{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,10,30]],"date-time":"2023-10-30T13:33:02Z","timestamp":1698672782709},"reference-count":53,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2007,8,15]]},"abstract":"<jats:p>In a search for genes that modify iron homoeostasis, a gene (1300017J02Rik) was located immediately upstream of the murine TF (transferrin) gene. However, expression of the 1300017J02Rik gene product was not responsive to a number of modulators of iron metabolism. Specifically, expression was not altered in mouse models of iron disorders including mice with deficiencies in the haemochromatosis protein Hfe, the recombination-activating protein, Rag, \u03b22-microglobulin, TF, ceruloplasmin or Hb, or in mice with microcytic anaemia. Additionally, neither lipopolysaccharide nor hypoxia treatment resulted in any significant changes in the 1300017J02Rik expression level. The genomic DNA sequence suggested that the 1300017J02Rik gene product might be a protein equivalent to the pICA {porcine ICA [inhibitor of CA (carbonic anhydrase)]}. The coding region for the murine 1300017J02Rik gene was placed into the pNUT expression vector. Transformed BHK cells (baby-hamster kidney cells) were transfected with this plasmid, resulting in secretion of recombinant mICA (murine ICA) into the tissue culture medium. Following purification to homogeneity, the yield of mICA from the BHK cells was found to be considerably greater (at least 4-fold) than the yield of pICA from a previously reported Pichia pastoris (yeast) expression system. MS showed that the recombinant mICA was a glycoprotein that associated with CA in a 1:1 stoichiometry. Despite its high sequence similarity to TF, titration experiments showed that mICA was unable to bind iron specifically. Although enzymatic assays revealed that mICA was able to inhibit CA, it is unclear if this is its sole or even its major function since, to date, humans and other primates appear to lack functional ICA. Lastly, we note that this member of the TF superfamily is a relatively recent addition resulting from a tandem duplication event.<\/jats:p>","DOI":"10.1042\/bj20070384","type":"journal-article","created":{"date-parts":[[2007,11,7]],"date-time":"2007-11-07T15:36:45Z","timestamp":1194449805000},"page":"85-95","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":12,"title":["A novel murine protein with no effect on iron homoeostasis is homologous with transferrin and is the putative inhibitor of carbonic anhydrase"],"prefix":"10.1042","volume":"406","author":[{"given":"Fudi","family":"Wang","sequence":"first","affiliation":[{"name":"Division of Hematology\/Oncology, Children's Hospital Boston, and Harvard Medical School, Boston, MA 02115, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Adam\u00a0P.","family":"Lothrop","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Vermont College of Medicine, 89 Beaumont Avenue, Burlington, VT 05405-0068, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nicholas\u00a0G.","family":"James","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Vermont College of Medicine, 89 Beaumont Avenue, Burlington, VT 05405-0068, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tanya\u00a0A.\u00a0M.","family":"Griffiths","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology and Centre for Blood Research, University of British Columbia, Vancouver, BC, Canada V6T 1Z3"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lisa\u00a0A.","family":"Lambert","sequence":"additional","affiliation":[{"name":"Department of Biology, Chatham University, Woodland Road, Pittsburgh, PA 15232, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rachael","family":"Leverence","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Massachusetts at Amherst, Amherst, MA 01003, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Igor\u00a0A.","family":"Kaltashov","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Massachusetts at Amherst, Amherst, MA 01003, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nancy\u00a0C.","family":"Andrews","sequence":"additional","affiliation":[{"name":"Division of Hematology\/Oncology, Children's Hospital Boston, and Harvard Medical School, Boston, MA 02115, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ross\u00a0T.\u00a0A.","family":"MacGillivray","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology and Centre for Blood Research, University of British Columbia, Vancouver, BC, Canada V6T 1Z3"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Anne\u00a0B.","family":"Mason","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Vermont College of Medicine, 89 Beaumont Avenue, Burlington, VT 05405-0068, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2007,7,26]]},"reference":[{"key":"2021112213345006000_B1","doi-asserted-by":"crossref","first-page":"48615","DOI":"10.1074\/jbc.R100045200","article-title":"Carbonic anhydrase: new insights for an ancient enzyme","volume":"276","author":"Tripp","year":"2001","journal-title":"J. Biol. Chem."},{"key":"2021112213345006000_B2","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1002\/humu.9266","article-title":"Carbonic anhydrase II deficiency syndrome (osteopetrosis with renal tubular acidosis and brain calcification): novel mutations in CA2 identified by direct sequencing expand the opportunity for genotype\u2013phenotype correlation","volume":"24","author":"Shah","year":"2004","journal-title":"Hum. Mutat."},{"key":"2021112213345006000_B3","doi-asserted-by":"crossref","first-page":"1947","DOI":"10.1182\/blood.V97.7.1947","article-title":"Bone marrow transplantation corrects osteopetrosis in the carbonic anhydrase II deficiency syndrome","volume":"97","author":"McMahon","year":"2001","journal-title":"Blood"},{"key":"2021112213345006000_B4","doi-asserted-by":"crossref","first-page":"4327","DOI":"10.1021\/bi9627424","article-title":"Cloning, sequencing, and recombinant expression of the porcine inhibitor of carbonic anhydrase: a novel member of the transferrin family","volume":"36","author":"Wuebbens","year":"1997","journal-title":"Biochemistry"},{"key":"2021112213345006000_B5","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1046\/j.1365-201X.2002.01010.x","article-title":"Localization of a protein inhibitor of carbonic anhydrase in pig tissues","volume":"176","author":"Ridderstrale","year":"2002","journal-title":"Acta Physiol. Scand."},{"key":"2021112213345006000_B6","doi-asserted-by":"crossref","first-page":"474","DOI":"10.1113\/jphysiol.1938.sp003574","article-title":"The carbonic anhydrase inhibitor in serum","volume":"91","author":"Booth","year":"1938","journal-title":"J. Physiol."},{"key":"2021112213345006000_B7","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1080\/713609332","article-title":"Molecular mechanisms and regulation of iron transport","volume":"40","author":"Chung","year":"2003","journal-title":"Crit. Rev. Clin. Lab. Sci."},{"key":"2021112213345006000_B8","doi-asserted-by":"crossref","first-page":"2263","DOI":"10.1073\/pnas.80.8.2263","article-title":"Binding of apotransferrin to K562 cells: explanation of the transferrin cycle","volume":"80","author":"Klausner","year":"1983","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021112213345006000_B9","doi-asserted-by":"crossref","first-page":"1930","DOI":"10.1016\/S0021-9258(19)62337-9","article-title":"Stoichiometric and site characteristics of the binding of iron to human transferrin","volume":"253","author":"Aisen","year":"1978","journal-title":"J. Biol. Chem."},{"key":"2021112213345006000_B10","doi-asserted-by":"crossref","first-page":"9947","DOI":"10.1021\/bi00105a019","article-title":"Receptor-modulated iron release from transferrin: differential effects on N- and C-terminal sites","volume":"30","author":"Bali","year":"1991","journal-title":"Biochemistry"},{"key":"2021112213345006000_B11","doi-asserted-by":"crossref","first-page":"12330","DOI":"10.1021\/bi034991f","article-title":"Iron release from transferrin, its C-lobe, and their complexes with transferrin receptor: presence of N-lobe accelerates release from C-lobe at endosomal pH","volume":"42","author":"Zak","year":"2003","journal-title":"Biochemistry"},{"key":"2021112213345006000_B12","doi-asserted-by":"crossref","first-page":"3701","DOI":"10.1021\/bi027071q","article-title":"Investigation of the mechanism of iron release from the C-lobe of human serum transferrin: mutational analysis of the role of a pH sensitive triad","volume":"42","author":"Halbrooks","year":"2003","journal-title":"Biochemistry"},{"key":"2021112213345006000_B13","doi-asserted-by":"crossref","first-page":"8013","DOI":"10.1021\/bi050015f","article-title":"Mutational analysis of C-lobe ligands of human serum transferrin: insights into the mechanism of iron release","volume":"44","author":"Mason","year":"2005","journal-title":"Biochemistry"},{"key":"2021112213345006000_B14","doi-asserted-by":"crossref","first-page":"15451","DOI":"10.1021\/bi0518693","article-title":"Composition of pH sensitive triad in C-lobe of human serum transferrin: comparison to sequences of ovotransferrin and lactoferrin provides insight into functional differences in iron release","volume":"44","author":"Halbrooks","year":"2005","journal-title":"Biochemistry"},{"key":"2021112213345006000_B15","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1139\/o01-153","article-title":"Lactoferrin and transferrin: functional variations on a common structural framework","volume":"80","author":"Baker","year":"2002","journal-title":"Biochem. Cell Biol."},{"key":"2021112213345006000_B16","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/j.cbpb.2005.07.007","article-title":"Evolution of the transferrin family: conservation of residues associated with iron and anion binding","volume":"142","author":"Lambert","year":"2005","journal-title":"Comp. Biochem. Physiol. Part B Biochem. Mol. Biol."},{"key":"2021112213345006000_B17","first-page":"742","article-title":"Biochemical and immunochemical comparison of saxiphilin and transferrin, two structurally related plasma proteins from Rana catesbeiana","volume":"44","author":"Li","year":"1993","journal-title":"Mol. Pharmacol."},{"key":"2021112213345006000_B18","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1016\/0014-5793(92)80060-T","article-title":"Human melanotransferrin (p97) has only one functional iron-binding site","volume":"298","author":"Baker","year":"1992","journal-title":"FEBS Lett."},{"key":"2021112213345006000_B19","doi-asserted-by":"crossref","first-page":"4435","DOI":"10.1046\/j.1432-1033.2002.03140.x","article-title":"The soluble form of the membrane-bound transferrin homologue, melanotransferrin, inefficiently donates iron to cells via nonspecific internalization and degradation of the protein","volume":"269","author":"Food","year":"2002","journal-title":"Eur. J. Biochem."},{"key":"2021112213345006000_B20","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.bbagen.2004.12.002","article-title":"Examination of the distribution of the transferrin homologue, melanotransferrin (tumour antigen p97), in mouse and human","volume":"1722","author":"Sekyere","year":"2005","journal-title":"Biochim. Biophys. Acta"},{"key":"2021112213345006000_B21","doi-asserted-by":"crossref","first-page":"2599","DOI":"10.1182\/blood-2005-10-4174","article-title":"Role of melanotransferrin in iron metabolism: studies using targeted gene disruption in vivo","volume":"107","author":"Sekyere","year":"2006","journal-title":"Blood"},{"key":"2021112213345006000_B22","doi-asserted-by":"crossref","first-page":"2157","DOI":"10.1093\/carcin\/bgl045","article-title":"The function of melanotransferrin: a role in melanoma cell proliferation and tumorigenesis","volume":"27","author":"Dunn","year":"2006","journal-title":"Carcinogenesis"},{"key":"2021112213345006000_B23","doi-asserted-by":"crossref","first-page":"1113","DOI":"10.1182\/blood.V96.3.1113","article-title":"The molecular defect in hypotransferrinemic mice","volume":"96","author":"Trenor","year":"2000","journal-title":"Blood"},{"key":"2021112213345006000_B24","doi-asserted-by":"crossref","first-page":"1209","DOI":"10.1172\/JCI9635","article-title":"Genes that modify the hemochromatosis phenotype in mice","volume":"105","author":"Levy","year":"2000","journal-title":"J. Clin. Invest."},{"key":"2021112213345006000_B25","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1038\/ng1152","article-title":"Regulatory defects in liver and intestine implicate abnormal hepcidin and Cybrd1 expression in mouse hemochromatosis","volume":"34","author":"Muckenthaler","year":"2003","journal-title":"Nat. Genet."},{"key":"2021112213345006000_B26","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1038\/ng1350","article-title":"An Hfe-dependent pathway mediates hyposideremia in response to lipopolysaccharide-induced inflammation in mice","volume":"36","author":"Roy","year":"2004","journal-title":"Nat. Genet."},{"key":"2021112213345006000_B27","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1038\/ng0897-383","article-title":"Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene","volume":"16","author":"Fleming","year":"1997","journal-title":"Nat. Genet."},{"key":"2021112213345006000_B28","doi-asserted-by":"crossref","first-page":"1270","DOI":"10.1038\/ng1659","article-title":"A mutation in Sec15l1 causes anemia in hemoglobin deficit (hbd) mice","volume":"37","author":"Lim","year":"2005","journal-title":"Nat. Genet."},{"key":"2021112213345006000_B29","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1016\/0092-8674(87)90497-1","article-title":"Cell lineage ablation in transgenic mice by cell-specific expression of a toxic gene","volume":"50","author":"Palmiter","year":"1987","journal-title":"Cell"},{"key":"2021112213345006000_B30","doi-asserted-by":"crossref","first-page":"1654","DOI":"10.1021\/bi00458a043","article-title":"Expression of the amino-terminal half-molecule of human serum transferrin in cultured cells and characterization of the recombinant protein","volume":"29","author":"Funk","year":"1990","journal-title":"Biochemistry"},{"key":"2021112213345006000_B31","doi-asserted-by":"crossref","first-page":"5472","DOI":"10.1021\/bi00071a025","article-title":"Expression of glycosylated and nonglycosylated human transferrin in mammalian cells: characterization of the recombinant proteins with comparison to three commercially available transferrins","volume":"32","author":"Mason","year":"1993","journal-title":"Biochemistry"},{"key":"2021112213345006000_B32","doi-asserted-by":"crossref","first-page":"9448","DOI":"10.1021\/bi025927l","article-title":"Differential effect of a His tag at the N- and C-termini: functional studies with recombinant human serum transferrin","volume":"41","author":"Mason","year":"2002","journal-title":"Biochemistry"},{"key":"2021112213345006000_B33","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1016\/j.pep.2004.04.013","article-title":"Expression, purification, and characterization of authentic monoferric and apo-human serum transferrins","volume":"36","author":"Mason","year":"2004","journal-title":"Protein Expression Purif."},{"key":"2021112213345006000_B34","doi-asserted-by":"crossref","first-page":"6663","DOI":"10.1021\/bi0600695","article-title":"Effect of glycosylation on the function of a soluble, recombinant form of the transferrin receptor","volume":"45","author":"Byrne","year":"2006","journal-title":"Biochemistry"},{"key":"2021112213345006000_B35","doi-asserted-by":"crossref","first-page":"2411","DOI":"10.1002\/pro.5560041120","article-title":"How to measure and predict the molar absorption coefficient of a protein","volume":"4","author":"Pace","year":"1995","journal-title":"Protein Sci."},{"key":"2021112213345006000_B36","first-page":"141","article-title":"Amino acid composition of various forms of bovine and human erythrocyte carbonic anhydrase","volume":"85","author":"Nyman","year":"1964","journal-title":"Biochim. Biophys. Acta"},{"key":"2021112213345006000_B37","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1016\/S0021-9258(18)51011-5","article-title":"Electrometric and colorimetric determination of carbonic anhydrase","volume":"176","author":"Wilbur","year":"1948","journal-title":"J. Biol. Chem."},{"key":"2021112213345006000_B38","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1002\/hep.21233","article-title":"Multiple polymorphic loci determine basal hepatic and splenic iron status in mice","volume":"44","author":"Grant","year":"2006","journal-title":"Hepatology"},{"key":"2021112213345006000_B39","first-page":"9","article-title":"Identification of the bacteria inhibiting, iron binding protein of egg white as conalbumin","volume":"11","author":"Alderton","year":"1946","journal-title":"Arch. Biochem. Biophys."},{"key":"2021112213345006000_B40","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/0003-9861(59)90091-8","article-title":"Conalbumin: a rapid, high-yield preparation from egg white","volume":"82","author":"Woodworth","year":"1959","journal-title":"Arch. Biochem. Biophys."},{"key":"2021112213345006000_B41","doi-asserted-by":"crossref","first-page":"12536","DOI":"10.1021\/bi00164a034","article-title":"Purification and characterization of a carbonic anhydrase II inhibitor from porcine plasma","volume":"31","author":"Roush","year":"1992","journal-title":"Biochemistry"},{"key":"2021112213345006000_B42","doi-asserted-by":"crossref","first-page":"3613","DOI":"10.1016\/S0021-9258(18)83413-5","article-title":"Fluorescence and absorption studies of the binding of copper and iron to transferrin","volume":"244","author":"Lehrer","year":"1969","journal-title":"J. Biol. Chem."},{"key":"2021112213345006000_B43","doi-asserted-by":"crossref","first-page":"L71","DOI":"10.1016\/S0020-1693(00)88536-9","article-title":"The origin of the visible absorption in metal transferrins","volume":"56","author":"Patch","year":"1981","journal-title":"Inorg. Chim. Acta"},{"key":"2021112213345006000_B44","doi-asserted-by":"crossref","first-page":"14853","DOI":"10.1021\/bi9719556","article-title":"Inequivalence of the two tyrosine ligands in the N-lobe of human serum transferrin","volume":"36","author":"He","year":"1997","journal-title":"Biochemistry"},{"key":"2021112213345006000_B45","doi-asserted-by":"crossref","first-page":"988","DOI":"10.1101\/gr.1865504","article-title":"GeneWise and Genomewise","volume":"14","author":"Birney","year":"2004","journal-title":"Genome Res."},{"key":"2021112213345006000_B46","doi-asserted-by":"crossref","first-page":"11963","DOI":"10.1021\/bi00096a004","article-title":"Structural evidence for a pH-sensitive dilysine trigger in the hen ovotransferrin N-lobe: implications for transferrin iron release","volume":"32","author":"Dewan","year":"1993","journal-title":"Biochemistry"},{"key":"2021112213345006000_B47","doi-asserted-by":"crossref","first-page":"9704","DOI":"10.1021\/bi990134t","article-title":"Dual role of Lys206\u2013Lys296 interaction in human transferrin N-lobe: iron-release trigger and anion-binding site","volume":"38","author":"He","year":"1999","journal-title":"Biochemistry"},{"key":"2021112213345006000_B48","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.cbpc.2004.09.012","article-title":"Evolution of the duplications in the transferrin family of proteins","volume":"140","author":"Lambert","year":"2005","journal-title":"Comp. Biochem. Physiol. Part B Biochem. Mol. Biol."},{"key":"2021112213345006000_B49","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1086\/302219","article-title":"When less is more: gene loss as an engine of evolutionary change","volume":"64","author":"Olson","year":"1999","journal-title":"Am. J. Hum. Genet."},{"key":"2021112213345006000_B50","doi-asserted-by":"crossref","first-page":"e76","DOI":"10.1371\/journal.pbio.0040076","article-title":"When less is more: losing genes on the path to becoming human","volume":"4","author":"Gross","year":"2006","journal-title":"PLoS Biol."},{"key":"2021112213345006000_B51","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1128\/MCB.23.1.178-185.2003","article-title":"Iron status in mice carrying a targeted disruption of lactoferrin","volume":"23","author":"Ward","year":"2003","journal-title":"Mol. Cell. Biol."},{"key":"2021112213345006000_B52","doi-asserted-by":"crossref","first-page":"2182","DOI":"10.1016\/S0021-9258(19)41699-2","article-title":"The synergistic binding of anions and Fe(III) by transferrin","volume":"250","author":"Schlabach","year":"1975","journal-title":"J. Biol. Chem."},{"key":"2021112213345006000_B53","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1093\/bib\/5.2.150","article-title":"MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment","volume":"5","author":"Kumar","year":"2004","journal-title":"Brief. Bioinform."}],"container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/406\/1\/85\/646470\/bj4060085.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/406\/1\/85\/646470\/bj4060085.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,22]],"date-time":"2021-11-22T14:37:50Z","timestamp":1637591870000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/406\/1\/85\/42276\/A-novel-murine-protein-with-no-effect-on-iron"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2007,7,26]]},"references-count":53,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2007,8,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj20070384","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[2007,7,26]]}}}