Ultrastructural localization of calcium-activated adenosine triphosphatase (Ca2+-ATPase) in growth-plate cartilage
The electron-microscopic cytochemical localization of calcium-activated adenosine triphosphatase (Ca2+-ATPase) was determined in chick epiphyseal growth-plate cartilage. In the reserve zone, mitochondria and lysosomes contained substantial amounts of reaction product, while the plasma membrane and t...
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| Veröffentlicht in: | The journal of histochemistry and cytochemistry 1985-09, Vol.33 (9), p.925-932 |
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| container_title | The journal of histochemistry and cytochemistry |
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| creator | Akisaka, T Gay, CV |
| description | The electron-microscopic cytochemical localization of calcium-activated adenosine triphosphatase (Ca2+-ATPase) was determined in chick epiphyseal growth-plate cartilage. In the reserve zone, mitochondria and lysosomes contained substantial amounts of reaction product, while the plasma membrane and the Golgi complex showed very weak enzymatic activity, and matrix vesicle membranes did not exhibit the cytochemical reaction. As maturation proceeded, the plasma membrane, Golgi complex, and matrix vesicle membranes also stained and were most intense in the proliferative and early hypertrophic zones. From the hypertrophic to the calcifying zone, cytochemical staining decreased progressively in the plasma membrane, the Golgi complex, and lysosomes, while in some cases mitochondrial reaction product remained intense. Matrix vesicles lost their enzymatic activity at the same time that matrix vesicle calcification commenced. It is proposed that this event allows matrix vesicles to calcify, since efflux of calcium would no longer occur. |
| doi_str_mv | 10.1177/33.9.3160764 |
| format | Article |
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In the reserve zone, mitochondria and lysosomes contained substantial amounts of reaction product, while the plasma membrane and the Golgi complex showed very weak enzymatic activity, and matrix vesicle membranes did not exhibit the cytochemical reaction. As maturation proceeded, the plasma membrane, Golgi complex, and matrix vesicle membranes also stained and were most intense in the proliferative and early hypertrophic zones. From the hypertrophic to the calcifying zone, cytochemical staining decreased progressively in the plasma membrane, the Golgi complex, and lysosomes, while in some cases mitochondrial reaction product remained intense. Matrix vesicles lost their enzymatic activity at the same time that matrix vesicle calcification commenced. 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In the reserve zone, mitochondria and lysosomes contained substantial amounts of reaction product, while the plasma membrane and the Golgi complex showed very weak enzymatic activity, and matrix vesicle membranes did not exhibit the cytochemical reaction. As maturation proceeded, the plasma membrane, Golgi complex, and matrix vesicle membranes also stained and were most intense in the proliferative and early hypertrophic zones. From the hypertrophic to the calcifying zone, cytochemical staining decreased progressively in the plasma membrane, the Golgi complex, and lysosomes, while in some cases mitochondrial reaction product remained intense. Matrix vesicles lost their enzymatic activity at the same time that matrix vesicle calcification commenced. It is proposed that this event allows matrix vesicles to calcify, since efflux of calcium would no longer occur.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Calcification, Physiologic</subject><subject>Calcium Chloride - metabolism</subject><subject>Calcium-Transporting ATPases - analysis</subject><subject>Cartilage - enzymology</subject><subject>Cartilage - ultrastructure</subject><subject>Chickens</subject><subject>Epiphyses - enzymology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Magnesium - metabolism</subject><subject>Magnesium Chloride</subject><subject>Microscopy, Electron</subject><subject>Skeleton and joints</subject><subject>Space life sciences</subject><subject>Vanadates</subject><subject>Vanadium - pharmacology</subject><subject>Vertebrates: osteoarticular system, musculoskeletal system</subject><issn>0022-1554</issn><issn>1551-5044</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kE1v1DAQhi1EVbaFG1ekHABRlSz-tnOsVkArVYJDe7a8jrNx5cTBdojg19ewUTlxssbzzDujB4DXCG4REuITIdtmSxCHgtNnYIMYQzWDlD4HGwgxrssHfQHOUnqAEFHK5Ck4XfENiPc-R51ynE2eo_aVD0Z791tnF8YqdFWpjJuHWpvsfups20q3dgzJjbbK0U19SFOvs062-rDT-LK-uvteiovKjdUhhiX39eTLXAmK2Xl9sC_BSad9sq_W9xzcf_l8t7uub799vdld3daGIpFr0jDGJG47ihpDpRZ4zznlHbRCyr3kRErccdZKaRrBDebESCqQaLFGBktGzsH7Y-4Uw4_ZpqwGl4z1Xo82zEkJjjHnQhTw4xE0MaQUbaem6AYdfykE1R_FihDVqNVZwd-sufN-sO0T_K__du3rVOx1UY_GpSesXNZAgQt2ccRScaIewhzHYuN_K98d2d4d-sVFq9KgvS8HILUsy1-2wYw8AheEnGs</recordid><startdate>198509</startdate><enddate>198509</enddate><creator>Akisaka, T</creator><creator>Gay, CV</creator><general>Histochemical Soc</general><general>SAGE Publications</general><general>Histochemical Society</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>198509</creationdate><title>Ultrastructural localization of calcium-activated adenosine triphosphatase (Ca2+-ATPase) in growth-plate cartilage</title><author>Akisaka, T ; Gay, CV</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c417t-3955582df419c48a72b6646f0e788b863882f65d88c976c263c84717d2a1c2853</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>Adenosine Triphosphate - metabolism</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Calcification, Physiologic</topic><topic>Calcium Chloride - metabolism</topic><topic>Calcium-Transporting ATPases - analysis</topic><topic>Cartilage - enzymology</topic><topic>Cartilage - ultrastructure</topic><topic>Chickens</topic><topic>Epiphyses - enzymology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Magnesium - metabolism</topic><topic>Magnesium Chloride</topic><topic>Microscopy, Electron</topic><topic>Skeleton and joints</topic><topic>Space life sciences</topic><topic>Vanadates</topic><topic>Vanadium - pharmacology</topic><topic>Vertebrates: osteoarticular system, musculoskeletal system</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Akisaka, T</creatorcontrib><creatorcontrib>Gay, CV</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The journal of histochemistry and cytochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Akisaka, T</au><au>Gay, CV</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ultrastructural localization of calcium-activated adenosine triphosphatase (Ca2+-ATPase) in growth-plate cartilage</atitle><jtitle>The journal of histochemistry and cytochemistry</jtitle><addtitle>J Histochem Cytochem</addtitle><date>1985-09</date><risdate>1985</risdate><volume>33</volume><issue>9</issue><spage>925</spage><epage>932</epage><pages>925-932</pages><issn>0022-1554</issn><eissn>1551-5044</eissn><coden>JHCYAS</coden><abstract>The electron-microscopic cytochemical localization of calcium-activated adenosine triphosphatase (Ca2+-ATPase) was determined in chick epiphyseal growth-plate cartilage. In the reserve zone, mitochondria and lysosomes contained substantial amounts of reaction product, while the plasma membrane and the Golgi complex showed very weak enzymatic activity, and matrix vesicle membranes did not exhibit the cytochemical reaction. As maturation proceeded, the plasma membrane, Golgi complex, and matrix vesicle membranes also stained and were most intense in the proliferative and early hypertrophic zones. From the hypertrophic to the calcifying zone, cytochemical staining decreased progressively in the plasma membrane, the Golgi complex, and lysosomes, while in some cases mitochondrial reaction product remained intense. Matrix vesicles lost their enzymatic activity at the same time that matrix vesicle calcification commenced. It is proposed that this event allows matrix vesicles to calcify, since efflux of calcium would no longer occur.</abstract><cop>Los Angeles, CA</cop><pub>Histochemical Soc</pub><pmid>3160764</pmid><doi>10.1177/33.9.3160764</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The journal of histochemistry and cytochemistry, 1985-09, Vol.33 (9), p.925-932 |
| issn | 0022-1554 1551-5044 |
| language | eng |
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| source | MEDLINE; SAGE Complete A-Z List; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | Adenosine Triphosphate - metabolism Animals Biological and medical sciences Calcification, Physiologic Calcium Chloride - metabolism Calcium-Transporting ATPases - analysis Cartilage - enzymology Cartilage - ultrastructure Chickens Epiphyses - enzymology Fundamental and applied biological sciences. Psychology Magnesium - metabolism Magnesium Chloride Microscopy, Electron Skeleton and joints Space life sciences Vanadates Vanadium - pharmacology Vertebrates: osteoarticular system, musculoskeletal system |
| title | Ultrastructural localization of calcium-activated adenosine triphosphatase (Ca2+-ATPase) in growth-plate cartilage |
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