Urinary markers of type I collagen degradation in the dog

2000 ◽  
Vol 69 (2) ◽  
pp. 123-127 ◽  
Author(s):  
M.J ALLEN ◽  
L.C.V ALLEN ◽  
W.E HOFFMANN ◽  
D.C RICHARDSON ◽  
G.J BREUR
Keyword(s):  
Type I Collagen ◽  
Collagen Degradation ◽  
Type I ◽  
Urinary Markers

1. Type I collagen degradation by murine osteoblasts stimulated with 1,25(OH)2-vitamin D3: evidence for a plasminogen activator—plasmin—metalloproteinase cascade

Bone ◽  
1989 ◽  
Vol 10 (6) ◽  
pp. 471 ◽  
Author(s):  
BM Thomson ◽  
SJ Atkinson ◽  
AM McGarrity ◽  
RM Hembry ◽  
JJ Reynolds ◽  
...  
Keyword(s):  
Plasminogen Activator ◽  
Vitamin D3 ◽  
Type I Collagen ◽  
Collagen Degradation ◽  
Type I

Tissue inhibitor of metalloproteinases (TIMP) regulates extracellular type I collagen degradation by chondrocytes and endothelial cells

1987 ◽  
Vol 87 (2) ◽  
pp. 357-362
Author(s):  
J. Gavrilovic ◽  
R.M. Hembry ◽  
J.J. Reynolds ◽  
G. Murphy
Keyword(s):  
Endothelial Cells ◽  
Type I Collagen ◽  
Model System ◽  
Collagen Degradation ◽  
Type I ◽  
Tissue Inhibitor Of Metalloproteinases ◽  
Regulatory Factor ◽  
Tissue Inhibitor ◽  
Cells Cultured

A specific antiserum to purified rabbit tissue inhibitor of metalloproteinases (TIMP) was raised in sheep, characterized and used to investigate the role of TIMP in a model system. Chondrocytes and endothelial cells cultured on 14C-labelled type I collagen films and stimulated to produce collagenase were unable to degrade the films unless the anti-TIMP antibody was added. The degradation induced was inhibited by a specific anti-rabbit collagenase antibody. It was concluded that TIMP is a major regulatory factor in cell-mediated collagen degradation.

scholarly journals Matrix Metalloproteinase Mediated Type I Collagen Degradation — An Independent Risk Factor for Mortality in Women

EBioMedicine ◽  
2015 ◽  
Vol 2 (7) ◽  
pp. 723-729 ◽  
Author(s):  
K. Dragsbæk ◽  
J.S. Neergaard ◽  
H.B. Hansen ◽  
I. Byrjalsen ◽  
P. Alexandersen ◽  
...  
Keyword(s):  
Risk Factor ◽  
Matrix Metalloproteinase ◽  
Independent Risk Factor ◽  
Type I Collagen ◽  
Collagen Degradation ◽  
Type I

scholarly journals Oligogalacturonic acid inhibit bone resorption and collagen degradation through its interaction with type I collagen

2009 ◽  
Vol 78 (12) ◽  
pp. 1448-1455 ◽  
Author(s):  
Jean-Marc Lion ◽  
Romuald Mentaverri ◽  
Stéphanie Rossard ◽  
Nathalie Jullian ◽  
Bernard Courtois ◽  
...  
Keyword(s):  
Bone Resorption ◽  
Type I Collagen ◽  
Collagen Degradation ◽  
Type I ◽  
Inhibit Bone Resorption ◽  
Oligogalacturonic Acid

Immunoassay for quantifying type I collagen degradation products in urine evaluated

1994 ◽  
Vol 40 (11) ◽  
pp. 2022-2025 ◽  
Author(s):  
M Bonde ◽  
P Qvist ◽  
C Fledelius ◽  
B J Riis ◽  
C Christiansen
Keyword(s):  
Type I Collagen ◽  
Degradation Products ◽  
Mean Value ◽  
Collagen Degradation ◽  
Enzyme Linked Immunosorbent Assay ◽  
Bone Resorption Marker ◽  
Type I ◽  
Analytical Recovery ◽  
Collagen Degradation Products ◽  
Better Than

Abstract An enzyme-linked immunosorbent assay (ELISA) for measuring type I collagen degradation products in urine < 3 h was evaluated. The measuring range was 0.5-10.5 mg/L with a detection limit of 0.2 mg/L. Within-run and total CVs were 5.3% and 6.6%, respectively. Analytical recovery averaged 100%. The mean (+/- SD) concentrations in urine samples from a healthy premenopausal population (n = 102) were 250 +/- 110 mg/mol creatinine (Cr). A group of healthy postmenopausal women (n = 410) gave a mean value of 416 +/- 189 mg/mol Cr. Values obtained in the ELISA correlated well (r = 0.83) to HPLC values for the established bone resorption marker deoxypyridinoline (n = 214), slightly better than the correlation to hydroxyproline measurements (r = 0.78, n = 421). We conclude that the assay described here presents a useful tool for further elucidating the importance of type I collagen degradation products in urine.

scholarly journals Sex- and Age-Specific Reference Curves for Serum Markers of Bone Turnover in Healthy Children from 2 Months to 18 Years

2006 ◽  
Vol 92 (2) ◽  
pp. 443-449 ◽  
Author(s):  
Markus Rauchenzauner ◽  
Andrea Schmid ◽  
Peter Heinz-Erian ◽  
Klaus Kapelari ◽  
Gerda Falkensammer ◽  
...  
Keyword(s):  
Bone Formation ◽  
Type I Collagen ◽  
Bone Markers ◽  
Collagen Degradation ◽  
Specific Reference ◽  
Type I ◽  
Healthy Children ◽  
Pubertal Stage ◽  
Reference Curves ◽  
Carboxyterminal Telopeptide

Abstract Introduction: This study aimed to establish sex- and age-specific reference curves enabling the calculation of z-scores and to examine correlations between bone markers and anthropometric data. Methods: Morning blood samples were obtained from 572 healthy children and adolescents (300 boys) aged 2 months to 18 yr. Height, weight, and pubertal stage were recorded. Serum osteocalcin (OC), bone-specific alkaline phosphatase (BALP), type-1 collagen degradation markers [carboxyterminal telopeptide region of type I collagen (ICTP), carboxyterminal telopeptide α1 chain of type I collagen (CTX)], and tartrate-resistant acid phosphatase (TRAP5b) were measured. Cross-sectional centile charts were created for the 3rd, 50th, and 97th centiles. Results: Apart from TRAP5b, all bone markers were nonnormally distributed, requiring logarithmic (BALP, OC, ICTP) or square root (CTX) transformation. Back-transformed centile curves for age and sex are presented for practical use. All bone markers varied with age and pubertal stage (P < 0.001). Significant correlations were found between sd score (SDS) for bone formation markers BALP and OC (r = 0.13; P = 0.004), SDS for collagen degradation markers ICTP and CTX (r = 0.14; P = 0.002), and SDS for the phosphatases (r = 0.34, P < 0.001). Height and weight SDS correlated weakly with some bone marker SDS, particularly with lnBALP SDS (r = 0.20 and 0.24, respectively; both P < 0.001). Conclusion: This study provides reference curves for OC, BALP, CTX, ICTP, and TRAP5b in healthy children. Taller and heavier individuals for age had greater bone marker concentrations, likely reflecting greater growth velocity. SDS for markers of bone formation, collagen degradation, and phosphatases were each independently correlated, suggesting they derive from the same biological processes. The possibility of calculating SDS will facilitate monitoring of antiresorptive therapy or disease progression in children with metabolic bone disease.

Effect of MMP-13 degraded SPARC on type I collagen and its biomarker potential in colorectal cancer.

2018 ◽  
Vol 36 (4_suppl) ◽  
pp. 717-717
Author(s):  
Stephanie Nina Kehlet ◽  
Henrik Harling ◽  
Lars N Jørgensen ◽  
Morten A Karsdal ◽  
Nicholas Willumsen
Keyword(s):  
Colorectal Cancer ◽  
Type I Collagen ◽  
Collagen Degradation ◽  
Enzyme Linked Immunosorbent Assay ◽  
Matricellular Protein ◽  
Elisa Assay ◽  
Type I ◽  
Healthy Controls ◽  
Collagen Deposition

717 Background: Increased collagen deposition and remodeling of the extracellular matrix has been shown to play a role in the pathology of gastrointestinal cancer (GC). The matricellular protein SPARC (secreted proteome acidic and rich in cysteine) binds collagens and hereby regulates collagen fibrillogenesis. Matrix metalloproteinase (MMP) mediated cleavage of SPARC, increases the affinity for collagens up to 20-fold. SPARC has been shown to be overexpressed in GC patients and associated with GC cell invasion and metastasis. Increased expression and cleavage of SPARC might therefore be implicated in GC pathology by increasing collagen deposition. Here, we present the development and validation of a competitive enzyme-linked immunosorbent assay (ELISA) quantifying a specific MMP-13 generated fragment of SPARC - a cleavage site involved in increased collagen affinity. The biomarker potential of this fragment was examined in serum from colorectal cancer (CRC) patients and healthy controls. Moreover, we evaluated the ability of cleaved SPARC to prevent type I collagen degradation in vitro. Methods: A monoclonal antibody was raised against a MMP-13-generated neo-epitope of SPARC and a competitive ELISA assay (SPARC-M) was developed and technically validated. Serum levels were assessed in CRC patients (n=50) and healthy controls (n=30). The ability of cleaved SPARC to prevent collagen degradation was investigated using an ELISA assay measuring type I collagen degradation by MMP-9. Results: SPARC-M was technically robust and specific for SPARC cleaved by MMP-13. The fragment was elevated in CRC patients when compared to healthy controls (p=0.0097). When MMP-13 degraded SPARC was incubated with type I collagen and MMP-9, type I collagen degradation was completely inhibited suggesting that SPARC increases collagen deposition by preventing collagen degradation. Conclusions: SPARC-M was significantly elevated in CRC patients compared to healthy controls suggesting biomarker potential. Biologically, cleaved SPARC may prevent type I collagen degradation hereby leading to a pro-tumorigenic environment. Larger clinical studies are needed to validate the clinical use of this biomarker in GC.

Cleavage Site Specificity and Conformational Selection in Type I Collagen Degradation

Biochemistry ◽  
2010 ◽  
Vol 49 (19) ◽  
pp. 4147-4158 ◽  
Author(s):  
Ramon Salsas-Escat ◽  
Paul S. Nerenberg ◽  
Collin M. Stultz
Keyword(s):  
Cleavage Site ◽  
Type I Collagen ◽  
Collagen Degradation ◽  
Site Specificity ◽  
Type I ◽  
Conformational Selection
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