scholarly journals Salivary Melatonin and the Severity of Attachment Loss: A Case-Control Study

2014 ◽  
Vol 2014 ◽  
pp. 1-4
Author(s):  
Leila Golpasand-Hagh ◽  
Faramarz Zakavi ◽  
Arash Daraeighadikolaei ◽  
Akram Ahangarpour ◽  
Sara Hajati ◽  
...  
Keyword(s):  
Chronic Periodontitis ◽  
Healthy Subjects ◽  
Type I Collagen ◽  
Periodontal Diseases ◽  
Protective Role ◽  
Enzyme Linked Immunosorbent Assay ◽  
Blood Levels ◽  
Melatonin Level ◽  
Type I ◽  
Salivary Melatonin

Background. Melatonin (MT: N-acetyl-5-methoxytryptamine) is a neuroendocrine hormone secreted mainly by the pineal gland in the brain. MT is produced with a circadian rhythm characterized by elevated blood levels during the night. In healthy individuals, maximal secretion of MT occurs between midnight and 2:00 am, whereas the minimal production occurs during the day. MT can be determined by repeated measurement of plasma or salivary MT or urine sulfatoxy-melatonin. Melatonin has powerful antioxidant effects, has an immunomodulatory role, stimulates the synthesis of type I collagen fibers, and promotes bone formation. Melatonin is also secreted in the saliva, although its role in the mouth is not known well. The purpose of this study was to examine the correlation between salivary melatonin level and periodontal diseases. Methods. Fifty subjects by mean age of 40.44±6.38 years were equally divided into 5 groups: 10 healthy subjects, 10 subjects with gingivitis, 10 subjects with localized moderate chronic periodontitis, 10 subjects with generalized moderate chronic periodontitis, and 10 subjects with generalized severe chronic periodontitis. Saliva samples were collected from all the subjects and melatonin levels were determined using an enzyme-linked immunosorbent assay. Two-way and one-way ANOVA and Tukey test were used to analyze relationships among variables. Results. Healthy subjects had significantly higher salivary melatonin level (5.29±0.50 pg/mL) compared to patients with gingivitis (4.35±0.30 pg/mL) (P<0.001). The difference between salivary melatonin level in patients with gingivitis and periodontitis was significant (P<0.001). Level of melatonin in patients with generalized severe chronic periodontitis (3.39±0.10 pg/mL) was significantly lower than that in other groups (P<0.01). Conclusions. This study determined that salivary melatonin level in patients with periodontal diseases is lower than that in healthy subjects. Consequently we conclude that there is a negative correlation between melatonin level and the severity of disease, suggesting that melatonin might have a protective role against periodontal diseases, although further research is required to validate this hypothesis.

scholarly journals Evaluation of salivary biomarkers for the diagnosis of periodontitis

2021 ◽  
Vol 21 (1) ◽  
Author(s):  
Yong Zhang ◽  
Ni Kang ◽  
Fei Xue ◽  
Jing Qiao ◽  
Jinyu Duan ◽  
...  
Keyword(s):  
Periodontal Disease ◽  
Healthy Subjects ◽  
Type I Collagen ◽  
Area Under The Curve ◽  
Diagnostic Value ◽  
Enzyme Linked Immunosorbent Assay ◽  
Type I ◽  
Cross Sectional ◽  
Diagnostic Potential ◽  
Auc Value

Abstract Background Salivary interleukin (IL)-1β, matrix metalloproteinase (MMP)-8, pyridinoline cross-linked carboxyterminal telopeptide of type I collagen (ICTP) and Porphyromonas gingivalis (Pg) are related to periodontitis. This study aimed to investigate the diagnostic potential of these biomarkers and to build a prediction panel for diagnosing periodontal disease. Methods A total of 80 participants were enrolled in a cross-sectional study and divided into healthy (n = 25), gingivitis (n = 24), and periodontitis (n = 31) groups based on their periodontal exam results. A full mouth periodontal examination was performed and unstimulated saliva was collected. Salivary IL-1β, MMP-8, ICTP, and Pg were assessed using enzyme-linked immunosorbent assay (ELISA) and quantitative real time PCR (qPCR). Their potentials for diagnosing periodontal disease were analyzed and combined prediction panels of periodontal disease were evaluated. Results As a single marker, IL-1β showed the best diagnostic value of the four markers evaluated and exhibited an area under the curve (AUC) value of 0.88 with 90% sensitivity and 76% specificity for discriminating periodontitis subjects from healthy subjects, an AUC value of 0.80 with 83% sensitivity and 76% specificity for discriminating gingivitis subjects from healthy subjects and an AUC value of 0.66 with 68% sensitivity and 64% specificity for differentiating periodontitis subjects from gingivitis subjects. The combination of IL-1β, ICTP, and Pg exhibited the highest efficacy for discriminating periodontitis subjects from healthy subjects (AUC = 0.94) and gingivitis subjects (AUC = 0.77). The combination of IL-1β and MMP-8 exhibited the best ability to discriminate gingivitis from healthy subjects (AUC = 0.84). Conclusions Salivary IL-1β, MMP-8, ICTP, and Pg showed significant effectiveness for diagnosing periodontal disease. The combination of IL-1β, ICTP, and Pg can be used to discriminate periodontitis subjects from healthy subjects and gingivitis subjects, and the combination of IL-1β and MMP-8 can be used to discriminate gingivitis subjects from healthy subjects.

scholarly journals Autophagy facilitates type I collagen synthesis in periodontal ligament cells

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Tomomi Nakamura ◽  
Motozo Yamashita ◽  
Kuniko Ikegami ◽  
Mio Suzuki ◽  
Manabu Yanagita ◽  
...  
Keyword(s):  
Periodontal Ligament ◽  
Collagen Synthesis ◽  
Type I Collagen ◽  
Periodontal Diseases ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Physiological Role ◽  
Type I ◽  
Periodontal Tissue ◽  
Pdl Cells

AbstractAutophagy is a lysosomal protein degradation system in which the cell self-digests its intracellular protein components and organelles. Defects in autophagy contribute to the pathogenesis of age-related chronic diseases, such as myocardial infarction and rheumatoid arthritis, through defects in the extracellular matrix (ECM). However, little is known about autophagy in periodontal diseases characterised by the breakdown of periodontal tissue. Tooth-supportive periodontal ligament (PDL) tissue contains PDL cells that produce various ECM proteins such as collagen to maintain homeostasis in periodontal tissue. In this study, we aimed to clarify the physiological role of autophagy in periodontal tissue. We found that autophagy regulated type I collagen synthesis by elimination of misfolded proteins in human PDL (HPDL) cells. Inhibition of autophagy by E-64d and pepstatin A (PSA) or siATG5 treatment suppressed collagen production in HPDL cells at mRNA and protein levels. Immunoelectron microscopy revealed collagen fragments in autolysosomes. Accumulation of misfolded collagen in HPDL cells was confirmed by sodium dodecyl sulfate–polyacrylamide gel electrophoresis. E-64d and PSA treatment suppressed and rapamycin treatment accelerated the hard tissue-forming ability of HPDL cells. Our findings suggest that autophagy is a crucial regulatory process that facilitates type I collagen synthesis and partly regulates osteoblastic differentiation of PDL cells.

(deleted)

2021 ◽  
Author(s):  
MV Osikov ◽  
EV Davydova ◽  
KS Abramov
Keyword(s):  
Bone Healing ◽  
Standard Therapy ◽  
Type I Collagen ◽  
Femoral Shaft ◽  
Control Group ◽  
Blood Levels ◽  
Type I ◽  
Mineral Density ◽  
Fracture Consolidation ◽  
To Receive

Efferent physical therapy holds promise as an adjunct to the combination treatment of femoral fractures in young, working-age individuals. The aim of the study was to investigate the dynamics of bone turnover markers at different stages of femoral fracture consolidation in patients undergoing ozone therapy. The study enrolled 20 men (group 2, 47.8 ± 3.5 years) with a femoral shaft fracture (AO/ASIF 32А, 32В). The control group (group 1, 46.8 ± 3.7 years) comprised 10 healthy males. Subgroup 2a (n = 10) was assigned to receive standard therapy; subgroup 2b (n = 10) was assigned to receive standard therapy complemented by minor autohemotherapy (MAHT) at 20 mg/L ozone concentrations. On days 7, 30 and 90, fracture consolidation was assessed on the RUST scale and blood levels of С-terminal telopeptides of type I collagen (bCTx, pg/ml) and procollagen type I carboxy-terminal propeptide (PICP, ng/ml) were measured. On day 7, the total RUST score in subgroups 2a and 2b was 4 points; on day 30, it was 6.5 and 8.7 points, respectively, and on day 90, it reached 10 and 11.5 points, respectively. Bone mineral density was as high as 90% in the MAHT subgroup vs. 78% in subgroup 2а, indicating faster bone healing. On day 30, bCTx levels in subgroup 2b were higher than in subgroup 2a (2289.4 [2145.3; 2365.4] vs. 1894.6 [1745.3; 2098.2], respectively. On day 7, PICP was significantly elevated in subgroup 2b in comparison with subgroup 2a; its levels peaked on days 30 and 90 (day 30: 268.3 [231.2; 286.3] vs. 183.2 [174.6; 195.6]; day 90: 584.6 [512.3; 589.3] vs. 351.2 [312.3; 369.4]. Thus, MAHT produces a positive effect on the quality and intensity of bone healing in men with isolated closed femoral shaft fractures.

scholarly journals A study of the interaction in vitro between type I collagen and a small dermatan sulphate proteoglycan

1988 ◽  
Vol 251 (3) ◽  
pp. 643-648 ◽  
Author(s):  
N Uldbjerg ◽  
C C Danielsen
Keyword(s):  
Steady State ◽  
Binding Sites ◽  
Type I Collagen ◽  
Enzyme Linked Immunosorbent Assay ◽  
Side Chains ◽  
Type I ◽  
Dermatan Sulphate ◽  
Collagen Fibrillogenesis ◽  
High Affinity ◽  
Sulphate Proteoglycan

The interaction between a small dermatan sulphate proteoglycan isolated from human uterine cervix and collagen type I from human and rat skin was investigated by collagen-fibrillogenesis experiments. Collagen fibrillogenesis was initiated by elevation of temperature and pH after addition of proteoglycan, chondroitinase-digested proteoglycan or isolated side chains, and monitored by turbidimetry. Collagen-associated and unbound proteoglycan was determined by enzyme-linked immunosorbent assay after aggregation was complete. (1) The binding of proteoglycan to collagen could be explained by the presence of two mutually non-interacting binding sites, with Ka1 = 1.3 x 10(8) M-1 and Ka2 = 1.3 x 10(6) M-1. The number of binding sites per tropocollagen molecule was n1 = 0.11 and n2 = 1.1. The 0.1 high-affinity binding site per tropocollagen molecule indicates that the strong interaction between proteoglycan and collagen results from a concerted action of tropocollagen molecules in fibrils. Digestion of the proteoglycan with chondroitinase ABC did not affect these binding characteristics. (2) Proteoglycan did not affect the rate of fibrillogenesis, but increased the steady-state A400 by up to 90%. This increase was directly proportional to the saturation of the high-affinity type of binding sites. Neither isolated core protein nor isolated side chains induced a similar high increase in steady-state A400. (3) Electron micrographs showed that the fibril diameter was affected only to a minor extent, if at all, by the proteoglycan, whereas bundles of laterally aligned fibrils were common in the presence of proteoglycan. (4) Results obtained with human and rat collagen were similar.

Evitar (l-Alanyl-l-Glutamine) Regulates Key Signaling Molecules in the Pathogenesis of Postoperative Tissue Fibrosis

2018 ◽  
Vol 26 (6) ◽  
pp. 724-733 ◽  
Author(s):  
Lynne M. Robertson ◽  
Nicole M. Fletcher ◽  
Michael P. Diamond ◽  
Ghassan M. Saed
Keyword(s):  
Cellular Response ◽  
Type I Collagen ◽  
Primary Cultures ◽  
Hypoxia Inducible Factor ◽  
Enzyme Linked Immunosorbent Assay ◽  
Type I ◽  
Dependent Manner ◽  
Tissue Fibrosis ◽  
Hypoxia Inducible Factor 1Α ◽  
Episodic Hypoxia

Aims:Hypoxia and the resulting oxidative stress play a major role in postoperative tissue fibrosis. The objective of this study was to determine the effect of l-alanyl-l-glutamine (Ala-Gln) on key markers of postoperative tissue fibrosis: hypoxia-inducible factor (HIF) 1α and type I collagen.Methods:Primary cultures of human normal peritoneal fibroblasts (NPF) established from normal peritoneal tissue were treated with increasing doses of Ala-Gln (0, 1, 2, or 10 mM) with hypoxia ([2% O2] 0-48 hours; continuous hypoxia) or after hypoxia (0.5, 1, 2, 4 hours) and restoration of normoxia (episodic hypoxia) with immediate treatment with Ala-Gln. Hypoxia-inducible factor 1α and type 1 collagen levels were determined by enzyme-linked immunosorbent assay. Data were analyzed with 1-way analysis of variance followed by Tukey tests with Bonferroni correction.Results:Hypoxia-inducible factor 1α and type I collagen levels increased in untreated controls by 3- to 4-fold in response to continuous and episodic hypoxia in human NPF. Under continuous hypoxia, HIF-1α and type I collagen levels were suppressed by Ala-Gln in a dose-dependent manner. l-alanyl-l-glutamine treatment after episodic hypoxia also suppressed HIF-1α and type I collagen levels for up to 24 hours for all doses and up to 48 hours at the highest dose, regardless of exposure time to hypoxia.Conclusions:l-alanyl-l-glutamine significantly suppressed hypoxia-induced levels of key tissue fibrosis (adhesion) phenotype markers under conditions of continuous as well as episodic hypoxia in vitro. This effect of glutamine on molecular events involved in the cellular response to insult or injury suggests potential therapeutic value for glutamine in the prevention of postoperative tissue fibrosis.

scholarly journals Binding of Brucella protein, Bp26, to select extracellular matrix molecules

2019 ◽  
Vol 20 (1) ◽  
Author(s):  
Yasmin ElTahir ◽  
Amna Al-Araimi ◽  
Remya R. Nair ◽  
Kaija J. Autio ◽  
Hongmin Tu ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Type I Collagen ◽  
Host Cells ◽  
Mouse Serum ◽  
Enzyme Linked Immunosorbent Assay ◽  
Target Cells ◽  
Type I ◽  
Dependent Manner ◽  
Biolayer Interferometry

Abstract Background Brucella is a facultative intracellular pathogen responsible for zoonotic disease brucellosis. Little is known about the molecular basis of Brucella adherence to host cells. In the present study, the possible role of Bp26 protein as an adhesin was explored. The ability of Brucella protein Bp26 to bind to extracellular matrix (ECM) proteins was determined by enzyme-linked immunosorbent assay (ELISA) and biolayer interferometry (BLI). Results ELISA experiments showed that Bp26 bound in a dose-dependent manner to both immobilized type I collagen and vitronectin. Bp26 bound weakly to soluble fibronectin but did not bind to immobilized fibronectin. No binding to laminin was detected. Biolayer interferometry showed high binding affinity of Bp26 to immobilized type I collagen and no binding to fibronectin or laminin. Mapping of Bp26 antigenic epitopes by biotinylated overlapping peptides spanning the entire sequence of Bp26 using anti Bp26 mouse serum led to the identification of five linear epitopes. Collagen and vitronectin bound to peptides from several regions of Bp26, with many of the binding sites for the ligands overlapping. The strongest binding for anti-Bp26 mouse serum, collagen and vitronectin was to the peptides at the C-terminus of Bp26. Fibronectin did not bind to any of the peptides, although it bound to the whole Bp26 protein. Conclusions Our results highlight the possible role of Bp26 protein in the adhesion process of Brucella to host cells through ECM components. This study revealed that Bp26 binds to both immobilized and soluble type I collagen and vitronectin. It also binds to soluble but not immobilized fibronectin. However, Bp26 does not bind to laminin. These are novel findings that offer insight into understanding the interplay between Brucella and host target cells, which may aid in future identification of a new target for diagnosis and/or vaccine development and prevention of brucellosis.

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 &lt; 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 Effect of Nonsurgical Periodontal Therapy on Crevicular Fluid and Serum Glutathione Peroxidase Levels

2012 ◽  
Vol 32 (1) ◽  
pp. 1-7 ◽  
Author(s):  
Swati Pradeep Patel ◽  
Nishanth S. Rao ◽  
A. R. Pradeep
Keyword(s):  
Oxidative Stress ◽  
Glutathione Peroxidase ◽  
Periodontal Disease ◽  
Chronic Periodontitis ◽  
Periodontal Diseases ◽  
Periodontal Therapy ◽  
Enzyme Linked Immunosorbent Assay ◽  
Pocket Depth ◽  
Nonsurgical Periodontal Therapy ◽  
Crevicular Fluid

Background: Plasma glutathione peroxidase (eGPx) is an important selenium containing antioxidant in human defense against oxidative stress. While crevicular fluid (GCF) eGPx levels and its association with periodontal disease is well documented, there is no data on correlation of GCF and serum eGPx levels in chronic periodontitis. Hence this study was undertaken to further probe into the role of oxidative stress in periodontal diseases and effect of nonsurgical periodontal therapy (NSPT) by correlating GCF and serum levels of eGPx.Materials and methods: Thirty subjects (16-Males and 14-Females; age: 30–38 years) participated in the study. The subjects were divided, based on gingival index, probing pocket depth and clinical attachment level into: Healthy (group-1,n=10), Gingivitis (group-2,n=10) and Periodontitis (group-3,n=10). Chronic periodontitis patients after NSPT constituted group 4. GCF and serum samples collected from each subject were quantified for eGPx levels using Enzyme linked Immunosorbent Assay.Results: The mean eGPx concentrations increased from health (14.01 ng/μl and 78.26 ng/ml) to gingivitis (22.86 ng/μl and 90.44 ng/ml) and then to periodontitis (29.89 ng/μl and 103.43 ng/ml), in GCF and serum respectively. After NSPT, there was statistically significant reduction in eGPx concentration in GCF and serum (19.41 ng/μl and 85.21 ng/ml). Further, all the GCF eGPx values showed a positive correlation to that of serum eGPx level.Conclusion: Thus, increased eGPx concentration in GCF can be considered as an indicator of local increase in oxidative stress. While, increase in serum eGPx levels indicates that periodontal disease can also lead to increased oxidative stress at the systemic level.

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.

scholarly journals Gingival Crevicular Fluid Calprotectin, Osteocalcin and Cross-Linked N-Terminal Telopeptid Levels in Health and Different Periodontal Diseases

2011 ◽  
Vol 31 (6) ◽  
pp. 343-352 ◽  
Author(s):  
Sema Becerik ◽  
Beral Afacan ◽  
Veli Özgen Öztürk ◽  
Harika Atmaca ◽  
Gülnur Emingil
Keyword(s):  
Healthy Subjects ◽  
Gingival Crevicular Fluid ◽  
Periodontal Diseases ◽  
Inflammatory Marker ◽  
Aggressive Periodontitis ◽  
Enzyme Linked Immunosorbent Assay ◽  
Probing Depth ◽  
Crevicular Fluid ◽  
First Time

Aim:The aim of the present study was to investigate gingival crevicular fluid (GCF) calprotectin, osteocalcin and cross-linked N-terminal telopeptide (NTx) levels in health along with different periodontal diseases.Material and methods:Twenty chronic periodontitis (CP), 20 generalized aggressive periodontitis (G-AgP), 20 gingivitis and 20 healthy subjects were included. Probing depth, clinical attachment level, plaque index and papillary bleeding index was recorded. GCF calprotectin, osteocalcin and NTx levels were analyzed by enzyme-linked immunosorbent assay (ELISA).Results:CP, G-AgP and gingivitis groups had higher GCF calprotectin total amount compared to healthy subjects (p< 0.008). CP and G-AgP groups had similar, but higher levels compared to gingivitis groups (p< 0.008). CP and G-AgP groups had lower GCF osteocalcin total amount compared to gingivitis and healthy groups (p< 0.008). CP group had higher GCF NTx but lower osteocalcin total amount and osteocalcin/NTx ratio than the G-AgP group (p< 0.008)Conclusions:Our results suggest that elevated GCF calprotectin levels play a role as a reliable inflammatory marker in the pathogenesis of periodontal disease. Fluctuating GCF levels of osteocalcin and NTx might point out to the abnormal bone turnover in periodontitis. Our data document for the first time the role of NTx in the pathogenesis of different periodontal diseases.

Sign in / Sign up

Export Citation Format

Share Document