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Localization of adenosine deaminase and adenosine deaminase complexing protein in rabbit brain
Adenosine deaminase and adenosine deaminase complexing protein have been localized in rabbit brain. Brains fixed in paraformaldehyde or in Clarke's solution were blocked coronally. Blocks from brains fixed in paraformaldehyde were either frozen in liquid nitrogen or embedded in paraffin. Tissue...
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Published in: | The journal of histochemistry and cytochemistry 1987-04, Vol.35 (4), p.443-451 |
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description | Adenosine deaminase and adenosine deaminase complexing protein have been localized in rabbit brain. Brains fixed in paraformaldehyde or in Clarke's solution were blocked coronally. Blocks from brains fixed in paraformaldehyde were either frozen in liquid nitrogen or embedded in paraffin. Tissue fixed in Clarke's solution was embedded in paraffin. Sections from each block were stained by the peroxidase-antiperoxidase method for adenosine deaminase or complexing protein using affinity-purified goat antibodies. Adenosine deaminase and complexing protein did not co-localize. Adenosine deaminase was detected in oligodendroglia and in endothelial cells lining blood vessels, whereas complexing protein was concentrated in neurons. The subcellular location and appearance of the peroxidase reaction product associated with individual cells was also quite distinctive. The cell bodies of adenosine deaminase-positive oligodendroglia were filled with intense deposits of peroxidase reaction product. In contrast to oligodendroglia, the reaction product associated with most neurons stained for complexing protein was concentrated in granular-appearing cytoplasmic deposits. In some instances, these deposits were clustered about the nuclear membrane. Staining of neurons in the granular layer of cerebellum was an exception. Granule cells were lightly outlined by peroxidase reaction product. Cerebellar islands, also referred to as glomeruli, were stained an intense uniform brown. These results raise the possibility that oligodendroglia and blood vessel endothelia, through the action of adenosine deaminase, might play a role in controlling the concentration of extracellular adenosine in brain. They do not, however, support the suggestion that complexing protein aids in adenosine metabolism by positioning adenosine deaminase on the plasma membrane. |
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Brains fixed in paraformaldehyde or in Clarke's solution were blocked coronally. Blocks from brains fixed in paraformaldehyde were either frozen in liquid nitrogen or embedded in paraffin. Tissue fixed in Clarke's solution was embedded in paraffin. Sections from each block were stained by the peroxidase-antiperoxidase method for adenosine deaminase or complexing protein using affinity-purified goat antibodies. Adenosine deaminase and complexing protein did not co-localize. Adenosine deaminase was detected in oligodendroglia and in endothelial cells lining blood vessels, whereas complexing protein was concentrated in neurons. The subcellular location and appearance of the peroxidase reaction product associated with individual cells was also quite distinctive. The cell bodies of adenosine deaminase-positive oligodendroglia were filled with intense deposits of peroxidase reaction product. In contrast to oligodendroglia, the reaction product associated with most neurons stained for complexing protein was concentrated in granular-appearing cytoplasmic deposits. In some instances, these deposits were clustered about the nuclear membrane. Staining of neurons in the granular layer of cerebellum was an exception. Granule cells were lightly outlined by peroxidase reaction product. Cerebellar islands, also referred to as glomeruli, were stained an intense uniform brown. These results raise the possibility that oligodendroglia and blood vessel endothelia, through the action of adenosine deaminase, might play a role in controlling the concentration of extracellular adenosine in brain. They do not, however, support the suggestion that complexing protein aids in adenosine metabolism by positioning adenosine deaminase on the plasma membrane.</description><identifier>ISSN: 0022-1554</identifier><identifier>EISSN: 1551-5044</identifier><identifier>DOI: 10.1177/35.4.3546489</identifier><identifier>PMID: 3546489</identifier><identifier>CODEN: JHCYAS</identifier><language>eng</language><publisher>Los Angeles, CA: Histochemical Soc</publisher><subject>Adenosine Deaminase - analysis ; Animals ; Biological and medical sciences ; Brain - enzymology ; Central nervous system ; Central neurotransmission. Neuromudulation. Pathways and receptors ; Fundamental and applied biological sciences. Psychology ; Glycoproteins - analysis ; Histocytochemistry ; Immunoenzyme Techniques ; Isoenzymes - analysis ; Nucleoside Deaminases - analysis ; Rabbits ; Vertebrates: nervous system and sense organs</subject><ispartof>The journal of histochemistry and cytochemistry, 1987-04, Vol.35 (4), p.443-451</ispartof><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c415t-56da3eae5909860066736a78fc53720c6924ea7e99240c69776fcfa27d0818e33</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7402951$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3546489$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schrader, WP</creatorcontrib><creatorcontrib>West, CA</creatorcontrib><creatorcontrib>Strominger, NL</creatorcontrib><title>Localization of adenosine deaminase and adenosine deaminase complexing protein in rabbit brain</title><title>The journal of histochemistry and cytochemistry</title><addtitle>J Histochem Cytochem</addtitle><description>Adenosine deaminase and adenosine deaminase complexing protein have been localized in rabbit brain. Brains fixed in paraformaldehyde or in Clarke's solution were blocked coronally. Blocks from brains fixed in paraformaldehyde were either frozen in liquid nitrogen or embedded in paraffin. Tissue fixed in Clarke's solution was embedded in paraffin. Sections from each block were stained by the peroxidase-antiperoxidase method for adenosine deaminase or complexing protein using affinity-purified goat antibodies. Adenosine deaminase and complexing protein did not co-localize. Adenosine deaminase was detected in oligodendroglia and in endothelial cells lining blood vessels, whereas complexing protein was concentrated in neurons. The subcellular location and appearance of the peroxidase reaction product associated with individual cells was also quite distinctive. The cell bodies of adenosine deaminase-positive oligodendroglia were filled with intense deposits of peroxidase reaction product. In contrast to oligodendroglia, the reaction product associated with most neurons stained for complexing protein was concentrated in granular-appearing cytoplasmic deposits. In some instances, these deposits were clustered about the nuclear membrane. Staining of neurons in the granular layer of cerebellum was an exception. Granule cells were lightly outlined by peroxidase reaction product. Cerebellar islands, also referred to as glomeruli, were stained an intense uniform brown. These results raise the possibility that oligodendroglia and blood vessel endothelia, through the action of adenosine deaminase, might play a role in controlling the concentration of extracellular adenosine in brain. They do not, however, support the suggestion that complexing protein aids in adenosine metabolism by positioning adenosine deaminase on the plasma membrane.</description><subject>Adenosine Deaminase - analysis</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Brain - enzymology</subject><subject>Central nervous system</subject><subject>Central neurotransmission. Neuromudulation. Pathways and receptors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycoproteins - analysis</subject><subject>Histocytochemistry</subject><subject>Immunoenzyme Techniques</subject><subject>Isoenzymes - analysis</subject><subject>Nucleoside Deaminases - analysis</subject><subject>Rabbits</subject><subject>Vertebrates: nervous system and sense organs</subject><issn>0022-1554</issn><issn>1551-5044</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><recordid>eNp1kM1r3DAQxUVJSTZpb70WfEgDgXgjWV_2sYR8wUIv7TViVh5vFGxpK3nZJH99lK5JLg0MPGbmx7zhEfKN0TljWp9zORdzLoUSdfOJzJiUrJRUiD0yo7SqyjwQB-QwpQdKmRCy3if7Ez4jd4tgoXfPMLrgi9AV0KIPyXksWoTBeUhYgG__O7dhWPf46PyqWMcwovNFrgjLpRuLZQTnv5DPHfQJv056RP5cXf6-uCkXv65vL34uSiuYHEupWuAIKBva1IpSpTRXoOvOSq4ralVTCQSNTdbXTmvV2Q4q3dKa1cj5ETnZ3c1__N1gGs3gksW-B49hk4zWgrKmURk824E2hpQidmYd3QDxyTBqXuM0XBphpnwy_n26u1kO2L7B7_vjaQ8p59hF8NalNyy7Vo1kGTvdYQlWaB7CJvqcxkeWP3bsvVvdb11Ekwbo-_wAM9vt9h8rBOcvxZOVzw</recordid><startdate>19870401</startdate><enddate>19870401</enddate><creator>Schrader, WP</creator><creator>West, CA</creator><creator>Strominger, NL</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>19870401</creationdate><title>Localization of adenosine deaminase and adenosine deaminase complexing protein in rabbit brain</title><author>Schrader, WP ; West, CA ; Strominger, NL</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c415t-56da3eae5909860066736a78fc53720c6924ea7e99240c69776fcfa27d0818e33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Adenosine Deaminase - analysis</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Brain - enzymology</topic><topic>Central nervous system</topic><topic>Central neurotransmission. Neuromudulation. Pathways and receptors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycoproteins - analysis</topic><topic>Histocytochemistry</topic><topic>Immunoenzyme Techniques</topic><topic>Isoenzymes - analysis</topic><topic>Nucleoside Deaminases - analysis</topic><topic>Rabbits</topic><topic>Vertebrates: nervous system and sense organs</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schrader, WP</creatorcontrib><creatorcontrib>West, CA</creatorcontrib><creatorcontrib>Strominger, NL</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>Schrader, WP</au><au>West, CA</au><au>Strominger, NL</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Localization of adenosine deaminase and adenosine deaminase complexing protein in rabbit brain</atitle><jtitle>The journal of histochemistry and cytochemistry</jtitle><addtitle>J Histochem Cytochem</addtitle><date>1987-04-01</date><risdate>1987</risdate><volume>35</volume><issue>4</issue><spage>443</spage><epage>451</epage><pages>443-451</pages><issn>0022-1554</issn><eissn>1551-5044</eissn><coden>JHCYAS</coden><abstract>Adenosine deaminase and adenosine deaminase complexing protein have been localized in rabbit brain. Brains fixed in paraformaldehyde or in Clarke's solution were blocked coronally. Blocks from brains fixed in paraformaldehyde were either frozen in liquid nitrogen or embedded in paraffin. Tissue fixed in Clarke's solution was embedded in paraffin. Sections from each block were stained by the peroxidase-antiperoxidase method for adenosine deaminase or complexing protein using affinity-purified goat antibodies. Adenosine deaminase and complexing protein did not co-localize. Adenosine deaminase was detected in oligodendroglia and in endothelial cells lining blood vessels, whereas complexing protein was concentrated in neurons. The subcellular location and appearance of the peroxidase reaction product associated with individual cells was also quite distinctive. The cell bodies of adenosine deaminase-positive oligodendroglia were filled with intense deposits of peroxidase reaction product. In contrast to oligodendroglia, the reaction product associated with most neurons stained for complexing protein was concentrated in granular-appearing cytoplasmic deposits. In some instances, these deposits were clustered about the nuclear membrane. Staining of neurons in the granular layer of cerebellum was an exception. Granule cells were lightly outlined by peroxidase reaction product. Cerebellar islands, also referred to as glomeruli, were stained an intense uniform brown. These results raise the possibility that oligodendroglia and blood vessel endothelia, through the action of adenosine deaminase, might play a role in controlling the concentration of extracellular adenosine in brain. They do not, however, support the suggestion that complexing protein aids in adenosine metabolism by positioning adenosine deaminase on the plasma membrane.</abstract><cop>Los Angeles, CA</cop><pub>Histochemical Soc</pub><pmid>3546489</pmid><doi>10.1177/35.4.3546489</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Adenosine Deaminase - analysis Animals Biological and medical sciences Brain - enzymology Central nervous system Central neurotransmission. Neuromudulation. Pathways and receptors Fundamental and applied biological sciences. Psychology Glycoproteins - analysis Histocytochemistry Immunoenzyme Techniques Isoenzymes - analysis Nucleoside Deaminases - analysis Rabbits Vertebrates: nervous system and sense organs |
title | Localization of adenosine deaminase and adenosine deaminase complexing protein in rabbit brain |
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