Source:http://linkedlifedata.com/resource/pubmed/id/10899536
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
2000-8-22
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pubmed:abstractText |
In ovariectomized (Ovx) mice, collagenolytic cysteine protease (CCP) activity in calvaria significantly increased 7 days after ovariectomy and was about 50% of that observed in sham-operated (Sham) mice 3 weeks later. In Ovx mice, subcutaneously (s.c.) administered estradiol-17beta (E2) (10 microg/kg) for 2 weeks led to a decrease in CCP activity in calvaria to the level observed in Sham mice. In Ovx mice, though the amount of cathepsin L increased more than that of cathepsin K, cathepsin K and cathepsin L content increased by 200-400% compared with the Sham mice; cathepsin K was detected in larger amounts than cathepsin L in calvaria from both Sham and Ovx mice. The amounts of cathepsin K and cathepsin L in Ovx mice were reduced to the values seen with Sham mice after administration (s.c.) of E2 (10 microg/kg) for 2 weeks. In mouse calvarial organ culture, the increase of CCP activity and release of hydroxyproline, an indicator of degradation of type-I collagen, in the presence of 1alpha,25-(OH)(2)D(3), parathyroid hormone, interleukin (IL)-1alpha, IL-6, or tumor necrosis factor-alpha was suppressed by E2 (10(-9)-10(-7) M). In all cases, secretion of both cathepsin K and cathepsin L were suppressed by E2. In osteoclasts, expression of cathepsin K and cathepsin L was suppressed by E2 at the mRNA level. Cathepsin B was detected faintly or not at all. These results suggest that synthesis of cathepsin K and cathepsin L was negatively regulated by E2 at the mRNA level. In Ovx mice, deficiency of E2 resulted in an augmentation of cathepsin K and cathepsin L synthesis, and the cathepsins might share roles in bone resorption in vivo.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin B,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin K,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin L,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsins,
http://linkedlifedata.com/resource/pubmed/chemical/Ctsk protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Ctsl protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Estradiol,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxyproline,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0039-128X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
65
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
371-8
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10899536-Animals,
pubmed-meshheading:10899536-Blotting, Western,
pubmed-meshheading:10899536-Bone and Bones,
pubmed-meshheading:10899536-Cathepsin B,
pubmed-meshheading:10899536-Cathepsin K,
pubmed-meshheading:10899536-Cathepsin L,
pubmed-meshheading:10899536-Cathepsins,
pubmed-meshheading:10899536-Cells, Cultured,
pubmed-meshheading:10899536-Cysteine Endopeptidases,
pubmed-meshheading:10899536-DNA Primers,
pubmed-meshheading:10899536-Endopeptidases,
pubmed-meshheading:10899536-Estradiol,
pubmed-meshheading:10899536-Female,
pubmed-meshheading:10899536-Hydroxyproline,
pubmed-meshheading:10899536-Male,
pubmed-meshheading:10899536-Mice,
pubmed-meshheading:10899536-Mice, Inbred ICR,
pubmed-meshheading:10899536-Organ Culture Techniques,
pubmed-meshheading:10899536-Osteoclasts,
pubmed-meshheading:10899536-Ovariectomy,
pubmed-meshheading:10899536-Ovary,
pubmed-meshheading:10899536-RNA, Messenger
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pubmed:year |
2000
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pubmed:articleTitle |
Regulation of collagenolytic cysteine protease synthesis by estrogen in osteoclasts.
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pubmed:affiliation |
Discovery Research Laboratory, Takeda Chemical Industries, Ltd., 17-85, Juso-honmachi 2-chome, Yodogawa-ku, 532-8686, Osaka, Japan. FURUYAMA_NAOKI@takeda.co.jp
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pubmed:publicationType |
Journal Article
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