέτη. Προσδιορίστηκαν οι χρόνοι ανάνηψης του φλεβοκόμβου και οι δραστικές ανερέθιστες περίοδοι σε μήκη κύκλου 600ms, 500ms και 400ms, στο υψηλό και χαμηλό πλάγιο τοίχωμα δεξιού κόλπου, στον εγγύ στεφανιαίο κόλπο και δεξιό κολπικό ωτίο, και χαρτογραφήθηκε ο δεξιός κόλπος. Το αμινοτελικό προπεπτίδιο του κολλαγόνου τύπου Ι (serum N-terminal propeptide of collagen type I-PINP) και ο ιστικός αναστολέας της μεταλλοπρωτεϊνάσης-1 (tissue inhibitor of matrix metalloproteinases, TIMP-1), υπολογίστηκαν ως βιοχημικοί δείκτες σύνθεσης του κολλαγόνου τύπου Ι, ενώ το διασταυρούμενο καρβοξυτελικό τελοπεπτίδιο του κολλαγόνου τύπου Ι (cross-linked C-terminal telopeptide of collagen type I-CTx) και η μεταλλοπρωτεϊνάση-1 (matrix metalloproteinase-1, MMP-1) ως βιοχημικοί δείκτες αποδόμησης του κολλαγόνου τύπου Ι μεταξύ των δύο ομάδων.Αποτελέσματα: Δε διαπιστώθηκε σημαντική διαφορά στους χρόνους ανάνηψης του φλεβοκόμβου, στις δραστικές ανερέθιστες περιόδους στο υψηλό και χαμηλό πλάγιο τοίχωμα δεξιού κόλπου σε μήκη κύκλου 600ms, στις δραστικές ανερέθιστες περιόδους στον εγγύ στεφανιαίο κόλπο και το δεξιό κολπικό ωτίο, στο μέσο δυναμικό του δεξιού κόλπου και στους βιοχημικούς δείκτες μεταβολών του κολλαγόνου μεταξύ των δύο ομάδων. Σε ασθενείς με μονήρη εμμένουσα κολπική μαρμαρυγή τα επίπεδα ορού του TIMP-1 σχετίζονται με τα μέσα δυναμικά στο υψηλό πλάγιο και υψηλό οπίσθιο τοίχωμα του δεξιού κόλπου. Συμπέρασμα: Ασθενείς με μονήρη εμμένουσα κολπική μαρμαρυγή και ασθενείς με εμμένουσα κολπική μαρμαρυγή και μη ισχαιμκή διατατική μυοκαρδιοπάθεια παρουσιάζουν παρόμοιες μεταβολές στις ηλεκτροφυσιολογικές και ηλεκτροανατομικές ιδιότητες του δεξιού κόλπου, καθώς και παρόμοιες δομικές μεταβολές. Επιπλέον, ο βιοχημικος δείκτης της σύνθεσης κολλαγόνου TIMP-1 σχετίζεται με τα μέσα δυναμικά στο υψηλό πλάγιο και υψηλό οπίσθιο τοίχωμα του δεξιού κόλπου σε ασθενείς με μονήρη εμμένουσα κολπική μαρμαρυγή.

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Matrix Metalloproteinases and Tissue Inhibitors of Metalloproteinases in Echinoderms: Structure and Possible Functions

Cells ◽

10.3390/cells10092331 ◽

2021 ◽

Vol 10 (9) ◽

pp. 2331

Author(s):

Igor Yu. Dolmatov ◽

Vladimir A. Nizhnichenko ◽

Lyudmila S. Dolmatova

Keyword(s):

Matrix Metalloproteinases ◽

Collagen Type ◽

Collagen Type I ◽

Tissue Inhibitors Of Metalloproteinases ◽

Type I ◽

Tissue Inhibitors ◽

Number Of Genes ◽

Genes Encoding ◽

Mechanisms Of Development ◽

Similar Domain

Echinoderms are one of the most ancient groups of invertebrates. The study of their genomes has made it possible to conclude that these animals have a wide variety of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs). The phylogenetic analysis shows that the MMPs and TIMPs underwent repeated duplication and active divergence after the separation of Ambulacraria (Echinodermata+Hemichordata) from the Chordata. In this regard the homology of the proteinases and their inhibitors between these groups of animals cannot be established. However, the MMPs of echinoderms and vertebrates have a similar domain structure. Echinoderm proteinases can be structurally divided into three groups—archetypal MMPs, matrilysins, and furin-activatable MMPs. Gelatinases homologous to those of vertebrates were not found in genomes of studied species and are probably absent in echinoderms. The MMPs of echinoderms possess lytic activity toward collagen type I and gelatin and play an important role in the mechanisms of development, asexual reproduction and regeneration. Echinoderms have a large number of genes encoding TIMPs and TIMP-like proteins. TIMPs of these animals, with a few exceptions, have a structure typical for this class of proteins. They contain an NTR domain and 10–12 conservatively located cysteine residues. Repeated duplication and divergence of TIMP genes of echinoderms was probably associated with an increase in the functional importance of the proteins encoded by them in the physiology of the animals.

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