Elevated extrahepatic expression and secretion of mammary-associated serum amyloid A 3 (M-SAA3) into colostrum
Mammary-associated serum amyloid A 3 (M-SAA3) was secreted at highly elevated levels in bovine, equine and ovine colostrum and found at lower levels in milk 4 days postparturition. N-terminal sequencing of the mature M-SAA3 protein from all the three species revealed a conserved four amino acid moti...
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| Veröffentlicht in: | Veterinary immunology and immunopathology 2001-12, Vol.83 (3), p.203-211 |
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| creator | McDonald, Thomas L. Larson, Marilynn A. Mack, David R. Weber, Annika |
| description | Mammary-associated serum amyloid A 3 (M-SAA3) was secreted at highly elevated levels in bovine, equine and ovine colostrum and found at lower levels in milk 4 days postparturition. N-terminal sequencing of the mature M-SAA3 protein from all the three species revealed a conserved four amino acid motif (TFLK) within the first eight residues. This motif has not been reported to be present in any of the hepatically-produced acute phase SAA (A-SAA) isoforms. Cloning of the bovine
M-Saa3 cDNA from mammary gland epithelial cells revealed an open reading frame that encoded a precursor protein of 131 amino acids which included an 18 amino acid signal peptide. The predicted 113 residue mature M-SAA3 protein had a theoretical molecular mass of 12,826
Da that corresponded with the observed 12.8
kDa molecular mass obtained for M-SAA3 in immunoblot analysis. The high abundance of this extrahepatically produced SAA3 isoform in the colostrum of healthy animals suggests that M-SAA3 may play an important functional role associated with newborn adaptation to extrauterine life and possibly mammary tissue remodeling. |
| doi_str_mv | 10.1016/S0165-2427(01)00380-4 |
| format | Article |
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M-Saa3 cDNA from mammary gland epithelial cells revealed an open reading frame that encoded a precursor protein of 131 amino acids which included an 18 amino acid signal peptide. The predicted 113 residue mature M-SAA3 protein had a theoretical molecular mass of 12,826
Da that corresponded with the observed 12.8
kDa molecular mass obtained for M-SAA3 in immunoblot analysis. The high abundance of this extrahepatically produced SAA3 isoform in the colostrum of healthy animals suggests that M-SAA3 may play an important functional role associated with newborn adaptation to extrauterine life and possibly mammary tissue remodeling.</description><identifier>ISSN: 0165-2427</identifier><identifier>EISSN: 1873-2534</identifier><identifier>DOI: 10.1016/S0165-2427(01)00380-4</identifier><identifier>PMID: 11730930</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Amino Acid Motifs - immunology ; Amino Acid Sequence ; Animals ; Base Sequence ; Bovine cDNA ; Cattle ; Chromatography, Affinity - veterinary ; Colostrum ; Colostrum - chemistry ; Colostrum - immunology ; DNA - chemistry ; Electrophoresis, Polyacrylamide Gel - veterinary ; Enzyme-Linked Immunosorbent Assay - veterinary ; Extrahepatic serum amyloid A ; Horses ; Mammary Glands, Animal - metabolism ; mammary-associated serum amyloid A3 ; Milk - chemistry ; Milk - immunology ; Molecular Sequence Data ; Molecular Weight ; Protein Isoforms ; Rabbits ; Reverse Transcriptase Polymerase Chain Reaction - veterinary ; RNA - chemistry ; RNA - isolation & purification ; Sequence Analysis, DNA ; Sequence Homology, Amino Acid ; Serum amyloid A 3 ; Serum Amyloid A Protein - biosynthesis ; Serum Amyloid A Protein - isolation & purification ; Serum Amyloid A Protein - metabolism ; Sheep</subject><ispartof>Veterinary immunology and immunopathology, 2001-12, Vol.83 (3), p.203-211</ispartof><rights>2001 Elsevier Science B.V.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c392t-436c378db3a94a074386d48b31f1cee288b04c197f1c9d9a1417fdfc791e21a73</citedby><cites>FETCH-LOGICAL-c392t-436c378db3a94a074386d48b31f1cee288b04c197f1c9d9a1417fdfc791e21a73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0165-2427(01)00380-4$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,778,782,3539,27907,27908,45978</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11730930$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>McDonald, Thomas L.</creatorcontrib><creatorcontrib>Larson, Marilynn A.</creatorcontrib><creatorcontrib>Mack, David R.</creatorcontrib><creatorcontrib>Weber, Annika</creatorcontrib><title>Elevated extrahepatic expression and secretion of mammary-associated serum amyloid A 3 (M-SAA3) into colostrum</title><title>Veterinary immunology and immunopathology</title><addtitle>Vet Immunol Immunopathol</addtitle><description>Mammary-associated serum amyloid A 3 (M-SAA3) was secreted at highly elevated levels in bovine, equine and ovine colostrum and found at lower levels in milk 4 days postparturition. N-terminal sequencing of the mature M-SAA3 protein from all the three species revealed a conserved four amino acid motif (TFLK) within the first eight residues. This motif has not been reported to be present in any of the hepatically-produced acute phase SAA (A-SAA) isoforms. Cloning of the bovine
M-Saa3 cDNA from mammary gland epithelial cells revealed an open reading frame that encoded a precursor protein of 131 amino acids which included an 18 amino acid signal peptide. The predicted 113 residue mature M-SAA3 protein had a theoretical molecular mass of 12,826
Da that corresponded with the observed 12.8
kDa molecular mass obtained for M-SAA3 in immunoblot analysis. The high abundance of this extrahepatically produced SAA3 isoform in the colostrum of healthy animals suggests that M-SAA3 may play an important functional role associated with newborn adaptation to extrauterine life and possibly mammary tissue remodeling.</description><subject>Amino Acid Motifs - immunology</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Bovine cDNA</subject><subject>Cattle</subject><subject>Chromatography, Affinity - veterinary</subject><subject>Colostrum</subject><subject>Colostrum - chemistry</subject><subject>Colostrum - immunology</subject><subject>DNA - chemistry</subject><subject>Electrophoresis, Polyacrylamide Gel - veterinary</subject><subject>Enzyme-Linked Immunosorbent Assay - veterinary</subject><subject>Extrahepatic serum amyloid A</subject><subject>Horses</subject><subject>Mammary Glands, Animal - metabolism</subject><subject>mammary-associated serum amyloid A3</subject><subject>Milk - chemistry</subject><subject>Milk - immunology</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Protein Isoforms</subject><subject>Rabbits</subject><subject>Reverse Transcriptase Polymerase Chain Reaction - veterinary</subject><subject>RNA - chemistry</subject><subject>RNA - isolation & purification</subject><subject>Sequence Analysis, DNA</subject><subject>Sequence Homology, Amino Acid</subject><subject>Serum amyloid A 3</subject><subject>Serum Amyloid A Protein - biosynthesis</subject><subject>Serum Amyloid A Protein - isolation & purification</subject><subject>Serum Amyloid A Protein - metabolism</subject><subject>Sheep</subject><issn>0165-2427</issn><issn>1873-2534</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1OHDEQhC1EBMuGRwD5hOAwidv2rO1TtEKQRCLKgeRsee0exdHMeGN7Ebw9sz8iRy7dKumrbqmKkAtgn4DB4vPjNNqGS66uGdwwJjRr5BGZgVai4a2Qx2T2hpySs1L-MsZao_UJOQVQghnBZmS86_HJVQwUn2t2f3DtavSTWGcsJaaRujHQgj5j3arU0cENg8svjSsl-bjzFsybgbrhpU8x0CUV9PpH87hcihsax5qoT30qdWI-kg-d6wueH_ac_L6_-3X7rXn4-fX77fKh8cLw2kix8ELpsBLOSMeUFHoRpF4J6MAjcq1XTHowapImGAcSVBc6rwwgB6fEnFzt765z-rfBUu0Qi8e-dyOmTbGKC75ohXkXBM2ZYhM6J-0e9DmVkrGz6xy3OVhgdtuI3TVit3FbBnbXiJWT7_LwYLMaMPx3HSqYgC97AKc8niJmW3zE0WOIGX21IcV3XrwCzvmaqw</recordid><startdate>20011201</startdate><enddate>20011201</enddate><creator>McDonald, Thomas L.</creator><creator>Larson, Marilynn A.</creator><creator>Mack, David R.</creator><creator>Weber, Annika</creator><general>Elsevier B.V</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>7T5</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20011201</creationdate><title>Elevated extrahepatic expression and secretion of mammary-associated serum amyloid A 3 (M-SAA3) into colostrum</title><author>McDonald, Thomas L. ; Larson, Marilynn A. ; Mack, David R. ; Weber, Annika</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c392t-436c378db3a94a074386d48b31f1cee288b04c197f1c9d9a1417fdfc791e21a73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Amino Acid Motifs - immunology</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Bovine cDNA</topic><topic>Cattle</topic><topic>Chromatography, Affinity - veterinary</topic><topic>Colostrum</topic><topic>Colostrum - chemistry</topic><topic>Colostrum - immunology</topic><topic>DNA - chemistry</topic><topic>Electrophoresis, Polyacrylamide Gel - veterinary</topic><topic>Enzyme-Linked Immunosorbent Assay - veterinary</topic><topic>Extrahepatic serum amyloid A</topic><topic>Horses</topic><topic>Mammary Glands, Animal - metabolism</topic><topic>mammary-associated serum amyloid A3</topic><topic>Milk - chemistry</topic><topic>Milk - immunology</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Protein Isoforms</topic><topic>Rabbits</topic><topic>Reverse Transcriptase Polymerase Chain Reaction - veterinary</topic><topic>RNA - chemistry</topic><topic>RNA - isolation & purification</topic><topic>Sequence Analysis, DNA</topic><topic>Sequence Homology, Amino Acid</topic><topic>Serum amyloid A 3</topic><topic>Serum Amyloid A Protein - biosynthesis</topic><topic>Serum Amyloid A Protein - isolation & purification</topic><topic>Serum Amyloid A Protein - metabolism</topic><topic>Sheep</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>McDonald, Thomas L.</creatorcontrib><creatorcontrib>Larson, Marilynn A.</creatorcontrib><creatorcontrib>Mack, David R.</creatorcontrib><creatorcontrib>Weber, Annika</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Veterinary immunology and immunopathology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>McDonald, Thomas L.</au><au>Larson, Marilynn A.</au><au>Mack, David R.</au><au>Weber, Annika</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Elevated extrahepatic expression and secretion of mammary-associated serum amyloid A 3 (M-SAA3) into colostrum</atitle><jtitle>Veterinary immunology and immunopathology</jtitle><addtitle>Vet Immunol Immunopathol</addtitle><date>2001-12-01</date><risdate>2001</risdate><volume>83</volume><issue>3</issue><spage>203</spage><epage>211</epage><pages>203-211</pages><issn>0165-2427</issn><eissn>1873-2534</eissn><abstract>Mammary-associated serum amyloid A 3 (M-SAA3) was secreted at highly elevated levels in bovine, equine and ovine colostrum and found at lower levels in milk 4 days postparturition. N-terminal sequencing of the mature M-SAA3 protein from all the three species revealed a conserved four amino acid motif (TFLK) within the first eight residues. This motif has not been reported to be present in any of the hepatically-produced acute phase SAA (A-SAA) isoforms. Cloning of the bovine
M-Saa3 cDNA from mammary gland epithelial cells revealed an open reading frame that encoded a precursor protein of 131 amino acids which included an 18 amino acid signal peptide. The predicted 113 residue mature M-SAA3 protein had a theoretical molecular mass of 12,826
Da that corresponded with the observed 12.8
kDa molecular mass obtained for M-SAA3 in immunoblot analysis. The high abundance of this extrahepatically produced SAA3 isoform in the colostrum of healthy animals suggests that M-SAA3 may play an important functional role associated with newborn adaptation to extrauterine life and possibly mammary tissue remodeling.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>11730930</pmid><doi>10.1016/S0165-2427(01)00380-4</doi><tpages>9</tpages></addata></record> |
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| subjects | Amino Acid Motifs - immunology Amino Acid Sequence Animals Base Sequence Bovine cDNA Cattle Chromatography, Affinity - veterinary Colostrum Colostrum - chemistry Colostrum - immunology DNA - chemistry Electrophoresis, Polyacrylamide Gel - veterinary Enzyme-Linked Immunosorbent Assay - veterinary Extrahepatic serum amyloid A Horses Mammary Glands, Animal - metabolism mammary-associated serum amyloid A3 Milk - chemistry Milk - immunology Molecular Sequence Data Molecular Weight Protein Isoforms Rabbits Reverse Transcriptase Polymerase Chain Reaction - veterinary RNA - chemistry RNA - isolation & purification Sequence Analysis, DNA Sequence Homology, Amino Acid Serum amyloid A 3 Serum Amyloid A Protein - biosynthesis Serum Amyloid A Protein - isolation & purification Serum Amyloid A Protein - metabolism Sheep |
| title | Elevated extrahepatic expression and secretion of mammary-associated serum amyloid A 3 (M-SAA3) into colostrum |
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