Generalized inhibition of cell-free translation by the amino-terminal propeptide of chick Type I procollagen

1985 ◽  
Vol 826 (2-3) ◽  
pp. 101-107 ◽  
Author(s):  
Richard Goldenberg ◽  
Richard E. Fine
Keyword(s):  
Type I ◽  
Amino Terminal ◽  
Type I Procollagen ◽  
Free Translation

scholarly journals Serum Sclerostin Levels Are Decreased in Adult Patients With Different Types of Osteogenesis Imperfecta

2014 ◽  
Vol 99 (2) ◽  
pp. E311-E319 ◽  
Author(s):  
Roland Kocijan ◽  
Christian Muschitz ◽  
Astrid Fahrleitner-Pammer ◽  
Karin Amrein ◽  
Peter Pietschmann ◽  
...  
Keyword(s):  
Body Composition ◽  
Mineral Content ◽  
Adult Patients ◽  
Type I ◽  
Healthy Controls ◽  
Amino Terminal ◽  
Type I Procollagen ◽  
Different Types ◽  
Turnover Markers

Context: There are no specific biochemical bone markers available for osteogenesis imperfecta (OI), and the role of sclerostin as a key regulator of bone formation in OI is unknown. Objectives: We aimed to evaluate the role of sclerostin and its association with bone turnover markers as well as body composition parameters in adult patients with different types of OI. Design, Setting, and Participants: This was a case-control study in 27 adult patients and 50 healthy age- and gender-matched controls. Main Outcome Measures: Serum sclerostin levels and bone turnover markers including serum osteocalcin, amino terminal propeptide of type I procollagen, and CrossLaps as well as body composition parameters were determined in mild OI stage I (OI-I) and moderate-severe OI stages III-IV (OI-III-IV), according to Sillence classification. Data were compared with healthy controls. Results: Sclerostin levels were significantly lower in OI-I (19.9 ± 10.9 pmol/L; P < .001) and OI-III-IV (13.3 ± 10.0 pmol/L; P < .001) compared with healthy adults (45.3 ± 14.9 pmol/L), even after adjustment for age, sex, bone mineral content, and body mass index. CrossLaps and PTH were significantly lower in OI-I (0.197 ± 0.15 ng/L; P = .007 and 33.7 ± 19.1 pg/L; P = .033, respectively) and OI-III-IV (0.221 ± 0.18 ng/L; P = .039, and 27.9 ± 14.7 pg/L; P = .001, respectively) than in healthy controls (0.322 ± 0.15 ng/L and 45.0 ± 16.6 pg/L). Amino-terminal propeptide of type I procollagen was below the reference range for OI-I and OI-III-IV. Patients with OI were shorter and lighter and had a decreased bone mineral content (P < .001) but similar fat distribution and lean body mass, compared with controls. Serum sclerostin levels were not related to any bone marker except osteocalcin, the number of prevalent fractures, or body composition readings. Conclusion: Decreased sclerostin levels in OI might reflect a down-regulation or negative feedback mechanism to prevent further bone loss.

scholarly journals Cortisol decreases the concentration of translatable type-I procollagen mRNA species in the developing chick-embryo calvaria

1981 ◽  
Vol 198 (3) ◽  
pp. 519-524 ◽  
Author(s):  
J Oikarinen ◽  
L Ryhänen
Keyword(s):  
Lower Amount ◽  
Translation System ◽  
Type I ◽  
Chick Embryos ◽  
Mrna Species ◽  
Procollagen Type ◽  
Type I Procollagen ◽  
Free Translation ◽  
Procollagen Type I ◽  
Reticulocyte Lysate

The calvarial mRNA species of chick embryos were translated in the rabbit reticulocyte-lysate cell-free translation system. The amount of procollagen type-I mRNA species was determined by digestion with bacterial collagenase and by fluorography of the cell-free translation products. Administration of cortisol resulted in a specific decrease in the cellular concentration of translatable procollagen type-I mRNA species in the calvaria of developing chick embryos. There was a lag period of up to 12 h before the response, which was dose-dependent. The data suggest that the decrease in amounts of procollagen mRNA species is the main reason for the lower amount of tissue collagen after topical or systemic administration of glucocorticoids, although other factors may contribute to the response.

Physical properties of the amino-terminal precursor-specific portion of type I procollagen

Biochemistry ◽  
1977 ◽  
Vol 16 (18) ◽  
pp. 4026-4033 ◽  
Author(s):  
Jurgen Engel ◽  
Peter Bruckner ◽  
Udo Becker ◽  
Rupert Timpl ◽  
Bea Rutschmann
Keyword(s):  
Physical Properties ◽  
Type I ◽  
Amino Terminal ◽  
Type I Procollagen

scholarly journals Diagnostic value of amino-terminal peptide of type I procollagen when retesting GH deficiency in the transition period

2015 ◽  
Author(s):  
Mariana Costache-Outas ◽  
Camelia Procopiuc ◽  
Andra Caragheorgheopol ◽  
Raluca Costache ◽  
Simona Fica
Keyword(s):  
Transition Period ◽  
Gh Deficiency ◽  
Diagnostic Value ◽  
Type I ◽  
Amino Terminal ◽  
Type I Procollagen

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.

scholarly journals Acute Decline in Serum Sclerostin in Response to PTH Infusion in Healthy Men

2011 ◽  
Vol 96 (11) ◽  
pp. E1848-E1851 ◽  
Author(s):  
Elaine W. Yu ◽  
Ruchit Kumbhani ◽  
Erica Siwila-Sackman ◽  
Benjamin Z. Leder
Keyword(s):  
Wnt Pathway ◽  
Healthy Adult ◽  
Serum Levels ◽  
Ionized Calcium ◽  
Type I ◽  
Amino Terminal ◽  
Adult Men ◽  
Type I Procollagen ◽  
Serum Ionized Calcium ◽  
Turnover Markers

Abstract Context: Animal models suggest that the osteoblast-stimulating actions of PTH are mediated by acute suppression of sclerostin, an inhibitor of the anabolic Wnt pathway. The immediate physiological changes in serum sclerostin in response to PTH infusion have not been reported in human studies. Objective: We sought to determine the acute physiological effects of PTH infusion on serum sclerostin and bone turnover markers in healthy adult men. Design, Setting, and Participants: Fifty-three healthy adult men underwent an 18-h iv infusion of human PTH(1-34) at a dose of 0.55 U/kg · h. Outcomes: Serum levels of ionized calcium, sclerostin, and markers of bone formation (osteocalcin and amino-terminal propeptide of type I procollagen) and bone resorption (C-telopeptide and N-telopeptide) were obtained at 0, 6, 12, and 18 h. Results: Serum ionized calcium, C-telopeptide, and N-telopeptide increased, and osteocalcin and amino-terminal propeptide of type I procollagen fell linearly throughout the PTH infusion (P < 0.001 for all). Average ± sem sclerostin levels declined from 936 ± 65 to 813 ± 63 pg/ml at 6 h (P < 0.001) and remained stably suppressed for the duration of the PTH infusion. There were no significant correlations between change in sclerostin and change in bone markers. Conclusions: Serum sclerostin declined in response to acute PTH infusion within 6 h in healthy adult men. The early plateau in sclerostin suppression may indicate that maximal stimulation of the Wnt pathway is achieved quickly after exposure to PTH. Our findings support the hypothesis that PTH may mediate its anabolic effects in part via suppression of sclerostin.

Synthetic peptide-based immunoassay for amino-terminal propeptide of type I procollagen: application for evaluation of bone formation

1993 ◽  
Vol 39 (11) ◽  
pp. 2254-2258 ◽  
Author(s):  
S G Linkhart ◽  
T A Linkhart ◽  
A K Taylor ◽  
J E Wergedal ◽  
P Bettica ◽  
...  
Keyword(s):  
Bone Formation ◽  
Synthetic Peptide ◽  
Type I ◽  
Normal Children ◽  
Amino Acid Peptide ◽  
Amino Terminal ◽  
Type I Procollagen ◽  
Serum Biochemical ◽  
Alkaline Phosphatase Isoenzyme ◽  
Normal Adults

Abstract Serum biochemical markers are powerful tools for the evaluation of bone turnover. In this study, we developed a radioimmunoassay, using a synthetic peptide for the N-terminal fragment of human type I [alpha 1(I)] procollagen (N-PCP). A 14-amino acid peptide was synthesized from the amino terminus and used to generate antibodies in rabbits. The synthetic peptide was used as standard and tracer in the assay. Both native type I amino procollagen (PINP), which was purified from skin fibroblasts, and human serum displaced tracer binding in parallel with the synthetic peptide. The range for measurement of N-PCP in serum was 0.7 to 30 micrograms/L (0.21-9.18 nmol/L). In a sample of 17 normal adults and 13 children (ages 9-16 years) there was a strong correlation between serum N-PCP determined by this assay and both skeletal alkaline phosphatase isoenzyme and osteocalcin, markers of bone formation. Serum concentrations of N-PCP in a group of normal children were eightfold higher than concentrations in normal adults, with no overlap between the two groups. N-PCP also correlated with C-terminal type I procollagen determined with a commercially available kit (r = 0.92).

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