The Identification of Secreted Carbonic Anhydrase VI as a Constitutive Glycoprotein of Human and Rat Milk
In addition to essential nutrients, human milk contains several classes of bioactive factors such as enzymes, hormones, and growth factors, many of which are implicated in infantile growth and development. Secretory carbonic anhydrase isoenzyme VI (CA VI) has been identified earlier as an essential...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2001-09, Vol.98 (20), p.11604-11608 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Karhumaa, Pepe Leinonen, Jukka Parkkila, Seppo Kaunisto, Kari Tapanainen, Juha Rajaniemi, Hannu |
| description | In addition to essential nutrients, human milk contains several classes of bioactive factors such as enzymes, hormones, and growth factors, many of which are implicated in infantile growth and development. Secretory carbonic anhydrase isoenzyme VI (CA VI) has been identified earlier as an essential component of mammalian saliva, and we demonstrate here by using biochemical and immunohistochemical techniques that it is also an elementary component of milk. The 42-kDa glycopolypeptide purified from human milk in CA inhibitor affinity chromatography shared 100% homology with salivary CA VI in the protein sequence analysis (40% coverage), and its digestion with PNGase F resulted in a polypeptide backbone similar in size to salivary CA VI. Quantification of CA VI in milk by using a time-resolved immunofluorometric assay revealed an approximately eight-times-higher concentration in human colostrum than in mature milk, the latter corresponding to the levels previously detected in human saliva. The high concentration in the colostrum, in particular its functional and structural stability in an acidic milieu, and its growth-supporting role in the taste buds suggest that milk CA VI is an essential factor in normal growth and development of the infant alimentary tract. |
| doi_str_mv | 10.1073/pnas.121172598 |
| format | Article |
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Secretory carbonic anhydrase isoenzyme VI (CA VI) has been identified earlier as an essential component of mammalian saliva, and we demonstrate here by using biochemical and immunohistochemical techniques that it is also an elementary component of milk. The 42-kDa glycopolypeptide purified from human milk in CA inhibitor affinity chromatography shared 100% homology with salivary CA VI in the protein sequence analysis (40% coverage), and its digestion with PNGase F resulted in a polypeptide backbone similar in size to salivary CA VI. Quantification of CA VI in milk by using a time-resolved immunofluorometric assay revealed an approximately eight-times-higher concentration in human colostrum than in mature milk, the latter corresponding to the levels previously detected in human saliva. The high concentration in the colostrum, in particular its functional and structural stability in an acidic milieu, and its growth-supporting role in the taste buds suggest that milk CA VI is an essential factor in normal growth and development of the infant alimentary tract.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.121172598</identifier><identifier>PMID: 11553764</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Adults ; Animals ; Antibodies ; Biological Sciences ; Carbonic Anhydrases - metabolism ; Cellular biology ; Colostrum ; Colostrum - enzymology ; Enzymes ; Female ; Hormones ; Human colostrum ; Humans ; Infant, Newborn ; Isoenzymes - metabolism ; Mammary glands ; Milk ; Milk - enzymology ; Milk, Human - enzymology ; Postpartum Period - metabolism ; Proteins ; Rabbits ; Rats ; Saliva ; Saliva - enzymology ; Salivary glands ; Taste buds ; Time Factors</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2001-09, Vol.98 (20), p.11604-11608</ispartof><rights>Copyright 1993-2001 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Sep 25, 2001</rights><rights>Copyright © 2001, The National Academy of Sciences 2001</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c555t-bc886c12bb442417416ca34dd579015a1ec97ca32e2aae8df4fb3bf75e2df5da3</citedby><cites>FETCH-LOGICAL-c555t-bc886c12bb442417416ca34dd579015a1ec97ca32e2aae8df4fb3bf75e2df5da3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/98/20.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3056761$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3056761$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11553764$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Karhumaa, Pepe</creatorcontrib><creatorcontrib>Leinonen, Jukka</creatorcontrib><creatorcontrib>Parkkila, Seppo</creatorcontrib><creatorcontrib>Kaunisto, Kari</creatorcontrib><creatorcontrib>Tapanainen, Juha</creatorcontrib><creatorcontrib>Rajaniemi, Hannu</creatorcontrib><title>The Identification of Secreted Carbonic Anhydrase VI as a Constitutive Glycoprotein of Human and Rat Milk</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>In addition to essential nutrients, human milk contains several classes of bioactive factors such as enzymes, hormones, and growth factors, many of which are implicated in infantile growth and development. Secretory carbonic anhydrase isoenzyme VI (CA VI) has been identified earlier as an essential component of mammalian saliva, and we demonstrate here by using biochemical and immunohistochemical techniques that it is also an elementary component of milk. The 42-kDa glycopolypeptide purified from human milk in CA inhibitor affinity chromatography shared 100% homology with salivary CA VI in the protein sequence analysis (40% coverage), and its digestion with PNGase F resulted in a polypeptide backbone similar in size to salivary CA VI. Quantification of CA VI in milk by using a time-resolved immunofluorometric assay revealed an approximately eight-times-higher concentration in human colostrum than in mature milk, the latter corresponding to the levels previously detected in human saliva. The high concentration in the colostrum, in particular its functional and structural stability in an acidic milieu, and its growth-supporting role in the taste buds suggest that milk CA VI is an essential factor in normal growth and development of the infant alimentary tract.</description><subject>Adults</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Biological Sciences</subject><subject>Carbonic Anhydrases - metabolism</subject><subject>Cellular biology</subject><subject>Colostrum</subject><subject>Colostrum - enzymology</subject><subject>Enzymes</subject><subject>Female</subject><subject>Hormones</subject><subject>Human colostrum</subject><subject>Humans</subject><subject>Infant, Newborn</subject><subject>Isoenzymes - metabolism</subject><subject>Mammary glands</subject><subject>Milk</subject><subject>Milk - enzymology</subject><subject>Milk, Human - enzymology</subject><subject>Postpartum Period - metabolism</subject><subject>Proteins</subject><subject>Rabbits</subject><subject>Rats</subject><subject>Saliva</subject><subject>Saliva - enzymology</subject><subject>Salivary glands</subject><subject>Taste buds</subject><subject>Time Factors</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp90c-PEyEUB3BiNG5dvXoySjwYL1OBgWEm8bJpdLfJGhNdvZI3wFjqFCowG_vfS22tPw6eSODzfbyXh9BjSuaUyPrV1kOaU0apZKJr76AZJR2tGt6Ru2hGCJNVyxk_Qw9SWhNCOtGS--iMUiFq2fAZcjcri5fG-uwGpyG74HEY8Eero83W4AXEPnin8YVf7UyEZPHnJYaEAS-CT9nlKbtbiy_HnQ7bGLJ1PwtcTRvwGLzBHyDjd278-hDdG2BM9tHxPEef3r65WVxV1-8vl4uL60oLIXLV67ZtNGV9z0vjVHLaaKi5MUJ2hAqgVney3DDLAGxrBj70dT9IYZkZhIH6HL0-1N1O_cYaXUaLMKptdBuIOxXAqb9fvFupL-FWiVbKpsRfHOMxfJtsymrjkrbjCN6GKSlJGWuk7Ap8_g9chyn6MppihNZCtpwXND8gHUNK0Q6nPihR-wWq_QLVaYEl8PTP7n_z48YKeHkE--Cv564tnxbUEK6GaRyz_Z4LffZ_WsSTg1inHOKJ1EQ0sqH1D0vluiw</recordid><startdate>20010925</startdate><enddate>20010925</enddate><creator>Karhumaa, Pepe</creator><creator>Leinonen, Jukka</creator><creator>Parkkila, Seppo</creator><creator>Kaunisto, Kari</creator><creator>Tapanainen, Juha</creator><creator>Rajaniemi, Hannu</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><general>The National Academy of Sciences</general><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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20010925</creationdate><title>The Identification of Secreted Carbonic Anhydrase VI as a Constitutive Glycoprotein of Human and Rat Milk</title><author>Karhumaa, Pepe ; Leinonen, Jukka ; Parkkila, Seppo ; Kaunisto, Kari ; Tapanainen, Juha ; Rajaniemi, Hannu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c555t-bc886c12bb442417416ca34dd579015a1ec97ca32e2aae8df4fb3bf75e2df5da3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Adults</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Biological Sciences</topic><topic>Carbonic Anhydrases - metabolism</topic><topic>Cellular biology</topic><topic>Colostrum</topic><topic>Colostrum - enzymology</topic><topic>Enzymes</topic><topic>Female</topic><topic>Hormones</topic><topic>Human colostrum</topic><topic>Humans</topic><topic>Infant, Newborn</topic><topic>Isoenzymes - metabolism</topic><topic>Mammary glands</topic><topic>Milk</topic><topic>Milk - enzymology</topic><topic>Milk, Human - enzymology</topic><topic>Postpartum Period - metabolism</topic><topic>Proteins</topic><topic>Rabbits</topic><topic>Rats</topic><topic>Saliva</topic><topic>Saliva - enzymology</topic><topic>Salivary glands</topic><topic>Taste buds</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Karhumaa, Pepe</creatorcontrib><creatorcontrib>Leinonen, Jukka</creatorcontrib><creatorcontrib>Parkkila, Seppo</creatorcontrib><creatorcontrib>Kaunisto, Kari</creatorcontrib><creatorcontrib>Tapanainen, Juha</creatorcontrib><creatorcontrib>Rajaniemi, Hannu</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Karhumaa, Pepe</au><au>Leinonen, Jukka</au><au>Parkkila, Seppo</au><au>Kaunisto, Kari</au><au>Tapanainen, Juha</au><au>Rajaniemi, Hannu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Identification of Secreted Carbonic Anhydrase VI as a Constitutive Glycoprotein of Human and Rat Milk</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2001-09-25</date><risdate>2001</risdate><volume>98</volume><issue>20</issue><spage>11604</spage><epage>11608</epage><pages>11604-11608</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>In addition to essential nutrients, human milk contains several classes of bioactive factors such as enzymes, hormones, and growth factors, many of which are implicated in infantile growth and development. Secretory carbonic anhydrase isoenzyme VI (CA VI) has been identified earlier as an essential component of mammalian saliva, and we demonstrate here by using biochemical and immunohistochemical techniques that it is also an elementary component of milk. The 42-kDa glycopolypeptide purified from human milk in CA inhibitor affinity chromatography shared 100% homology with salivary CA VI in the protein sequence analysis (40% coverage), and its digestion with PNGase F resulted in a polypeptide backbone similar in size to salivary CA VI. Quantification of CA VI in milk by using a time-resolved immunofluorometric assay revealed an approximately eight-times-higher concentration in human colostrum than in mature milk, the latter corresponding to the levels previously detected in human saliva. 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| subjects | Adults Animals Antibodies Biological Sciences Carbonic Anhydrases - metabolism Cellular biology Colostrum Colostrum - enzymology Enzymes Female Hormones Human colostrum Humans Infant, Newborn Isoenzymes - metabolism Mammary glands Milk Milk - enzymology Milk, Human - enzymology Postpartum Period - metabolism Proteins Rabbits Rats Saliva Saliva - enzymology Salivary glands Taste buds Time Factors |
| title | The Identification of Secreted Carbonic Anhydrase VI as a Constitutive Glycoprotein of Human and Rat Milk |
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