Carboxy-terminal propeptide of human type I collagen and pyridinium cross-links as markers of bone growth in infants 1 to 18 months of age

2009 ◽  
Vol 10 (6) ◽  
pp. 849-853 ◽  
Author(s):  
Mariska Lieuw-A-Fa ◽  
Rosa I. Sierra ◽  
Bonny L. Specker
Keyword(s):  
Bone Growth ◽  
Type I Collagen ◽  
Type I ◽  
Human Type ◽  
Cross Links ◽  
Carboxy Terminal

Bone resorption in healthy and osteoporotic postmenopausal women: comparison markers for serum carboxy-terminal telopeptide of type I collagen and urinary pyridinium cross-links

1994 ◽  
Vol 131 (3) ◽  
pp. 258-262 ◽  
Author(s):  
Matti J Välimäki ◽  
Riitta Tähtelä ◽  
James D Jones ◽  
James M Peterson ◽  
B Lawrence Riggs
Keyword(s):  
Bone Resorption ◽  
Bone Formation ◽  
Postmenopausal Women ◽  
Type I Collagen ◽  
Correlation Coefficients ◽  
Type I ◽  
Bone Specific Alkaline Phosphatase ◽  
Serum Ictp ◽  
Cross Links ◽  
Carboxy Terminal

Välimäki MJ, Tähtelä R, Jones JD, Peterson JM, Riggs BL. Bone resorption in healthy and osteoporotic postmenopausal women: comparison markers for serum carboxy-terminal telopeptide of type I collagen and urinary pyridinium cross-links. Eur J Endocrinol 1994;131:258–62. ISSN 0804–4643 We compared two highly specific markers for bone resorption–pyridinium cross-links (pyridinoline (PYR) and deoxypyridinoline (DPR)) in urine and carboxy-terminal telopeptide of type I collagen (ICTP) in serum – in 63 healthy postmenopausal women and 63 women with osteoporosis characterized by more bone resorption than bone formation. The ICTP, PYR and DPR levels were all higher, by 24% (p = 0.001), 16% (p = 0.05) and 25% (p = 0.004), respectively, in the osteoporotic women. For the merged groups, there were significant correlations between serum ICTP concentration and urinary PYR (r = 0.667, p < 0.0001) and DPR (r = 0.452, p < 0.0001) excretion; for the osteoporotic and normal women separately, the r values were 0.73 (p < 0.01) and 0.45 (p < 0.01) for PYR and 0.51 (p < 0.01) and 0.22 (p = 0.08) for DPR versus ICTP respectively. Weak correlations in linear regression between ICTP and various indices of bone formation (osteocalcin, bone-specific alkaline phosphatase and carboxy-terminal propeptide of type I procollagen) disappeared when the correlation between ICTP and pyridinolines was accounted for by calculation of partial correlation coefficients in multiple regression analysis. Serum ICTP concentration appears to discriminate between groups of normal and osteoporotic women as well as urinary pyridinium cross-links, which is thus far the most sensitive method for assessing bone resorption. Matti Välimäki, Third Department of Medicine, Helsinki University Central Hospital, SF-00290 Helsinki, Finland

scholarly journals Collagen molecular phenotypic switch between non-neoplastic and neoplastic canine mammary tissues

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Masahiko Terajima ◽  
Yuki Taga ◽  
Becky K. Brisson ◽  
Amy C. Durham ◽  
Kotaro Sato ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Mammary Gland ◽  
Mammary Carcinoma ◽  
Cancer Biology ◽  
Type I Collagen ◽  
Critical Role ◽  
Premature Death ◽  
Mammary Tissue ◽  
Type I ◽  
Cross Links

AbstractIn spite of major advances over the past several decades in diagnosis and treatment, breast cancer remains a global cause of morbidity and premature death for both human and veterinary patients. Due to multiple shared clinicopathological features, dogs provide an excellent model of human breast cancer, thus, a comparative oncology approach may advance our understanding of breast cancer biology and improve patient outcomes. Despite an increasing awareness of the critical role of fibrillar collagens in breast cancer biology, tumor-permissive collagen features are still ill-defined. Here, we characterize the molecular and morphological phenotypes of type I collagen in canine mammary gland tumors. Canine mammary carcinoma samples contained longer collagen fibers as well as a greater population of wider fibers compared to non-neoplastic and adenoma samples. Furthermore, the total number of collagen cross-links enriched in the stable hydroxylysine-aldehyde derived cross-links was significantly increased in neoplastic mammary gland samples compared to non-neoplastic mammary gland tissue. The mass spectrometric analyses of type I collagen revealed that in malignant mammary tumor samples, lysine residues, in particular those in the telopeptides, were markedly over-hydroxylated in comparison to non-neoplastic mammary tissue. The extent of glycosylation of hydroxylysine residues was comparable among the groups. Consistent with these data, expression levels of genes encoding lysyl hydroxylase 2 (LH2) and its molecular chaperone FK506-binding protein 65 were both significantly increased in neoplastic samples. These alterations likely lead to an increase in the LH2-mediated stable collagen cross-links in mammary carcinoma that may promote tumor cell metastasis in these patients.

scholarly journals Functional analysis of cis-acting DNA sequences controlling transcription of the human type I collagen genes.

1990 ◽  
Vol 265 (22) ◽  
pp. 13351-13356
Author(s):  
S Boast ◽  
M W Su ◽  
F Ramirez ◽  
M Sanchez ◽  
E V Avvedimento
Keyword(s):  
Functional Analysis ◽  
Dna Sequences ◽  
Type I Collagen ◽  
Type I ◽  
Cis Acting ◽  
Human Type ◽  
Collagen Genes

scholarly journals Protease-dependent versus -independent cancer cell invasion programs: three-dimensional amoeboid movement revisited

2009 ◽  
Vol 185 (1) ◽  
pp. 11-19 ◽  
Author(s):  
Farideh Sabeh ◽  
Ryoko Shimizu-Hirota ◽  
Stephen J. Weiss
Keyword(s):  
Cancer Cells ◽  
Type I Collagen ◽  
Three Dimensional ◽  
Amoeboid Movement ◽  
Type I ◽  
Collagen Network ◽  
Normal Tissues ◽  
Tissue Invasion ◽  
Absolute Requirement ◽  
Cross Links

Tissue invasion during metastasis requires cancer cells to negotiate a stromal environment dominated by cross-linked networks of type I collagen. Although cancer cells are known to use proteinases to sever collagen networks and thus ease their passage through these barriers, migration across extracellular matrices has also been reported to occur by protease-independent mechanisms, whereby cells squeeze through collagen-lined pores by adopting an ameboid phenotype. We investigate these alternate models of motility here and demonstrate that cancer cells have an absolute requirement for the membrane-anchored metalloproteinase MT1-MMP for invasion, and that protease-independent mechanisms of cell migration are only plausible when the collagen network is devoid of the covalent cross-links that characterize normal tissues.

scholarly journals Ιδιοπαθής υπερασβεστιουρία στην παιδική ηλικία

2017 ◽  
Author(s):  
Μαρία Παύλου
Keyword(s):  
Type I Collagen ◽  
Cross Linking ◽  
Type I ◽  
Nuclear Factor ◽  
Soluble Receptor ◽  
Calcium Sensing Receptor ◽  
Calcium Sensing ◽  
Receptor Activator ◽  
Carboxy Terminal ◽  
Nuclear Factor Kb

Η ιδιοπαθής υπερασβεστιουρία (ΙΥΑ) στα παιδιά έχει επιπολασμό 2,2-17,7%. Ποσοστό 2635% των ασθενών εμφανίζει μειωμένη οστική πυκνότητα, που αποδίδεται μάλλον σε αυξημένη οστική απορρόφηση και/ή οστικό ανασχηματισμό, καθώς καταγράφεται φυσιολογική κατά μήκος αύξηση των οστών στα περισσότερα παιδιά με ΙΥΑ. Περιορισμένες είναι οι μελέτες εκτίμησης βιοχημικών δεικτών οστικού μεταβολισμού, αλλά και γονιδιακού ελέγχου σε παιδιά με ΙΥΑ στην διεθνή βιβλιογραφία και καμία στην ελληνική. Επίσης, δεν πραγματοποιήθηκαν μελέτες εκτίμησης των κυτταροκινών οστεοκλαστογένεσης οστεοπροτεγερίνη (osteoprotegerin, OPG) και sRANKL (soluble receptor activator of nuclear factor kB ligand) σε ασθενείς με ΙΥΑ. Σκοπός της μελέτης ήταν η εκτίμηση των βιοχημικών δεικτών οστικής παραγωγής, αλκαλική φωσφατάση (alkaline phosphatase, ALP) και οστεοκαλσίνη (osteocalcin, OC) και οστικής απορρόφησης β-Crosslaps (serum Carboxy-terminal cross-linking telopeptide of type I collagen) και της OPG και sRANKL στον ορό σε παιδιά με ΙΥΑ. Επίσης έγινε γονιδιακή ανάλυση των πολυμορφισμών του γονιδίου του ασβεστιοευαίσθητου υποδοχέα (Calcium sensing Receptor, CaSR). Πενήντα παιδιά με ΙΥΑ αποτέλεσαν την ομάδα ασθενών και 60 υγιή παιδιά την ομάδα ελέγχου. Οι ασθενείς εκτιμήθηκαν κατά τον χρόνο της διάγνωσης και 3 μήνες μετά την εφαρμογή διαιτητικών οδηγιών αντιμετώπισης της ΙΥΑ. Οι ασθενείς της μελέτης μας είχαν σχετικά ήπια προς μέτρια υπερασβεστιουρία (6,49±2,03 mg/Kg/day) κατά την ένταξη στην μελέτη. Μετά την εφαρμογή των διατροφικών οδηγιών, μείωσαν σημαντικά τα επίπεδα του Ca στα ούρα 24ώρου και τον λόγο του Ca προς κρεατινίνη στα δείγματα ούρων, χωρίς όμως να φτάνουν τις φυσιολογικές τιμές. Τα επίπεδα της ALP και OC και το ύψος των ασθενών δεν διέφεραν από της ομάδας ελέγχου, που δείχνει ανεπηρέαστη οστική παραγωγή στους ασθενείς. Τα επίπεδα των β-Crosslaps των ασθενών, στους δύο χρόνους εκτίμησης, ήταν υψηλότερα από των μαρτύρων, ενώ καταγράφηκε τάση μείωσης της μέσης τιμής μετά την τρίμηνη παρέμβαση. Το εύρημα δείχνει αυξημένη οστική απορρόφηση στους ασθενείς με τάση βελτίωσης κατά τον επανέλεγχο. Ο λόγος β-Crosslaps/OC στους ασθενείς κατά την ένταξη στην μελέτη ήταν αυξημένος συγκριτικά με των μαρτύρων, καταγράφοντας υψηλότερο ρυθμό οστικής απορρόφησης συγκριτικά με οστικής παραγωγής. Τα επίπεδα των OPG και sRANKL των ασθενών, στους δύο χρόνους εκτίμησης δε διέφεραν από των μαρτύρων. Ωστόσο, ο λόγος sRANKL/OPG στους ασθενείς κατά την ένταξη στην μελέτη ήταν ελαφρά χαμηλότερος, πιθανά σαν απάντηση αντιρρόπησης του υψηλότερου ρυθμού οστεοκλαστογένεσης. Από την γονιδιακή ανάλυση των πολυμορφισμών A986S, R990G και Q1011E του CaSR, καταγράφηκε συσχέτιση μόνο του A986S με την ΙΥΑ στα παιδιά της μελέτης. Συμπερασματικά οι ασθενείς της μελέτης μας φαίνεται να έχουν φυσιολογική οστική παραγωγή, αλλά αυξημένη οστική απορρόφηση, που βελτιώθηκε μετά την παρέμβαση. Βρέθηκε συσχέτιση μόνο του πολυμορφισμού A986S του CaSR με την ΙΥΑ. Θεωρούμε χρήσιμη την εκτίμηση των βιοχημικών δεικτών οστικής παραγωγής ALP και OC και απορρόφησης β-Crosslaps στον ορό στα παιδιά με ΙΥΑ, ως μια μη επεμβατική μέθοδο ανίχνευσης διαταραχών οστικού μεταβολισμού και παρακολούθησης της αντιμετώπισης της.

Radioimmunoassay for the pyridinoline cross-linked carboxy-terminal telopeptide of type I collagen: a new serum marker of bone collagen degradation

1993 ◽  
Vol 39 (4) ◽  
pp. 635-640 ◽  
Author(s):  
J Risteli ◽  
I Elomaa ◽  
S Niemi ◽  
A Novamo ◽  
L Risteli
Keyword(s):  
Type I Collagen ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Bone Collagen ◽  
Collagen Molecule ◽  
Type I ◽  
Serum Samples ◽  
Amino Terminal ◽  
Wide Range ◽  
Carboxy Terminal

Abstract We developed a radioimmunoassay (RIA) for the carboxy-terminal telopeptides of type I collagen (ICTP), cross-linked with the helical domain of another type I collagen molecule, after isolation from human femoral bone. The cross-linked peptide was liberated by digesting insoluble, denatured bone collagen either with bacterial collagenase or with trypsin, and purified by two successive reversed-phase separations on HPLC, with monitoring of pyridinoline-specific fluorescence. The purity of the peptide was verified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and its origin in the type I collagen fibers was determined by amino-terminal amino acid sequencing. Polyclonal antibodies and a separation reagent containing second antibody and polyethylene glycol are used in the RIA. An immunologically identical, somewhat larger antigen is present in human serum; its concentration increases in multiple myeloma and in rheumatoid arthritis. The ICTP antigen seems to be cleared from the circulation by the kidneys, because glomerular filtration rates that are two-thirds of normal or less are associated with increased circulating ICTP concentrations. The CVs of the method are between 3% and 8% for a wide range of concentrations. The analysis of 40 serum samples can be completed in 4 h.

scholarly journals Bone Metabolism in Patients Treated for Depression

2020 ◽  
Vol 17 (13) ◽  
pp. 4756
Author(s):  
Elżbieta Skowrońska-Jóźwiak ◽  
Piotr Gałecki ◽  
Ewa Głowacka ◽  
Cezary Wojtyła ◽  
Przemysław Biliński ◽  
...  
Keyword(s):  
Bone Metabolism ◽  
Type I Collagen ◽  
Depression Scale ◽  
Type I ◽  
Hamilton Depression Scale ◽  
Recurrent Depression ◽  
Hydroxyvitamin D ◽  
Vitamin D Levels ◽  
Turnover Markers ◽  
Carboxy Terminal

Background: Depression and osteoporosis are severe public health problems. There are conflicting findings regarding the influence of depression on bone metabolism. The aim of the presented study was to compare bone turnover markers and vitamin D levels between patients treated for depression and healthy controls. Patients and Methods: We determined a concentration of osteocalcin, carboxy-terminal telopeptide of type I collagen (β-CTX), 25-hydroxyvitamin D (25OHD) and 1,25(OH)2D3 in 99 patients, aged 46.9 ± 11 years, treated for depression, as well as in 45 healthy subjects. Depressive status was determined with the Hamilton Depression Scale (HDRS). Results: In patients treated for depression, we demonstrated significantly lower osteocalcin concentrations (p < 0.03) and higher concentration of β-CTX (result on the border of significance; p = 0.08). Those relationship were stronger in women. The level of 25OHD and 1,25(OH)2D3 did not differ significantly between the examined groups. We observed a negative correlation between the 25OHD and HDRS score after treatment in all patients treated for depression and in subgroups of women and subjects with recurrent depression. Conclusions: Our results indicate that depression is related to disturbances in bone metabolism, especially in women and patients with recurrent depression, suggesting its role in context of osteoporosis development.

Serum Carboxy Terminal Telopeptide of Type I Collagen (ICTP) Predicts Progression of Left Ventricular LV Remodeling After Reperfused AMI

2009 ◽  
Vol 15 (7) ◽  
pp. S178-S179
Author(s):  
Akira Funayama ◽  
Tetsuro Shishido ◽  
Shigehiko Katou ◽  
Tatsuro Kitahara ◽  
Shunsuke Netsu ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Left Ventricular ◽  
Type I ◽  
Lv Remodeling ◽  
Carboxy Terminal

scholarly journals A Novel Role of Annexin A2 in Human Type I Collagen Gene Expression

2015 ◽  
Vol 116 (3) ◽  
pp. 408-417 ◽  
Author(s):  
Georgia Schäfer ◽  
Jessica K. Hitchcock ◽  
Tamlyn M. Shaw ◽  
Arieh A. Katz ◽  
M. Iqbal Parker
Keyword(s):  
Gene Expression ◽  
Type I Collagen ◽  
Annexin A2 ◽  
Type I ◽  
Collagen Gene ◽  
Human Type ◽  
Collagen Gene Expression
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