Calcified Tissue Research最新文献_第9页

A thermodynamic analysis of the secondary transition in the spontaneous precipitation of calcium phosphate. 磷酸钙自发沉淀过程中二次转变的热力学分析。

Calcified Tissue Research Pub Date : 1978-08-18 DOI: 10.1007/BF02010771

J L Meyer, E D Eanes

{"title":"A thermodynamic analysis of the secondary transition in the spontaneous precipitation of calcium phosphate.","authors":"J L Meyer, E D Eanes","doi":"10.1007/BF02010771","DOIUrl":"https://doi.org/10.1007/BF02010771","url":null,"abstract":"A thermodynamic analysis has been made of the secondary transition stage in the spontaneous precipitation of calcium phosphate following the amorphous-crystalline transformation. The first formed crystalline material has a solubility similar to that of octacalcium phosphate (OCP) and the computed thermodynamic solubility product remains invariant in the pH range 7.00--8.60. The duration of the secondary stage is sensitive to pH and the transition appears to occur by hydrolysis of the first formed OCP-like phase to a more basic apatitic phase with a tricalcium phosphate (TCP) stoichiometry. The crystalline material at the end of this transition has an invariant solubility product, in the pH range 7.00 to 8.60, when the TCP-like molecular formula is assumed. Changes in the solution chemistry which accompany the solid-to-solid transitions are consistent with the above conclusions. The results of this study are also consistent with those of a previous study which suggest that the stability of the amorphous calcium phosphate phase is dependent upon the instability of the solution phase with respect to OCP formation.","PeriodicalId":9389,"journal":{"name":"Calcified Tissue Research","volume":"25 3","pages":"209-16"},"PeriodicalIF":0.0,"publicationDate":"1978-08-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF02010771","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11252848","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 82

Selective stimulation of net calcium efflux from chick embryo tibiae by parathyroid hormone in vitro. 甲状旁腺激素选择性刺激鸡胚胫骨净钙外排的实验研究。

Calcified Tissue Research Pub Date : 1978-08-18 DOI: 10.1007/BF02010774

W K Ramp, R W McNeil

引用次数: 7

Oestrogen binding proteins in bone cell cytosol. 骨细胞质中的雌激素结合蛋白。

Calcified Tissue Research Pub Date : 1978-08-18 DOI: 10.1007/BF02010778

H C van Paassen, J Poortman, I H Borgart-Creutzburg, J H Thijssen, S A Duursma

引用次数: 4

Changes in the red cell, plasma and inulin spaces and in the total water contents of rat femurs in cortisone induced osteoporosis. 可的松所致骨质疏松大鼠股骨红细胞、血浆、胰岛素间隙及总含水量的变化。

Calcified Tissue Research Pub Date : 1978-08-18 DOI: 10.1007/BF02010777

J Lien, M Kaye

引用次数: 5

Effect of sex steroids on bone collagen synthesis in vitro. 性类固醇对体外骨胶原合成的影响。

Calcified Tissue Research Pub Date : 1978-05-26 DOI: 10.1007/BF02010758

E Canalis, L G Raisz

引用次数: 19

[The shell of the quail's egg: ultrastructural and crystallographic study (author's transl)]. [鹌鹑蛋壳:超微结构和晶体学研究[作者简介]]。

Calcified Tissue Research Pub Date : 1978-05-26 DOI: 10.1007/BF02010763

C Quintana, D Sandoz

{"title":"[The shell of the quail's egg: ultrastructural and crystallographic study (author's transl)].","authors":"C Quintana, D Sandoz","doi":"10.1007/BF02010763","DOIUrl":"https://doi.org/10.1007/BF02010763","url":null,"abstract":"The egg-shell of Japanese quail was studied by several techniques. Semithin sections (1 micron thick) of non-decalcified shell were observed by normal and polarized light microscopy. Thin sections of non-decalcified shell, examined by transmission electron microscopy, permitted us to observe the forms and dimensions of crystals of calcite within different layers of the shell: mammilary layer, layer of cones, palissade layer and surface crystal layer. There appears to be two distinct zones in the layer of cones as well as in the superficial crystal layer. Electron microdiffraction revealed the orientation of calcite crystals in the columns. Some crystal defects (twins?) were described and the possibility of their artefactual formation during ultramicrotomy is discussed. Localization of Ca, Mg, P and S were made by X-ray microanalysis of semithin sections. This technique shows that shell membranes, and chiefly the true cuticle, are also mineralized but, in these layers, minerals are not crystallized. Otherwise the distribution of Mg is not uniform throughout the shell thickness; it is less concentrated in the external zone of the layer of cones. These results together with observation of developing shells by scanning electron microscopy allowed us to propose a scheme for shell organization of the quail egg. This organization was related with decalcification which occurs during hatching.","PeriodicalId":9389,"journal":{"name":"Calcified Tissue Research","volume":"25 2","pages":"145-59"},"PeriodicalIF":0.0,"publicationDate":"1978-05-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF02010763","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11869619","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 9

Effect of dichloromethylene diphosphonate on morphology, enzyme activity, and ash content of bones of thyroparathyroidectomized rats. 二膦酸二氯亚甲基对去甲状旁腺大鼠骨形态、酶活性及灰分含量的影响。

Calcified Tissue Research Pub Date : 1978-05-26 DOI: 10.1007/BF02010760

S E Weisbrode, C C Capen, C B Pendley

{"title":"Effect of dichloromethylene diphosphonate on morphology, enzyme activity, and ash content of bones of thyroparathyroidectomized rats.","authors":"S E Weisbrode, C C Capen, C B Pendley","doi":"10.1007/BF02010760","DOIUrl":"https://doi.org/10.1007/BF02010760","url":null,"abstract":"Dichloromethylene diphosphonate (Cl2MDP) was given at doses of 4 mg/kg and 10 mg/kg daily for 7 days to adult thyroparathyroidectomized rats fed a low calcium diet. Primary metaphyseal trabeculae in Cl2MDP-treated rats were more numerous and longer than in controls. The light and electron microscopic appearance of osteoblasts, osteocytes and osteoclasts were unaltered by Cl2MDP. Bone alkaline phosphatase was significantly elevated in rats given Cl2MDP but adenosine triphosphatase activity was unchanged. Bone fat-free weight, fat-free minus ash weight, and bone calcium and phosphorus concentration were reduced significantly in rats given 10 mg/kg Cl2MDP compared to controls. Bone magnesium concentration was significantly elevated in rats given 10 mg/kg Cl2MDP. Serum calcium and phosphorus concentration were lower in Cl2MDP-treated rats. These results suggest that Cl2MDP is capable of altering bone remodeling, enzyme activity and mineral content, without significantly altering bone cell morphology, independent of the effects of parathyroid hormone, calcitonin, and dietary calcium.","PeriodicalId":9389,"journal":{"name":"Calcified Tissue Research","volume":"25 2","pages":"119-26"},"PeriodicalIF":0.0,"publicationDate":"1978-05-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF02010760","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11368850","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 1

X-ray diffraction and electron microscope study of osteons during calcification. 骨钙化过程的x射线衍射和电镜研究。

Calcified Tissue Research Pub Date : 1978-05-26 DOI: 10.1007/BF02010762

A Ascenzi, E Bonucci, A Ripamonti, N Roveri

{"title":"X-ray diffraction and electron microscope study of osteons during calcification.","authors":"A Ascenzi, E Bonucci, A Ripamonti, N Roveri","doi":"10.1007/BF02010762","DOIUrl":"https://doi.org/10.1007/BF02010762","url":null,"abstract":"To obtain information on the changes in the inorganic bone fraction during calcification, low- and wide-angle X-ray diffraction techniques and electron microscopy have been applied to single osteon samples. The samples were cylindrically shaped and their axes corresponded to the axes of the Haversian canals. The selection was made according to the degree of calcification and the orientation of collagen bundles and inorganic particles. Osteons at both the initial and final stages of calcification were chosen. Arrangements of fiber bundles and inorganic particles in successive lamellae characteristic of three types of osteon were selected, that is, longitudinally structured osteons, transversely structured osteons, and alternately structured osteons. The results indicate that in osteonic lamellar bone there are two types of inorganic particles: (1) granules arranged in linear or needle-shapred entities with maximum width 40-45 A, which are regularly distributed at the level of the main band of the collagen fibrils where their maximum length reaches the length of the main band itself; that is , about 400 A; and (2) very long crystallites, with a diameter of 40-45 A, which grow with their crystallographic c-axis parallel to the collagen fibrils and cover much more than a major collagen period.","PeriodicalId":9389,"journal":{"name":"Calcified Tissue Research","volume":"25 2","pages":"133-43"},"PeriodicalIF":0.0,"publicationDate":"1978-05-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF02010762","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11868856","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 28

A macromolecular inhibitor of in vitro calcification of tendon matrix. 一种肌腱基质体外钙化的大分子抑制剂。

Calcified Tissue Research Pub Date : 1978-05-26 DOI: 10.1007/BF02010764

C Quittner, C L Wadkins

{"title":"A macromolecular inhibitor of in vitro calcification of tendon matrix.","authors":"C Quittner, C L Wadkins","doi":"10.1007/BF02010764","DOIUrl":"https://doi.org/10.1007/BF02010764","url":null,"abstract":"Bovine and human tendon tissue do not induce calcification in vitro. However, extraction of those tissues with 3% Na2HPO4 converts them to calcifiable matrices. The supernatant fraction derived from the extraction contains a nondialyzable, perchloric acid soluble component that inhibits calcification of the extracted matrix. This inhibitory substance is characterized by a molecular weight in the range of 85,000-100,000. Exposure to pronase or hyaluronidase did not alter the inhibitory potency but did render the inhibitor dialyzable. Commercial sources of hyaluronic acid, chondrotitin-6-sulfate, chrondroitin-4-sulfate, dermatan sulfate, heparin and lysozyme did not inhibit calcification of the extracted matrix. Phosvitin, a phosphoglycoprotein is a potent inhibitor. Although phosvitin and the tendon extract also inhibit calcification of previously calcified matrix, they have no detectable effect on the rate of decalcification. We conclude that the mechanism of inhibition is characterized by a degree of specificity and that phosvitin and a macromolecular component of tendon tissue blocks conversion of an intermediate matrix-bound CaP complex to crystalline apatite. It seems reasonable that the tendon inhibitor could function in situ and possibly in vivo to control calcification of tendon tissue.","PeriodicalId":9389,"journal":{"name":"Calcified Tissue Research","volume":"25 2","pages":"161-8"},"PeriodicalIF":0.0,"publicationDate":"1978-05-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF02010764","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11869621","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 4

Phosphophoryns-major noncollagenous proteins of rat incisor dentin. 大鼠门牙本质的主要非胶原蛋白磷酸蛋白。

Calcified Tissue Research Pub Date : 1978-05-26 DOI: 10.1007/BF02010765

M T Dimuzio, A Veis

{"title":"Phosphophoryns-major noncollagenous proteins of rat incisor dentin.","authors":"M T Dimuzio, A Veis","doi":"10.1007/BF02010765","DOIUrl":"https://doi.org/10.1007/BF02010765","url":null,"abstract":"Freshly excised rat incisors were immediately cleaned and demineralized in 0.5 M ethylene diaminetetracetic acid at pH 7.5. The extracts were freed of calcium, diffusible phosphate and low molecular weight polypeptide components by dialysis in membranes with cut-off of 3500 molecular weight. The extract was resolved into at least 7 protein components by chromatography on DEAE-cellulose at pH 8.2. The composition of each protein component was determined. Two proteins, rich in serine, phosphorous and aspartic acid were unlike any proteins attributed to enamel, and hence were considered to be components of incisor dentin. These were the principal non-collagenous components of the teeth. Further purification was carried out under dissociative conditions on Sepharose CL-6B gel filtration columns in 3.0 M guanidine hydrochloride. The two phosphoproteins have mol wts, by this method, of 71,000 and 65,000, respectively, and differ in content of apolar amino acids, although both contain greater than 70 residue % of seryl (or phosphoseryl) and aspartyl residues. The name \"phosphophoryns\" is proposed to describe these dentinal proteins. The insoluble collagenous matrix remaining after the original demineralizing extraction was degraded with cyanogen bromide. Several non-collagenous protein components were released as well as the typical collagen derived peptides. Two collagen phosphoprotein complex peptides were also isolated, demonstrating as in bovine dentin, the probable direct covalent interaction of a dentin phosphoprotein with hte collagen of the mineralized matrix.","PeriodicalId":9389,"journal":{"name":"Calcified Tissue Research","volume":"25 2","pages":"169-78"},"PeriodicalIF":0.0,"publicationDate":"1978-05-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF02010765","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11869624","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 68