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Renin and cathepsin B in human pituitary lactotroph cells: an ultrastructural study
Renin, prorenin and cathepsin B were localized in human lactotrophs using immunoelectron microscopic techniques. Renin and prorenin were found in numerous cytoplasmic granules. Cathepsin B, a lysosomal enzyme known to be able to activate prorenin into renin, was also present in cytoplasmic granules...
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Published in: | Histochemistry 1989-01, Vol.91 (4), p.291-297 |
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container_title | Histochemistry |
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creator | SAINT-ANDRE, J. P ROHMER, V PINET, F ROUSSELET, M. C BIGORGNE, J. C CORVOL, P |
description | Renin, prorenin and cathepsin B were localized in human lactotrophs using immunoelectron microscopic techniques. Renin and prorenin were found in numerous cytoplasmic granules. Cathepsin B, a lysosomal enzyme known to be able to activate prorenin into renin, was also present in cytoplasmic granules of lactotrophs. The co-localization of renin and prolactin in the same secretory granules was demonstrated by double immunolabelling. Renin and cathepsin B were co-localized in some granules by the same technique. These results suggest a local activation of renin in the secretory granules of lactotrophs and support the hypothesis of a possible autocrine action of the renin-angiotensin system on prolactin release. |
doi_str_mv | 10.1007/BF00493003 |
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P ; ROHMER, V ; PINET, F ; ROUSSELET, M. C ; BIGORGNE, J. C ; CORVOL, P</creator><creatorcontrib>SAINT-ANDRE, J. P ; ROHMER, V ; PINET, F ; ROUSSELET, M. C ; BIGORGNE, J. C ; CORVOL, P</creatorcontrib><description>Renin, prorenin and cathepsin B were localized in human lactotrophs using immunoelectron microscopic techniques. Renin and prorenin were found in numerous cytoplasmic granules. Cathepsin B, a lysosomal enzyme known to be able to activate prorenin into renin, was also present in cytoplasmic granules of lactotrophs. The co-localization of renin and prolactin in the same secretory granules was demonstrated by double immunolabelling. Renin and cathepsin B were co-localized in some granules by the same technique. These results suggest a local activation of renin in the secretory granules of lactotrophs and support the hypothesis of a possible autocrine action of the renin-angiotensin system on prolactin release.</description><identifier>ISSN: 0301-5564</identifier><identifier>EISSN: 1432-119X</identifier><identifier>DOI: 10.1007/BF00493003</identifier><identifier>PMID: 2659557</identifier><identifier>CODEN: HCMYAL</identifier><language>eng</language><publisher>Berlin: Springer</publisher><subject>Adenoma - metabolism ; Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Cathepsins - metabolism ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. 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These results suggest a local activation of renin in the secretory granules of lactotrophs and support the hypothesis of a possible autocrine action of the renin-angiotensin system on prolactin release.</description><subject>Adenoma - metabolism</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Cathepsins - metabolism</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Hydrolases</subject><subject>Immunohistochemistry</subject><subject>Pituitary Gland - metabolism</subject><subject>Pituitary Gland - pathology</subject><subject>Pituitary Neoplasms - metabolism</subject><subject>Renin - metabolism</subject><issn>0301-5564</issn><issn>1432-119X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><recordid>eNpFkM1Lw0AQxRdRaq1evAt70YMQnc1usllvtlgVCoIf4C1MNhsaSZO4H4f-96Y02MsMw_zm8eYRcsngjgHI-_kSQCgOwI_IlAkeR4yp72MyBQ4sSpJUnJIz534AUpAym5BJnCYqSeSUfLybtm4ptiXV6Nemd8M0p0NZhw22tK99qD3aLW1Q-87brl9TbZrGPQxHNDTeovM2aB8sNtT5UG7PyUmFjTMXY5-Rr-XT5-IlWr09vy4eV5GOJfMRxqpMmIqrNNN88F8JXkgQJWIaSxSAcZGojDNTSmEKw8BAJkEpDQpZwSSfkZu9bm-732Cczze123nD1nTB5VKBYFzBAN7uQW0756yp8t7Wm-GpnEG-SzA_JDjAV6NqKDam_EfHyIb99bhHp7GpLLa6dgdFxdNMZMD_AMuud54</recordid><startdate>19890101</startdate><enddate>19890101</enddate><creator>SAINT-ANDRE, J. 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C ; CORVOL, P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c271t-a29d5192f68c3049f43b704daa627a40a2b59831ed74ebe10e087099c09a1b173</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Adenoma - metabolism</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Cathepsins - metabolism</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Hydrolases</topic><topic>Immunohistochemistry</topic><topic>Pituitary Gland - metabolism</topic><topic>Pituitary Gland - pathology</topic><topic>Pituitary Neoplasms - metabolism</topic><topic>Renin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>SAINT-ANDRE, J. P</creatorcontrib><creatorcontrib>ROHMER, V</creatorcontrib><creatorcontrib>PINET, F</creatorcontrib><creatorcontrib>ROUSSELET, M. C</creatorcontrib><creatorcontrib>BIGORGNE, J. C</creatorcontrib><creatorcontrib>CORVOL, P</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>Histochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>SAINT-ANDRE, J. P</au><au>ROHMER, V</au><au>PINET, F</au><au>ROUSSELET, M. C</au><au>BIGORGNE, J. C</au><au>CORVOL, P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Renin and cathepsin B in human pituitary lactotroph cells: an ultrastructural study</atitle><jtitle>Histochemistry</jtitle><addtitle>Histochemistry</addtitle><date>1989-01-01</date><risdate>1989</risdate><volume>91</volume><issue>4</issue><spage>291</spage><epage>297</epage><pages>291-297</pages><issn>0301-5564</issn><eissn>1432-119X</eissn><coden>HCMYAL</coden><abstract>Renin, prorenin and cathepsin B were localized in human lactotrophs using immunoelectron microscopic techniques. Renin and prorenin were found in numerous cytoplasmic granules. Cathepsin B, a lysosomal enzyme known to be able to activate prorenin into renin, was also present in cytoplasmic granules of lactotrophs. The co-localization of renin and prolactin in the same secretory granules was demonstrated by double immunolabelling. Renin and cathepsin B were co-localized in some granules by the same technique. These results suggest a local activation of renin in the secretory granules of lactotrophs and support the hypothesis of a possible autocrine action of the renin-angiotensin system on prolactin release.</abstract><cop>Berlin</cop><pub>Springer</pub><pmid>2659557</pmid><doi>10.1007/BF00493003</doi><tpages>7</tpages></addata></record> |
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ispartof | Histochemistry, 1989-01, Vol.91 (4), p.291-297 |
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language | eng |
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source | Springer Online Journal Archives |
subjects | Adenoma - metabolism Analytical, structural and metabolic biochemistry Biological and medical sciences Cathepsins - metabolism Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Humans Hydrolases Immunohistochemistry Pituitary Gland - metabolism Pituitary Gland - pathology Pituitary Neoplasms - metabolism Renin - metabolism |
title | Renin and cathepsin B in human pituitary lactotroph cells: an ultrastructural study |
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