Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2000-8-22
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
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
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0039-128X
pubmed:author
pubmed:issnType
Print
pubmed:volume
65
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
371-8
pubmed:dateRevised
2009-11-19
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
pubmed:year
2000
pubmed:articleTitle
Regulation of collagenolytic cysteine protease synthesis by estrogen in osteoclasts.
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
pubmed:publicationType
Journal Article