Effect of concentric exercise on serum muscle and collagen markers

1993 ◽  
Vol 75 (3) ◽  
pp. 1272-1277 ◽  
Author(s):  
P. Virtanen ◽  
J. T. Viitasalo ◽  
J. Vuori ◽  
K. Vaananen ◽  
T. E. Takala
Keyword(s):  
Type I Collagen ◽  
Male Students ◽  
Type I ◽  
Subsequent Increase ◽  
Collagen Production ◽  
Amino Terminal ◽  
Type I Procollagen ◽  
Concentric Exercise ◽  
Marker Proteins ◽  
Collagen Markers

The effect of an acute bout of high-intensity concentric exercise on serum muscle and collagen marker proteins was studied in nine male students. The muscle-derived serum carbonic anhydrase III, myoglobin, and creatine kinase all increased as a result of the exercise. Serum type I procollagen carboxyterminal propeptide decreased at first but started to increase 2 days after the exercise. Serum galactosylhydroxylysyl glucosyltransferase was elevated immediately after the exercise. No significant changes were seen in the concentrations of serum amino-terminal propeptide of type III procollagen or 4-hydroxyproline. It seems that a single bout of heavy concentric exercise causes protein leakage from muscles and probably from the collagen-synthesizing cells of the connective tissue, which may be accompanied by an initial decrease and a subsequent increase in type I collagen production. The activation of type I collagen production seems to depend on the strain and damage of the musculoskeletal system.

Atrial natriuretic peptide, B-type natriuretic peptide, and serum collagen markers after acute myocardial infarction

2004 ◽  
Vol 96 (4) ◽  
pp. 1306-1311 ◽  
Author(s):  
Jarkko Magga ◽  
Mikko Puhakka ◽  
Seppo Hietakorpi ◽  
Kari Punnonen ◽  
Paavo Uusimaa ◽  
...  
Keyword(s):  
Myocardial Infarction ◽  
Acute Myocardial Infarction ◽  
Atrial Natriuretic Peptide ◽  
Natriuretic Peptide ◽  
Type I Collagen ◽  
Left Ventricular ◽  
Type I ◽  
Amino Terminal ◽  
Collagen Markers ◽  
Atrial Natriuretic

Experimental data suggest that atrial natriuretic peptide (ANP) and B-type natriuretic peptide (BNP) act locally as antifibrotic factors in heart. We investigated the interrelationships of natriuretic peptides and collagen markers in 93 patients receiving thrombolytic treatment for their first acute myocardial infarction (AMI). Collagen formation following AMI, evaluated as serum levels of amino terminal propeptide of type III procollagen, correlated with NH2-terminal proANP ( r = 0.45, P < 0.001), BNP ( r = 0.55, P < 0.001) and NH2-terminal proBNP ( r = 0.50, P < 0.01) on day 4 after thrombolysis. Levels of intact amino terminal propeptide of type I procollagen decreased by 34% ( P < 0.001), and levels of carboxy terminal cross-linked telopeptide of type I collagen (ICTP) increased by 65% ( P < 0.001). ICTP levels correlated with NH2-terminal proBNP ( r = 0.25, P < 0.05) and BNP ( r = 0.28, P < 0.05) on day 4. Our results suggest that ANP and BNP may act as regulators of collagen scar formation and left ventricular remodeling after AMI in humans. Furthermore, degradation of type I collagen is increased after AMI and may be regulated by BNP.

scholarly journals Serum concentrations of carboxyl-terminal propeptide of type I procollagen, amino-terminal propeptide of type III procollagen, cross-linked carboxyl-terminal telopeptide of type I collagen, and their interrelationships in schoolchildren

1997 ◽  
Vol 43 (9) ◽  
pp. 1577-1581 ◽  
Author(s):  
Patricia M Crofton ◽  
Jean C Wade ◽  
Mervyn R H Taylor ◽  
Celia V Holland
Keyword(s):  
Type I Collagen ◽  
Reference Intervals ◽  
Type I ◽  
High Turnover ◽  
Childhood Growth ◽  
Type Iii ◽  
Procollagen Type ◽  
Amino Terminal ◽  
Type I Procollagen ◽  
Carboxyl Terminal

Abstract We report pediatric age- and sex-specific 95% reference intervals for procollagen type I C-terminal propeptide (PICP), the cross-linked C-terminal telopeptide of type I collagen (ICTP), and procollagen type III N-terminal propeptide (P3NP), measured in plasma from 302 schoolchildren (156 boys, 146 girls) ages 4–19 years. All three markers displayed a significant variation with age (ANOVA P ≤0.0015). PICP showed no detectable increase during adolescence for either sex, but decreased towards adult concentrations after the age of puberty, with an earlier decrease for girls than for boys (P &lt;0.01). ICTP and P3NP both increased in pubertal-aged children (P &lt;0.05), with an earlier increase in girls than in boys (P &lt;0.05), before decreasing towards adult concentrations (P &lt;0.01). All three collagen markers were highly correlated with one another (P &lt;0.001). The patterns observed mirrored the childhood growth curve and reflected the high turnover of bone and soft tissue during childhood growth.

Discovery of a Lead Compound for Specific Inhibition of Type I Collagen Production in Fibrosis

2021 ◽  
Vol 12 (3) ◽  
pp. 477-484
Author(s):  
Branko Stefanovic ◽  
Heather A. Michaels ◽  
Adel Nefzi
Keyword(s):  
Type I Collagen ◽  
Type I ◽  
Specific Inhibition ◽  
Lead Compound ◽  
Collagen Production

scholarly journals Inhibition of type I collagen production by dermal fibroblasts upon contact with activated T cells: Different sensitivity to inhibition between systemic sclerosis and control fibroblasts

1998 ◽  
Vol 41 (11) ◽  
pp. 2039-2047 ◽  
Author(s):  
Carlo Chizzolini ◽  
Roger Rezzonico ◽  
Clio Ribbens ◽  
Danielle Burger ◽  
Frank A. Wollheim ◽  
...  
Keyword(s):  
T Cells ◽  
Systemic Sclerosis ◽  
Type I Collagen ◽  
Dermal Fibroblasts ◽  
Type I ◽  
Activated T Cells ◽  
Collagen Production ◽  
And Control

Role of the amino-terminal extrahelical region of type I collagen in directing the 4D overlap in fibrillogenesis

Biopolymers ◽  
1979 ◽  
Vol 18 (12) ◽  
pp. 3005-3014 ◽  
Author(s):  
Donald L. Helseth ◽  
Joseph H. Lechner ◽  
Arthur Veis
Keyword(s):  
Type I Collagen ◽  
Type I ◽  
Amino Terminal

scholarly journals Responses of Markers of Bone and Collagen Turnover to Exercise, Growth Hormone (GH) Administration, and GH Withdrawal in Trained Adult Males1

2000 ◽  
Vol 85 (1) ◽  
pp. 124-133 ◽  
Author(s):  
Jennifer D. Wallace ◽  
Ross C. Cuneo ◽  
Per Arne Lundberg ◽  
Thord Rosén ◽  
Jens Otto Lunde Jørgensen ◽  
...  
Keyword(s):  
Acute Exercise ◽  
Type I Collagen ◽  
Controlled Study ◽  
Bone Resorption Marker ◽  
Type I ◽  
Serum Osteocalcin ◽  
Collagen Turnover ◽  
Gh Treatment ◽  
Type I Procollagen ◽  
Procollagen Iii

To examine the interactions between acute exercise and GH on markers of bone and collagen turnover and to assess the potential for detecting GH abuse in athletes using these markers, we studied 17 aerobically trained males (age, 26.9 ± 1.5 yr). Sequential studies of exercise, GH administration, and GH withdrawal were undertaken. A randomized, controlled study of rest vs. exercise showed that exercise did not change serum osteocalcin; other markers of formation increased transiently (each P &lt; 0.001): bone-specific alkaline phosphatase (+16.1%), carboxyterminal propeptide of type I procollagen (+14.1%), and procollagen III N-terminal extension peptide (+5.0%). The carboxyterminal cross-linked telopeptide of type I collagen, a bone resorption marker, increased 9.7% (P = 0.018) in response to exercise. A randomized, double blind, placebo-controlled, parallel study of recombinant human GH treatment (0.15 IU/kg·day) for 1 week increased serum osteocalcin (net increase preexercise, +10.0%; P = 0.017), carboxyterminal propeptide of type I procollagen (+17.6%; P = 0.002), procollagen III N-terminal extension peptide (+48.4%; P = 0.001), and carboxyterminal cross-linked telopeptide of type I collagen (53.3%; P = 0.009). Disappearance half-times after cessation of recombinant human GH for pre- and postexercise markers ranged from 248–770 h. We conclude 1) endurance exercise transiently activates bone and collagen turnover; 2) brief GH administration results in similar but quantitatively greater augmentation; and 3) these data will assist in designing a GH detection strategy.

scholarly journals Reduced Serum Levels of Bone Formation Marker P1NP in Psoriasis

2021 ◽  
Vol 8 ◽  
Author(s):  
Julia Mentzel ◽  
Tabea Kynast ◽  
Johannes Kohlmann ◽  
Holger Kirsten ◽  
Matthias Blüher ◽  
...  
Keyword(s):  
Bone Formation ◽  
Bone Metabolism ◽  
Type I Collagen ◽  
Skin Inflammation ◽  
Serum Levels ◽  
Serum Markers ◽  
Chronic Inflammatory Disease ◽  
Type I ◽  
Patient Counseling ◽  
Type I Procollagen

Psoriasis is a chronic inflammatory disease of the skin and joints. More recent data emphasize an association with dysregulated glucose and fatty acid metabolism, obesity, elevated blood pressure and cardiac disease, summarized as metabolic syndrome. TNF-α and IL-17, central players in the pathogenesis of psoriasis, are known to impair bone formation. Therefore, the relation between psoriasis and bone metabolism parameters was investigated. Two serum markers of either bone formation—N-terminal propeptide of type I procollagen (P1NP) or bone resorption—C-terminal telopeptide of type I collagen (CTX-I)—were analyzed in a cohort of patients with psoriasis vulgaris. In patients with psoriasis, P1NP serum levels were reduced compared to gender-, age-, and body mass index-matched healthy controls. CTX-I levels were indistinguishable between patients with psoriasis and controls. Consistently, induction of psoriasis-like skin inflammation in mice decreases bone volume and activity of osteoblasts. Moreover, efficient anti-psoriatic treatment improved psoriasis severity, but did not reverse decreased P1NP level suggesting that independent of efficient skin treatment psoriasis did affect bone metabolism and might favor the development of osteoporosis. Taken together, evidence is provided that bone metabolism might be affected by psoriatic inflammation, which may have consequences for future patient counseling and disease monitoring.

Collagen fibrillogenesis in vitro: interaction of types I and V collagen regulates fibril diameter

1990 ◽  
Vol 95 (4) ◽  
pp. 649-657 ◽  
Author(s):  
D.E. Birk ◽  
J.M. Fitch ◽  
J.P. Babiarz ◽  
K.J. Doane ◽  
T.F. Linsenmayer
Keyword(s):  
Type I Collagen ◽  
Small Diameter ◽  
Collagen Molecule ◽  
Type I ◽  
Collagen Types ◽  
Type V Collagen ◽  
Amino Terminal ◽  
Type V ◽  
Fibril Diameter

The small-diameter fibrils of the chick corneal stroma are heterotypic, composed of both collagen types I and V. This tissue has a high concentration of type V collagen relative to other type I-containing tissues with larger-diameter fibrils, suggesting that heterotypic interactions may have a regulatory role in the control of fibril diameter. The interactions of collagen types I and V were studied using an in vitro self-assembly system. Collagens were purified from lathyritic chick embryos in the presence of protease inhibitors. The type V collagen preparations contained higher molecular weight forms of the alpha 1(V) and alpha 2(V) chains constituting 60–70% of the total. Rotary-shadow electron micrographs showed a persistence of a small, pepsin-sensitive terminal region in an amount consistent with that seen by electrophoresis. In vitro, this purified type V collagen formed thin fibrils with no apparent periodicity, while type I collagen fibrils had a broad distribution of large diameters. However, when type I collagen was mixed with increasing amounts of type V collagen a progressive and significant decrease in both the mean fibril diameter and the variance was observed for D periodic fibrils. The amino-terminal domain of the type V collagen molecule was required for this regulatory effect and in its absence little diameter reducing activity was observed. Electron microscopy using collagen type-specific monoclonal antibodies demonstrated that the fibrils formed were heterotypic, containing both collagen types I and V. These data indicate that the interaction of type V with type I collagen is one mechanism modulating fibril diameter and is at least partially responsible for the regulation of collagen fibril formation.

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.

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