{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,10]],"date-time":"2026-03-10T15:31:05Z","timestamp":1773156665249,"version":"3.50.1"},"reference-count":31,"publisher":"Rockefeller University Press","issue":"3","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1998,5,4]]},"abstract":"<jats:p>Microfibrils are ubiquitous fibrillin-rich polymers that are thought to provide long-range elasticity to extracellular matrices, including the zonular filaments of mammalian eyes. X-ray diffraction of hydrated bovine zonular filaments demonstrated meridional diffraction peaks indexing on a fundamental axial periodicity (D) of \u223c56 nm. A Ca2+-induced reversible change in the intensities of the meridional Bragg peaks indicated that supramolecular rearrangements occurred in response to altered concentrations of free Ca2+. In the presence of Ca2+, the dominant diffracting subspecies were microfibrils aligned in an axial 0.33-D stagger. The removal of Ca2+ caused an enhanced regularity in molecular spacing of individual microfibrils, and the contribution from microfibrils not involved in staggered arrays became more dominant. Scanning transmission electron microscopy of isolated microfibrils revealed that Ca2+ removal or addition caused significant, reversible changes in microfibril mass distribution and periodicity. These results were consistent with evidence from x-ray diffraction. Simulated meridional x-ray diffraction profiles and analyses of isolated Ca2+-containing, staggered microfibrillar arrays were used to interpret the effects of Ca2+. These observations highlight the importance of Ca2+ to microfibrils and microfibrillar arrays in vivo.<\/jats:p>","DOI":"10.1083\/jcb.141.3.829","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T16:47:50Z","timestamp":1027702070000},"page":"829-837","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":52,"title":["Calcium Determines the Supramolecular Organization of Fibrillin-rich Microfibrils"],"prefix":"10.1083","volume":"141","author":[{"given":"T.J.","family":"Wess","sequence":"first","affiliation":[{"name":"*Department of Biological and Molecular Sciences, University of Stirling, Stirling FK9 4LA, United Kingdom; \u2021The Royal Veterinary and Agricultural University, 1958 Fredriksberg C, Copenhagen, Denmark; and \u00a7School of Biological Sciences, University of Manchester, Manchester M13 9PT, United Kingdom"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"P.P.","family":"Purslow","sequence":"additional","affiliation":[{"name":"*Department of Biological and Molecular Sciences, University of Stirling, Stirling FK9 4LA, United Kingdom; \u2021The Royal Veterinary and Agricultural University, 1958 Fredriksberg C, Copenhagen, Denmark; and \u00a7School of Biological Sciences, University of Manchester, Manchester M13 9PT, United Kingdom"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M.J.","family":"Sherratt","sequence":"additional","affiliation":[{"name":"*Department of Biological and Molecular Sciences, University of Stirling, Stirling FK9 4LA, United Kingdom; \u2021The Royal Veterinary and Agricultural University, 1958 Fredriksberg C, Copenhagen, Denmark; and \u00a7School of Biological Sciences, University of Manchester, Manchester M13 9PT, United Kingdom"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"J.","family":"Ashworth","sequence":"additional","affiliation":[{"name":"*Department of Biological and Molecular Sciences, University of Stirling, Stirling FK9 4LA, United Kingdom; \u2021The Royal Veterinary and Agricultural University, 1958 Fredriksberg C, Copenhagen, Denmark; and \u00a7School of Biological Sciences, University of Manchester, Manchester M13 9PT, United Kingdom"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"C.A.","family":"Shuttleworth","sequence":"additional","affiliation":[{"name":"*Department of Biological and Molecular Sciences, University of Stirling, Stirling FK9 4LA, United Kingdom; \u2021The Royal Veterinary and Agricultural University, 1958 Fredriksberg C, Copenhagen, Denmark; and \u00a7School of Biological Sciences, University of Manchester, Manchester M13 9PT, United Kingdom"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"C.M.","family":"Kielty","sequence":"additional","affiliation":[{"name":"*Department of Biological and Molecular Sciences, University of Stirling, Stirling FK9 4LA, United Kingdom; \u2021The Royal Veterinary and Agricultural University, 1958 Fredriksberg C, Copenhagen, Denmark; and \u00a7School of Biological Sciences, University of Manchester, Manchester M13 9PT, United Kingdom"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"291","published-online":{"date-parts":[[1998,5,4]]},"reference":[{"key":"2023072207355871800_B1","doi-asserted-by":"crossref","first-page":"476","DOI":"10.1006\/geno.1993.1350","article-title":"Fibrillin binds calcium and is coded by cDNAs that reveal a multidomain structure and alternatively spliced exons at the 5\u2032 end","volume":"17","author":"Corson","year":"1993","journal-title":"Genomics"},{"key":"2023072207355871800_B2","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1083\/jcb.136.3.729","article-title":"Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility","volume":"136","author":"Danielson","year":"1997","journal-title":"J Cell Biol"},{"key":"2023072207355871800_B3","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1016\/S0092-8674(00)81259-3","article-title":"Solution structure of a pair of Ca2+binding epidermal growth factor-like domains: implications for the Marfan syndrome and other genetic disorders","volume":"85","author":"Downing","year":"1996","journal-title":"Cell"},{"key":"2023072207355871800_B4","doi-asserted-by":"crossref","first-page":"11429","DOI":"10.1016\/S0021-9258(18)67403-4","article-title":"The major antigen of elastin-associated microfibrils is a 31-kDa glycoprotein","volume":"261","author":"Gibson","year":"1986","journal-title":"J Biol Chem"},{"key":"2023072207355871800_B5","doi-asserted-by":"crossref","first-page":"6932","DOI":"10.1128\/MCB.15.12.6932","article-title":"Bovine latent transforming growth factor \u03b2 1-binding protein 2: molecular cloning, identification of tissue isoforms, and immunolocalization to elastin-associated microfibrils","volume":"15","author":"Gibson","year":"1995","journal-title":"Mol Cell Biol"},{"key":"2023072207355871800_B6","doi-asserted-by":"crossref","first-page":"1096","DOI":"10.1074\/jbc.271.2.1096","article-title":"Further characterization of proteins associated with elastic fiber microfibrils including the molecular cloning of MAGP-2 (MP25)","volume":"271","author":"Gibson","year":"1996","journal-title":"J Biol Chem"},{"key":"2023072207355871800_B7","doi-asserted-by":"crossref","first-page":"6751","DOI":"10.1074\/jbc.270.12.6751","article-title":"Defective calcium binding to an epidermal growth factor-like domain of fibrillin-1 causes the Marfan syndrome","volume":"270","author":"Handford","year":"1995","journal-title":"J Biol Chem"},{"key":"2023072207355871800_B8","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/0022-2836(91)90385-J","article-title":"Morphology of sheet-like assemblies of pN-collagen, pC-collagen and procollagen studied by scanning transmission electron microscopy mass measurements","volume":"220","author":"Holmes","year":"1991","journal-title":"J Mol Biol"},{"key":"2023072207355871800_B9","doi-asserted-by":"crossref","first-page":"15758","DOI":"10.1016\/S0021-9258(18)82320-1","article-title":"Ehlers-Danlos syndrome type VIIB. Morphology of type I collagen fibrils formed in vivo and in vitro is determined by the conformation of the retained N-propeptide","volume":"268","author":"Holmes","year":"1993","journal-title":"J Biol Chem"},{"key":"2023072207355871800_B10","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1177\/39.4.2005373","article-title":"Extraction of extendible beaded structures and their identification as fibrillin-containing extracellular microfibrils","volume":"39","author":"Keene","year":"1991","journal-title":"J Histochem Cytochem"},{"key":"2023072207355871800_B11","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1016\/0014-5793(93)80829-J","article-title":"The role of calcium in the organisation of fibrillin microfibrils","volume":"336","author":"Kielty","year":"1993","journal-title":"FEBS (Fed Eur Biochem Soc) Lett"},{"key":"2023072207355871800_B12","doi-asserted-by":"crossref","first-page":"997","DOI":"10.1083\/jcb.124.6.997","article-title":"Abnormal fibrillin assembly by dermal fibroblasts from two patients with Marfan syndrome","volume":"124","author":"Kielty","year":"1994","journal-title":"J Cell Biol"},{"key":"2023072207355871800_B13","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1016\/1357-2725(95)00028-N","article-title":"Fibrillin-containing microfibrils: structure and function in health and disease","volume":"27","author":"Kielty","year":"1995","journal-title":"Int J Biochem Cell Biol"},{"key":"2023072207355871800_B14","doi-asserted-by":"crossref","first-page":"797","DOI":"10.1242\/jcs.99.4.797","article-title":"Isolation and ultrastructural analysis of microfibrillar structures from foetal elastic tissues","volume":"99","author":"Kielty","year":"1991","journal-title":"J Cell Sci"},{"key":"2023072207355871800_B15","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1136\/jmg.32.1.1","article-title":"Marfan syndrome: fibrillin expression and microfibrillar abnormalities in a family with predominant ocular defects","volume":"32","author":"Kielty","year":"1995","journal-title":"J Med Genet"},{"key":"2023072207355871800_B16","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/0014-5793(96)00423-1","article-title":"Fibrillin: evidence that chondroitin sulphate proteoglycans are components of microfibrils and associate with newly-synthesised monomers","volume":"386","author":"Kielty","year":"1996","journal-title":"FEBS (Fed Eur Biochem Soc) Lett"},{"key":"2023072207355871800_B17","doi-asserted-by":"crossref","first-page":"21381","DOI":"10.1016\/S0021-9258(19)30091-2","article-title":"Connective tissue microfibrils. Isolation and characterisation of three large pepsin-resistant domains of fibrillin","volume":"264","author":"Maddox","year":"1989","journal-title":"J Biol Chem"},{"key":"2023072207355871800_B18","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1113\/jphysiol.1997.sp021945","article-title":"Microfibrils provide non-linear elastic behavior in the abdominal artery of the lobster Homarus americanus.","volume":"499","author":"McConnell","year":"1997","journal-title":"J Physiol"},{"key":"2023072207355871800_B19"},{"key":"2023072207355871800_B20","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1016\/0304-3991(92)90022-C","article-title":"Factors influencing the precision of quantitative scanning transmission electron microscopy","volume":"46","author":"Muller","year":"1992","journal-title":"Ultramicroscopy"},{"key":"2023072207355871800_B21","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1093\/hmg\/2.7.961","article-title":"Genomic organisation of the sequence coding for the fibrillin gene product in Marfan syndrome","volume":"2","author":"Pereira","year":"1993","journal-title":"Hum Molec Genet"},{"key":"2023072207355871800_B22","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1006\/jmbi.1996.0237","article-title":"Fibrillin-1: organisation in microfibrils and structural properties","volume":"258","author":"Reinhardt","year":"1996","journal-title":"J Mol Biol"},{"key":"2023072207355871800_B23","doi-asserted-by":"crossref","first-page":"7368","DOI":"10.1074\/jbc.272.11.7368","article-title":"Calcium determines the shape of fibrillin","volume":"272","author":"Reinhardt","year":"1997","journal-title":"J Biol Chem"},{"key":"2023072207355871800_B24","doi-asserted-by":"crossref","first-page":"2499","DOI":"10.1083\/jcb.103.6.2499","article-title":"Fibrillin, a new 350-kD glycoprotein, is a component of extracellular microfibrils","volume":"103","author":"Sakai","year":"1986","journal-title":"J Cell Biol"},{"key":"2023072207355871800_B25","doi-asserted-by":"crossref","first-page":"14763","DOI":"10.1016\/S0021-9258(18)98752-1","article-title":"Purification and partial characterisation of fibrillin, a cysteine-rich structural component of connective tissue microfibrils","volume":"266","author":"Sakai","year":"1991","journal-title":"J Biol Chem"},{"key":"2023072207355871800_B26","doi-asserted-by":"crossref","first-page":"1063","DOI":"10.1016\/S1357-2725(97)00028-9","article-title":"Scanning transmission electron microscopy mass analysis of fibrillin-containing microfibrils from foetal elastic tissues","volume":"29","author":"Sherratt","year":"1997","journal-title":"Int J Biochem Cell Biol"},{"key":"2023072207355871800_B27","doi-asserted-by":"crossref","first-page":"875","DOI":"10.1177\/44.8.8756760","article-title":"Latent transforming growth factor-beta-1 and its binding protein are components of extracellular matrix microfibrils","volume":"44","author":"Taipale","year":"1996","journal-title":"J Histochem Cytochem"},{"key":"2023072207355871800_B28","doi-asserted-by":"crossref","first-page":"1817","DOI":"10.1242\/jeb.199.8.1817","article-title":"Morphology and biomechanics of the microfibrillar network of sea-cucumber dermis","volume":"199","author":"Thurmond","year":"1996","journal-title":"J Exp Biol"},{"key":"2023072207355871800_B29","doi-asserted-by":"crossref","first-page":"424","DOI":"10.1016\/S0014-5793(97)00950-2","article-title":"Fibrillin-rich microfibrils: an X-ray diffraction study of the fundamental axial periodicity","volume":"413","author":"Wess","year":"1997","journal-title":"FEBS (Fed Eur Biochem Soc) Lett"},{"key":"2023072207355871800_B30","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/S0021-9975(97)80072-2","article-title":"The structure of avian cartilage: a combined X-ray and biochemical analysis","volume":"116","author":"Wess","year":"1997","journal-title":"J Comp Pathol"},{"key":"2023072207355871800_B31","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1006\/jmbi.1997.1449","article-title":"Molecular packing of type I collagen in tendon","volume":"275","author":"Wess","year":"1998","journal-title":"J Mol Biol"}],"container-title":["The Journal of Cell Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/rupress.org\/jcb\/article-pdf\/141\/3\/829\/1490632\/15150.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/rupress.org\/jcb\/article-pdf\/141\/3\/829\/1490632\/15150.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,7,22]],"date-time":"2023-07-22T07:36:56Z","timestamp":1690011416000},"score":1,"resource":{"primary":{"URL":"https:\/\/rupress.org\/jcb\/article\/141\/3\/829\/1004\/Calcium-Determines-the-Supramolecular-Organization"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1998,5,4]]},"references-count":31,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1998,5,4]]}},"URL":"https:\/\/doi.org\/10.1083\/jcb.141.3.829","relation":{},"ISSN":["0021-9525","1540-8140"],"issn-type":[{"value":"0021-9525","type":"print"},{"value":"1540-8140","type":"electronic"}],"subject":[],"published":{"date-parts":[[1998,5,4]]}}}