Family 2 cystatins inhibit osteoclast-mediated bone resorption in calvarial bone explants.

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Fältnamn	Indikatorer	Metadata
000		05344naa a2200829 4500
001		oai:gup.ub.gu.se/106100
003		SwePub
008		240528s2004 \| \|\|\|\|\|\|\|\|\|\|\|000 \|\|eng\|
009		oai:DiVA.org:umu-18057
009		oai:lup.lub.lu.se:c20fcced-a2e1-4e83-b18c-737e25177189
024	7	a https://gup.ub.gu.se/publication/1061002 URI
024	7	a https://doi.org/10.1016/j.bone.2004.05.0152 DOI
024	7	a https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-180572 URI
024	7	a https://lup.lub.lu.se/record/2665722 URI
040		a (SwePub)gud (SwePub)umud (SwePub)lu
041		a eng
042		9 SwePub
072	7	a ref2 swepub-contenttype
072	7	a art2 swepub-publicationtype
100	1	a Brand, H S4 aut
245	1 0	a Family 2 cystatins inhibit osteoclast-mediated bone resorption in calvarial bone explants.
264	1	b Elsevier BV,c 2004
520		a Osteoclastic bone resorption depends on the activity of various proteolytic enzymes, in particular those belonging to the group of cysteine proteinases. Biochemical studies have shown that cystatins, naturally occurring inhibitors of these enzymes, inhibit bone matrix degradation. Since the mechanism by which cystatins exert this inhibitory effect is not completely resolved yet, we studied the effect of cystatins on bone resorption microscopically and by Ca-release measurements. Calvarial bone explants were cultured in the presence or absence of family 2 cystatins and processed for light and electron microscopic analysis, and the culture media were analyzed for calcium release. Both egg white cystatin and human cystatin C decreased calcium release into the medium significantly. Microscopic analyses of the bone explants demonstrated that in the presence of either inhibitor, a high percentage of osteoclasts was associated with demineralized non-degraded bone matrix. Following a 24-h incubation in the presence of cystatin C, 41% of the cells were adjacent to areas of demineralized non-degraded bone matrix, whereas in controls, this was only 6%. If bone explants were cultured with both PTH and cystatin C, 60% of the osteoclasts were associated with demineralized non-degraded bone matrix, compared to 27% for bones treated with PTH only (P < 0.01). Our study provides evidence that cystatins, the naturally occurring inhibitors of cysteine proteinases, reversibly inhibit bone matrix degradation in the resorption lacunae adjacent to osteoclasts. These findings suggest the involvement of cystatins in the modulation of osteoclastic bone degradation.
650	7	a MEDICIN OCH HÄLSOVETENSKAPx Klinisk medicinx Odontologi0 (SwePub)302162 hsv//swe
650	7	a MEDICAL AND HEALTH SCIENCESx Clinical Medicinex Dentistry0 (SwePub)302162 hsv//eng
650	7	a MEDICIN OCH HÄLSOVETENSKAPx Klinisk medicinx Endokrinologi och diabetes0 (SwePub)302052 hsv//swe
650	7	a MEDICAL AND HEALTH SCIENCESx Clinical Medicinex Endocrinology and Diabetes0 (SwePub)302052 hsv//eng
650	7	a MEDICIN OCH HÄLSOVETENSKAPx Medicinska och farmaceutiska grundvetenskaperx Fysiologi0 (SwePub)301062 hsv//swe
650	7	a MEDICAL AND HEALTH SCIENCESx Basic Medicinex Physiology0 (SwePub)301062 hsv//eng
650	7	a MEDICIN OCH HÄLSOVETENSKAPx Klinisk medicinx Ortopedi0 (SwePub)302112 hsv//swe
650	7	a MEDICAL AND HEALTH SCIENCESx Clinical Medicinex Orthopaedics0 (SwePub)302112 hsv//eng
653		a Animals
653		a Bone Resorption
653		a metabolism
653		a prevention & control
653		a Cattle
653		a Cells
653		a Cultured
653		a Chickens
653		a Cystatin C
653		a Cystatins
653		a pharmacology
653		a Dose-Response Relationship
653		a Drug
653		a Humans
653		a Mice
653		a Osteoclasts
653		a drug effects
653		a metabolism
653		a ultrastructure
653		a Skull
653		a drug effects
653		a physiology
653		a ultrastructure
653		a cysteine proteinases
653		a cystatins
653		a cathepsins
653		a bone
653		a calcium
653		a osteoclasts
700	1	a Lerner, Ulf Hu Umeå universitet,Gothenburg University,Göteborgs universitet,Institutionen för invärtesmedicin, Avdelningen för internmedicin,Institute of Internal Medicine, Dept of Medicine,Oral cellbiologi4 aut0 (Swepub:umu)ulle0001
700	1	a Grubb, Andersu Lund University,Lunds universitet,Avdelningen för klinisk kemi och farmakologi,Institutionen för laboratoriemedicin,Medicinska fakulteten,Division of Clinical Chemistry and Pharmacology,Department of Laboratory Medicine,Faculty of Medicine4 aut0 (Swepub:lu)kkem-agr
700	1	a Beertsen, W4 aut
700	1	a Nieuw Amerongen, A V4 aut
700	1	a Everts, V4 aut
710	2	a Göteborgs universitetb Institutionen för invärtesmedicin, Avdelningen för internmedicin4 org
773	0	t Boned : Elsevier BVg 35:3, s. 689-96q 35:3<689-96x 8756-3282x 1873-2763
856	4	u http://dx.doi.org/10.1016/j.bone.2004.05.015y FULLTEXT
856	4 8	u https://gup.ub.gu.se/publication/106100
856	4 8	u https://doi.org/10.1016/j.bone.2004.05.015
856	4 8	u https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-18057
856	4 8	u https://lup.lub.lu.se/record/266572

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By the author/editor: Brand, H S; Lerner, Ulf H; Grubb, Anders; Beertsen, W; Nieuw Amerongen, ...; Everts, V

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