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17beta-estradiol induces the proliferation of the in vitro cultured human urothelium.

https://arctichealth.org/en/permalink/ahliterature89268
Source
Scand J Urol Nephrol. 2009;43(3):179-85
Publication Type
Article
Date
2009
Author
Koskela Sanna
Lehtonen Siri
Santala Markku
Venhola Mika
Parpala-Spårman Teija
Lehenkari Petri
Author Affiliation
Department of Anatomy and Cell Biology, University of Oulu, Oulu, Finland. sannako@paju.oulu.fi
Source
Scand J Urol Nephrol. 2009;43(3):179-85
Date
2009
Language
English
Publication Type
Article
Keywords
Adolescent
Adult
Aged
Blotting, Western
Cell Nucleus - metabolism
Cell Proliferation - drug effects
Cells, Cultured
Child
Child, Preschool
Cytoplasm - metabolism
Estradiol - pharmacology
Female
Humans
Immunohistochemistry
Keratin-7 - metabolism
Male
Middle Aged
Urothelium - cytology
Young Adult
Abstract
OBJECTIVE: The genitourinary tract is considered to be a target for the actions of sex steroid hormones. Decreased ovarian function and lack of estrogen after menopause are associated with lower genitourinary tract symptoms as well as bladder dysfunctions such as incontinence. Estrogen may also affect urothelial cells. The estrogen receptors (ERs) are found in the mucosa of the urinary tract. The purpose of this study was to culture human urothelial cells (HUCs) originating from urothelial tissue biopsies and to use them as a reproducible test platform to evaluate the effect of 17beta-estradiol (E2). MATERIAL AND METHODS: Urothelial tissue biopsies were obtained from 95 patients undergoing gynaecological open surgery for urinary incontinence, paediatric vesicoureteral reflux or transurethral resection of the prostate (TURP) for benign prostatic hyperplasia. HUCs originating from biopsies were cultured in vitro in the absence or in the presence of 0.1 nmol, 0.01 micromol and 1 micromol of E2. ER expression of the cultured HUCs was examined by Western analysis and immunofluorescence microscopy, which was also used for HUC characterization. The effect of E2 in the proliferation of the HUCs was determined by tetrazolium salt 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium bromide (MTT)-assay. RESULTS: HUCs were cultured successfully in four to six passages but there was variation between samples. The cultured cells showed expression of beta(4)-integrin, E-cadherin and cytokeratins 7, 8, 9 and 19, indicating the epithelial origin of the cells. Both types of ERs, ERalpha and ERbeta, were found in the in vitro cultured HUCs. E2 treatment of HUCs did not affect remarkably the expression of ERalpha but cell proliferation was induced. However, no concentration-dependent effect was seen. CONCLUSIONS: This study indicates that HUCs originating from small tissue biopsies can be cultured in several passages in vitro and could have potential in repairing or restoring urinary tract tissue by tissue engineering therapy. HUCs serve as a good in vitro test platform, as shown by analysing E2-treated HUCs. E2 induced the proliferation of cultured HUCs even though concentration dependency was not observed. The findings of this study may have relevance in determining the mechanisms of estrogen therapy in postmenopausal urinary tract symptoms and in the future development of tissue engineering technology.
PubMed ID
19384677 View in PubMed
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The 68K protease has beta-secretase-like activity for lymphocyte precursor protein but not for brain substrate.

https://arctichealth.org/en/permalink/ahliterature199515
Source
Neuroreport. 2000 Feb 7;11(2):373-7
Publication Type
Article
Date
Feb-7-2000
Author
A. Matsumoto
Author Affiliation
Department of Radiation Biophysics and Genetics, Kobe University School of Medicine, Japan.
Source
Neuroreport. 2000 Feb 7;11(2):373-7
Date
Feb-7-2000
Language
English
Publication Type
Article
Keywords
Aged
Aged, 80 and over
Alzheimer Disease - enzymology
Amino Acid Sequence
Amyloid Precursor Protein Secretases
Amyloid beta-Protein Precursor - metabolism
Aspartic Acid Endopeptidases - metabolism
Blotting, Western
Cells, Cultured
Cerebral Cortex - enzymology
Chondroitin ABC Lyase - metabolism
Endopeptidases
Female
Humans
Isoenzymes - metabolism
Lymphocytes - cytology - enzymology
Male
Middle Aged
Molecular Sequence Data
Organ Specificity
Peptide Fragments - chemistry
Polysaccharide-Lyases - metabolism
Protein Processing, Post-Translational
Sequence Analysis, Protein
Serine Endopeptidases - metabolism
Substrate Specificity
Abstract
Processing and metabolism of beta-amyloid precursor protein (APP) and generation of a variety of beta-amyloid (Abeta) peptides in the human brain is essentially associated with pathophysiology of Alzheimer's disease (AD). APP degradation activity of the 68 kDa serine protease, which was originally prepared from familial AD lymphoblastoid cells and harbors beta-secretase-like activity, was analyzed by Western blot using anti Abeta 1/40 antibody and anti APP cytoplasmic domain (CT) antibody. Native lymphocyte APP (LAPP) prepared from normal or AD-derived lymphoblastoid cells was degraded by the protease, generating a 16 kDa Abeta-bearing C-terminal fragment of APP. N-terminal amino acid sequencing of the fragment indicated that the protease cleaves LAPP at the Abeta-N-terminus. When the LAPP was treated with chondroitinase ABC prior to proteolysis, the activity to generate the fragment was inhibited, but pretreatment with heparitinase resulted in no effect. Native hippocampal APP prepared from normal brain, however, did not generate the 16 kDa peptide by the protease treatment. These results suggest that the process of APP degradation and Abeta-peptides generation, including beta-secretase activity, is associated with tissue specificity of both APP substrate and proteases. They also indicate that sulfated glycoconjugates attached to a portion of APP isoforms may play a role as a molecular determinant in the proteolysis.
PubMed ID
10674489 View in PubMed
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Absence of evidence of Borna disease virus infection in Swedish patients with Chronic Fatigue Syndrome.

https://arctichealth.org/en/permalink/ahliterature200265
Source
J Neurovirol. 1999 Oct;5(5):495-9
Publication Type
Article
Date
Oct-1999
Author
B. Evengård
T. Briese
G. Lindh
S. Lee
W I Lipkin
Author Affiliation
Department of Immunology, Microbiology, Pathology and Infectious Diseases, Clinic for Infectious Diseases, Karolinska Institutet at Huddinge University Hospital.
Source
J Neurovirol. 1999 Oct;5(5):495-9
Date
Oct-1999
Language
English
Publication Type
Article
Keywords
Adult
Aged
Blotting, Western
Borna Disease - virology
Borna disease virus - immunology - isolation & purification - pathogenicity
Enzyme-Linked Immunosorbent Assay
Fatigue Syndrome, Chronic - virology
Female
Humans
Leukocytes, Mononuclear - chemistry - metabolism - virology
Male
Middle Aged
Reverse Transcriptase Polymerase Chain Reaction
Sweden
Abstract
Chronic Fatigue Syndrome (CFS) is characterized by debilitating fatigue, somatic symptoms and cognitive impairment. An infectious basis has been proposed; candidate agents include enteroviruses, herpesviruses, retroviruses and Borna disease virus (BDV), a novel neurotropic virus associated with neuropsychiatric disorders. Sera and peripheral blood mononuclear cells (PBMC) from Swedish CFS patients were assayed for evidence of infection using ELISA and Western immunoblot for detection of antibodies to BDV proteins N, P and gp18; and using nested reverse transcriptase polymerase chain reaction (RT-PCR) for detection of BDV N- and P-gene transcripts. No specific immunoreactivity to BDV proteins was found in sera from 169 patients or 62 controls. No BDV N- or P-gene transcripts were found through RT-PCR analysis of PBMC from 18 patients with severe CFS. These results do not support a role for BDV in pathogenesis of CFS.
PubMed ID
10568886 View in PubMed
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Absence of human T-lymphotropic virus types I and II infection in an Ontario hemophilia population.

https://arctichealth.org/en/permalink/ahliterature223481
Source
Transfusion. 1992 Jul-Aug;32(6):513-6
Publication Type
Article
Author
G. Dekaban
M. Inwood
D. Waters
J. Drouin
J. Teitel
Author Affiliation
Immunology Group, John Roberts Research Institute, University of Western Ontario, London, Canada.
Source
Transfusion. 1992 Jul-Aug;32(6):513-6
Language
English
Publication Type
Article
Keywords
Adult
Blood Donors
Blotting, Western
DNA, Viral - analysis
HIV Seropositivity - blood
HTLV-I Infections - blood
HTLV-II Infections - blood
Hemophilia A - blood - microbiology
Humans
Ontario
Polymerase Chain Reaction
Retrospective Studies
Abstract
Two hundred ninety-three serum samples from Ontario hemophiliacs and 200 samples from human immunodeficiency virus-positive blood donors were screened for the presence of antibodies to human T-lymphotropic virus type I (HTLV-I) by enzyme-linked immunosorbent assay, radioimmunoassay, and Western blot techniques. None of the serum samples provided unequivocal positive results, but several samples gave inconclusive results. Of the hemophiliacs with inconclusive serologic results from whom peripheral blood lymphocyte DNA could be obtained, all were negative for HTLV-I and HTLV type II (HTLV-II) sequences as determined by polymerase chain reaction (PCR). PCR was also performed on a lymph node biopsy sample taken from a hemophiliac who developed a rare T-cell lymphoma; the sample was negative for HTLV-I and -II sequences. These results indicate that Ontario hemophiliacs have not been exposed to HTLV-I or HTLV-II.
PubMed ID
1502703 View in PubMed
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Abundance of the Na-K-2Cl cotransporter NKCC2 is increased by high-fat feeding in Fischer 344 X Brown Norway (F1) rats.

https://arctichealth.org/en/permalink/ahliterature90141
Source
Am J Physiol Renal Physiol. 2009 Apr;296(4):F762-70
Publication Type
Article
Date
Apr-2009
Author
Riazi Shahla
Tiwari Swasti
Sharma Nikhil
Rash Arjun
Ecelbarger C M
Author Affiliation
Associate Professor, Dept. of Medicine, Georgetown Univ., 4000 Reservoir Rd, NW, Washington, DC, 20007, USA.
Source
Am J Physiol Renal Physiol. 2009 Apr;296(4):F762-70
Date
Apr-2009
Language
English
Publication Type
Article
Keywords
Animals
Antioxidants - pharmacology
Biological Markers - urine
Blood pressure
Blotting, Western
Crosses, Genetic
Cyclic N-Oxides - pharmacology
Dietary Fats - administration & dosage - metabolism
Dinoprost - analogs & derivatives - urine
Enzyme Inhibitors - pharmacology
Furosemide - pharmacology
Glucose Intolerance - metabolism - physiopathology
Hypertension - metabolism - physiopathology
Insulin Resistance
Kidney Medulla - drug effects - metabolism
Male
NG-Nitroarginine Methyl Ester - pharmacology
Natriuresis
Nitric Oxide - urine
Nitric Oxide Synthase - antagonists & inhibitors - metabolism
Oxidative Stress
Potassium Channels, Inwardly Rectifying - metabolism
Rats
Rats, Inbred BN
Rats, Inbred F344
Sodium Potassium Chloride Symporter Inhibitors - pharmacology
Sodium-Potassium-Chloride Symporters - antagonists & inhibitors - metabolism
Sodium-Potassium-Exchanging ATPase - metabolism
Spin Labels
Telemetry
Time Factors
Up-Regulation
Abstract
Insulin resistance is associated with hypertension by mechanisms likely involving the kidney. To determine how the major apical sodium transporter of the thick ascending limb, the bumetanide-sensitive Na-K-2Cl cotransporter (NKCC2) is regulated by high-fat feeding, we treated young male, Fischer 344 X Brown Norway (F344BN) rats for 8 wk with diets containing either normal (NF, 4%) or high (HF, 36%) fat, by weight, primarily as lard. HF-fed rats had impaired glucose tolerance, increased urine excretion of 8-isoprostane (a marker of oxidative stress), increased protein levels for NKCC2 (50-125%) and the renal outer medullary potassium channel (106%), as well as increased natriuretic response to furosemide (20-40%). To test the role of oxidative stress in this response, in study 2, rats were fed the NF or HF diet plus plain drinking water, or water containing N(G)-nitro-l-arginine methyl ester (l-NAME), a nitric oxide synthase inhibitor (100 mg/l), or tempol, a superoxide dismutase mimetic (1 mmol/l). The combination of tempol with HF nullified the increase in medullary NKCC2, while l-NAME with HF led to the highest expression of medullary NKCC2 (to 498% of NF mean). However, neither of these drugs dramatically affected the elevated natriuretic response to furosemide with HF. Finally, l-NAME led to a marked increase in blood pressure (measured by radiotelemetry), which was significantly enhanced with HF. Mean arterial blood pressure at 7 wk was as follows (mmHg): NF, 100 +/- 2; NF plus l-NAME, 122 +/- 3; and HF plus l-NAME, 131 +/- 2. Overall, HF feeding increased the abundance of NKCC2. Inappropriately high sodium reabsorption in the thick ascending limb via NKCC2 may contribute to hypertension with insulin resistance.
PubMed ID
19193725 View in PubMed
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Accelerated apoptosis and low bcl-2 expression associated with neuroendocrine differentiation predict shortened survival in operated large cell carcinoma of the lung.

https://arctichealth.org/en/permalink/ahliterature20816
Source
Pathol Oncol Res. 1999;5(3):179-86
Publication Type
Article
Date
1999
Author
A K Eerola
H. Ruokolainen
Y. Soini
H. Raunio
P. Pääkkö
Author Affiliation
University of Oulu, Department of Pathology Kajaanintie 52 D, Oulu, FIN-90401, Finland.
Source
Pathol Oncol Res. 1999;5(3):179-86
Date
1999
Language
English
Publication Type
Article
Keywords
Adult
Aged
Apoptosis
Blotting, Western
Carcinoma, Neuroendocrine - metabolism - mortality - pathology - surgery
Carcinoma, Non-Small-Cell Lung - metabolism - mortality - pathology - surgery
Cell Differentiation
Cyclin D1 - metabolism
Female
Follow-Up Studies
Humans
Immunohistochemistry
Lung Neoplasms - metabolism - mortality - pathology - surgery
Male
Membrane Proteins - metabolism
Middle Aged
Necrosis
Neoplasm Proteins - metabolism
Prognosis
Proto-Oncogene Proteins - metabolism
Proto-Oncogene Proteins c-bcl-2 - metabolism
Survival Rate
bcl-2 Homologous Antagonist-Killer Protein
bcl-2-Associated X Protein
Abstract
In order to test the hypothesis that increased apoptotic activity is connected with neuroendocrine differentiation and low differentiation degree in large cell carcinoma (LCLC) and is regulated by bcl-2 family proteins, we analysed the extent of apoptosis and tumor necrosis and their relation to the expression of bcl-2, bax, bak and mcl-1 in 35 LCLCs, of which 20 were classified as large cell neuroendocrine lung carcinomas (LCNEC) and 15 as large cell non-neuroendocrine lung carcinomas (LCNNEC). The extent of apoptosis was determined by detecting and counting the relative and absolute numbers of apoptotic cells and bodies using in situ 3 -end labelling of the apoptotic DNA. The extent and intensity of expression of the bcl-2, bax, bak and mcl-1 proteins were studied by immunohistochemistry. Also the relative volume density of necrosis was evaluated and correlated with the other parameters. Finally, all the parameters were evaluated as prognostic markers and correlated with data on the survival of the patients. Relatively high apoptotic indices were seen in both tumor types (average for both 2.53%, range 0.09 27.01%). Significantly higher bcl-2 and bak indices were detected more often in LCNECs than in LCNNECs. Immunohistochemically detected bax, bcl-2 and bak expression was independent of apoptotic index in both tumor types, while there was a statistically significant positive association between mcl-1 expression and apoptotic index in LCNNEC but not in LCNEC. There was a statistically significant association between high apoptotic index and shortened survival in LCLC. However, no association was found between tumor stage and apoptosis. The patients with LCNEC and low bcl-2 protein expression had a significantly shorter survival time than those with high bcl-2 indices. There was also a clear association between shortened survival and necrotic LCNNEC. LCLCs show relatively high apoptotic activity, which is associated with shortened survival. The expression of bcl-2, bak and mcl- 1 is associated with neuroendocrine differentiation in LCLC. Finally, our results support some previous reports suggesting that bcl-2 expression in combination with some other markers involved in apoptosis and/or proliferation may be of prognostic value in cases of lung carcinoma with neuroendocrine differentiation.
PubMed ID
10491014 View in PubMed
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AG 85, a major secretion protein of Mycobacterium tuberculosis, can be identified in ancient bone.

https://arctichealth.org/en/permalink/ahliterature271332
Source
Tuberculosis (Edinb). 2015 Jun;95 Suppl 1:S87-92
Publication Type
Article
Date
Jun-2015
Author
Tyede H Schmidt-Schultz
Michael Schultz
Source
Tuberculosis (Edinb). 2015 Jun;95 Suppl 1:S87-92
Date
Jun-2015
Language
English
Publication Type
Article
Keywords
Adult
Aged
Biomarkers - analysis
Blotting, Western
Case-Control Studies
Female
Germany
History, Ancient
History, Medieval
Humans
Indoles - analysis
Male
Microscopy - methods
Middle Aged
Mycobacterium tuberculosis
Paleopathology - methods
Siberia
Tuberculosis, Osteoarticular - diagnosis - history
Young Adult
Abstract
For the confirmation of Ag 85 in ancient and recent ECM of native macerated human bone, five cases were investigated. In three individuals, highly positive results for Ag 85 were identified in Western blot: 1) a male from Arzhan, South Siberia, dating from the 7th century BC, 2) a male from Kirchberg in Hesse, Germany, dating from the 10th - 12th century AD and 3) a recent female with a proven diagnosis of TB. As a negative control, a recent male is presented who did not suffer from TB. In another recent male, Ag 85 could be identified only very weakly. From cases in the literature it is well-known that highly positive results for Ag 85 indicate active TB, however, weakly positive results indicate a silent initial infection with Mtb. Thus, apparently, also in ancient individuals, it might well be possible to differentiate between diseased persons and disease carriers using paleoproteomic techniques.
PubMed ID
25890594 View in PubMed
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Age-associated changes in MAPK activation in fast- and slow-twitch skeletal muscle of the F344/NNiaHSD X Brown Norway/BiNia rat model.

https://arctichealth.org/en/permalink/ahliterature82974
Source
Exp Gerontol. 2006 Feb;41(2):205-14
Publication Type
Article
Date
Feb-2006
Author
Mylabathula D B
Rice K M
Wang Z.
Uddemarri S.
Kinnard R S
Blough E R
Author Affiliation
Department of Biological Sciences, Marshall University, Huntington, WV 25755-1090, USA.
Source
Exp Gerontol. 2006 Feb;41(2):205-14
Date
Feb-2006
Language
English
Publication Type
Article
Keywords
Aging - physiology
Animals
Blotting, Western
Electrophoresis, Polyacrylamide Gel
MAP Kinase Signaling System - physiology
Male
Mitogen-Activated Protein Kinase Kinases - metabolism
Models, Animal
Muscle Contraction
Muscle Fibers, Fast-Twitch - enzymology - physiology
Muscle Fibers, Slow-Twitch - enzymology - physiology
Phosphorylation
Rats
Rats, Inbred BN
Rats, Inbred F344
Abstract
We compared the tissue content, basal phosphorylation, and stretch-induced phosphorylation of the mitogen-activated protein kinase (MAPK) members; extracellular-signal-regulated kinases (ERK 1/2), p38, and c-Jun NH2-terminal kinase (JNK) in the fast-twitch extensor digitorium longus (EDL) and slow-twitch soleus of young adult (6 month), aged (30 month), and very aged (36 month) F344/NNiaHSD X Brown Norway/BiNia (F344/NXBN) rats. The expression and basal phosphorylation of the ERK 1/2, p38, and JNK MAPK proteins were regulated differently with aging in the EDL and soleus. Stretch induced significant phosphorylation of each signaling molecule in both muscle types of young adult and aged animals. In the very aged animals, stretch stimulated ERK 1/2 MAPK phosphorylation; however, EDL stretch failed to induce JNK MAPK phosphorylation, while soleus stretch was unable to induce the phosphorylation of p38 MAPK. The results suggest that skeletal muscle mechanotransduction processes are affected in very aged F344/NXBN rats and that aging alters load-induced signaling in fast- and slow-twitch muscle types differently.
PubMed ID
16378702 View in PubMed
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Age-dependent increase in oxidative stress in gastrocnemius muscle with unloading.

https://arctichealth.org/en/permalink/ahliterature91973
Source
J Appl Physiol. 2008 Dec;105(6):1695-705
Publication Type
Article
Date
Dec-2008
Author
Siu Parco M
Pistilli Emidio E
Alway Stephen E
Author Affiliation
Dept. of Health Technology and Informatics, The Hong Kong Polytechnic Univ., Hung Hom, Kowloon, Hong Kong, China. htpsiu@inet.polyu.edu.hk
Source
J Appl Physiol. 2008 Dec;105(6):1695-705
Date
Dec-2008
Language
English
Publication Type
Article
Keywords
Aging - physiology
Animals
Blotting, Western
Catalase - metabolism
Female
Hindlimb Suspension - physiology
Hydrogen Peroxide - metabolism
Male
Malondialdehyde - metabolism
Muscle, Skeletal - growth & development - metabolism - physiology
Organ Size - physiology
Oxidative Stress - physiology
Rats
Rats, Inbred BN
Rats, Inbred F344
Reverse Transcriptase Polymerase Chain Reaction
Superoxide Dismutase - metabolism
Tyrosine - analogs & derivatives - metabolism
Abstract
Oxidative stress increases during unloading in muscle from young adult rats. The present study examined the markers of oxidative stress and antioxidant enzyme gene and protein expressions in medial gastrocnemius muscles of aged and young adult (30 and 6 mo of age) Fischer 344 x Brown Norway rats after 14 days of hindlimb suspension. Medial gastrocnemius muscle weight was decreased by approximately 30% in young adult and aged rats following suspension. When muscle weight was normalized to animal body weight, it was reduced by 12% and 22% in young adult and aged rats, respectively, after suspension. Comparisons between young adult and aged control animals demonstrated a 25% and 51% decline in muscle mass when expressed as absolute muscle weight and muscle weight normalized to the animal body weight, respectively. H(2)O(2) content was elevated by 43% while Mn superoxide dismutase (MnSOD) protein content was reduced by 28% in suspended muscles compared with control muscles exclusively in the aged animals. Suspended muscles had greater content of malondialdehyde (MDA)/4-hydroxyalkenals (4-HAE) (29% and 58% increase in young adult and aged rats, respectively), nitrotyrosine (76% and 65% increase in young adult and aged rats, respectively), and catalase activity (69% and 43% increase in young adult and aged rats, respectively) relative to control muscles. Changes in oxidative stress markers MDA/4-HAE, H(2)O(2), and MnSOD protein contents in response to hindlimb unloading occurred in an age-dependent manner. These findings are consistent with the hypotheses that oxidative stress has a role in mediating disuse-induced and sarcopenia-associated muscle losses. Our data suggest that aging may predispose skeletal muscle to increased levels of oxidative stress both at rest and during unloading.
PubMed ID
18801960 View in PubMed
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Aggrecanase- and matrix metalloproteinase-mediated aggrecan degradation is associated with different molecular characteristics of aggrecan and separated in time ex vivo.

https://arctichealth.org/en/permalink/ahliterature98494
Source
Biomarkers. 2010 May;15(3):266-76
Publication Type
Article
Date
May-2010
Author
Suzi Hoegh Madsen
Eren Ufuk Sumer
Anne-Christine Bay-Jensen
Bodil-Cecilie Sondergaard
Per Qvist
Morten Asser Karsdal
Author Affiliation
Nordic Bioscience A/S, Herlev, Denmark.
Source
Biomarkers. 2010 May;15(3):266-76
Date
May-2010
Language
English
Publication Type
Article
Keywords
ADAM Proteins - metabolism
Aggrecans - metabolism
Animals
Biological Markers - blood
Blotting, Western - methods
Cartilage - metabolism
Cattle
Cytokines - metabolism
Endopeptidases - blood
Glycosaminoglycans - metabolism
Matrix Metalloproteinase 9 - metabolism
Matrix Metalloproteinases - blood
Models, Animal
Models, Biological
Osteoarthritis - blood - diagnosis
Procollagen N-Endopeptidase - metabolism
Abstract
Aggrecan is one of the first proteins to be depleted from articular cartilage in early osteoarthritis. We investigated the molecular differences between matrix metalloproteinase (MMP)- and aggrecanase-mediated aggrecan degradation, as a consequence of their distinct time-dependent degradation profiles. Cartilage degradation was induced by cytokine stimulation in bovine articular cartilage explants and quantified by a dye-binding assay and immunoassays. The size of degradation fragments was analysed by Western blot. Cytokine stimulation resulted in the early release of aggrecanase-mediated aggrecan degradation fragments. In contrast, MMP-mediated aggrecan degradation began only at day 16 and continued to day 21. Western blot analysis showed that glycosylated high-molecular-weight (374)ARGSVI fragments appeared at day 7, in contrast to deglycosylated low-molecular-weight (342)FFGVG fragments which were detected at day 21. Aggrecan degradation may be divided into two different pools, a high-molecular-weight aggrecanase-mediated pool, and a low-molecular-weight MMP-mediated pool. This may have implications for the development of intervention strategies for OA.
PubMed ID
20039789 View in PubMed
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234 records – page 1 of 24.