A molecular ensemble in the rER for procollagen maturation

Biochimica et Biophysica Acta - Molecular Cell Research

Volumn 1833, Issue 11, 2013, Pages 2479-2491

  Ishikawa, Yoshihiro ^a   Bächinger, Hans Peter ^b  

^a SHRINERS HOSPITAL FOR CHILDREN   (United States)

^b OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

Author keywords

Biosynthesis; Collagen; Endoplasmic reticulum; Extracellular matrix; Molecular chaperone; Posttranslational modification

Indexed keywords

CALCIUM; COLLAGEN TYPE 11; COLLAGEN TYPE 2; COLLAGEN TYPE 3; COLLAGEN TYPE 5; COLLAGEN TYPE 7; PROCOLLAGEN;

BASEMENT MEMBRANE; BONE DEVELOPMENT; BONE FRAGILITY; CALCIUM BINDING; CARBOXY TERMINAL SEQUENCE; CHEMICAL STRUCTURE; CHONDRODYSPLASIA; CYTOPLASM; EXTRACELLULAR MATRIX; GENE MUTATION; GLYCOSYLATION; HOMEOSTASIS; HUMAN; HYDROXYLATION; ISOMERIZATION; NONHUMAN; OSTEOGENESIS IMPERFECTA; OSTEOPOROSIS; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROCESSING; PROTEIN SECRETION; PROTEIN SYNTHESIS; RECEPTOR BINDING; REVIEW; TISSUE DISTRIBUTION; TRIPLE HELIX;

BIOSYNTHESIS; COLLAGEN; ENDOPLASMIC RETICULUM; EXTRACELLULAR MATRIX; MOLECULAR CHAPERONE; POSTTRANSLATIONAL MODIFICATION;

ANIMALS; ENDOPLASMIC RETICULUM, ROUGH; EXTRACELLULAR MATRIX PROTEINS; HUMANS; MOLECULAR CHAPERONES; PROCOLLAGEN;

EID: 84880588489     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2013.04.008     Document Type: Review

References (238)

1. Bächinger H.P., Mizuno K., Vranka J., Boudko S. Collagen formation and structure. Comprehensive Natural Products II: Chemistry and Biology 2010, 469-530. Amino Acids, Peptides and Proteins Elsevier Ltd. L. Mander, H.-W. Liu (Eds.).
2. Bateman J.F., Boot-Handford R.P., Lamande S.R. Genetic diseases of connective tissues: cellular and extracellular effects of ECM mutations. Nat. Rev. Genet. 2009, 10:173-183.
3. Starborg T., Lu Y., Kadler K.E., Holmes D.F. Electron microscopy of collagen fibril structure in vitro and in vivo including three-dimensional reconstruction. Methods Cell Biol. 2008, 88:319-345.
4. Bächinger H.P., Engel J. The Thermodynamics and Kinetics of Collagen Folding, Protein Folding Handbook 2008, 1059-1110. Wiley-VCH Verlag GmbH.
5. Morris N.P., Fessler L.I., Weinstock A., Fessler J.H. Procollagen assembly and secretion in embryonic chick bone. J. Biol. Chem. 1975, 250:5719-5726.
6. Bruckner P., Eikenberry E.F., Prockop D.J. Formation of the triple helix of type I procollagen in cellulo. A kinetic model based on cis-trans isomerization of peptide bonds. Eur. J. Biochem. 1981, 118:607-613.
7. Bächinger H.P., Morris N.P., Davis J.M. Thermal stability and folding of the collagen triple helix and the effects of mutations in osteogenesis imperfecta on the triple helix of type I collagen. Am. J. Med. Genet. 1993, 45:152-162.
8. Vranka J.A., Pokidysheva E., Hayashi L., Zientek K., Mizuno K., Ishikawa Y., Maddox K., Tufa S., Keene D.R., Klein R., Bächinger H.P. Prolyl 3-hydroxylase 1 null mice display abnormalities in fibrillar collagen-rich tissues such as tendons, skin, and bones. J. Biol. Chem. 2010, 285:17253-17262.
9. Byers P.H., Cole W.G. Osteogenesis imperfecta. Connective Tissue and Heritable Disorders 2002, 285-430. Wiley-Liss, New York. Second Edition. P.M. Royce, B. Stinmann (Eds.).
10. Rauch F., Glorieux F.H. Osteogenesis imperfecta. Lancet 2004, 363:1377-1385.
11. Sillence D.O., Rimoin D.L. Classification of osteogenesis imperfect. Lancet 1978, 1:1041-1042.
12. Marini J.C., Forlino A., Cabral W.A., Barnes A.M., San Antonio J.D., Milgrom S., Hyland J.C., Korkko J., Prockop D.J., De Paepe A., Coucke P., Symoens S., Glorieux F.H., Roughley P.J., Lund A.M., Kuurila-Svahn K., Hartikka H., Cohn D.H., Krakow D., Mottes M., Schwarze U., Chen D., Yang K., Kuslich C., Troendle J., Dalgleish R., Byers P.H. Consortium for osteogenesis imperfecta mutations in the helical domain of type I collagen: regions rich in lethal mutations align with collagen binding sites for integrins and proteoglycans. Hum. Mutat. 2007, 28:209-221.
13. Pihlajaniemi T., Dickson L.A., Pope F.M., Korhonen V.R., Nicholls A., Prockop D.J., Myers J.C. Osteogenesis imperfecta: cloning of a pro-alpha 2(I) collagen gene with a frameshift mutation. J. Biol. Chem. 1984, 259:12941-12944.
14. Willing M.C., Deschenes S.P., Scott D.A., Byers P.H., Slayton R.L., Pitts S.H., Arikat H., Roberts E.J. Osteogenesis imperfecta type I: molecular heterogeneity for COL1A1 null alleles of type I collagen. Am. J. Hum. Genet. 1994, 55:638-647.
15. Morello R., Bertin T.K., Chen Y., Hicks J., Tonachini L., Monticone M., Castagnola P., Rauch F., Glorieux F.H., Vranka J., Bächinger H.P., Pace J.M., Schwarze U., Byers P.H., Weis M., Fernandes R.J., Eyre D.R., Yao Z., Boyce B.F., Lee B. CRTAP is required for prolyl 3-hydroxylation and mutations cause recessive osteogenesis imperfecta. Cell 2006, 127:291-304.
16. Vranka J.A., Sakai L.Y., Bächinger H.P. Prolyl 3-hydroxylase 1, enzyme characterization and identification of a novel family of enzymes. J. Biol. Chem. 2004, 279:23615-23621.
17. Ishikawa Y., Wirz J., Vranka J.A., Nagata K., Bächinger H.P. Biochemical characterization of the prolyl 3-hydroxylase 1·cartilage-associated protein·cyclophilin B complex. J. Biol. Chem. 2009, 284:17641-17647.
18. Barnes A.M., Carter E.M., Cabral W.A., Weis M., Chang W., Makareeva E., Leikin S., Rotimi C.N., Eyre D.R., Raggio C.L., Marini J.C. Lack of cyclophilin B in osteogenesis imperfecta with normal collagen folding. N. Engl. J. Med. 2010, 362:521-528.
19. Cabral W.A., Chang W., Barnes A.M., Weis M., Scott M.A., Leikin S., Makareeva E., Kuznetsova N.V., Rosenbaum K.N., Tifft C.J., Bulas D.I., Kozma C., Smith P.A., Eyre D.R., Marini J.C. Prolyl 3-hydroxylase 1 deficiency causes a recessive metabolic bone disorder resembling lethal/severe osteogenesis imperfecta. Nat. Genet. 2007, 39:359-365.
20. Baldridge D., Schwarze U., Morello R., Lennington J., Bertin T.K., Pace J.M., Pepin M.G., Weis M., Eyre D.R., Walsh J., Lambert D., Green A., Robinson H., Michelson M., Houge G., Lindman C., Martin J., Ward J., Lemyre E., Mitchell J.J., Krakow D., Rimoin D.L., Cohn D.H., Byers P.H., Lee B. CRTAP and LEPRE1 mutations in recessive osteogenesis imperfecta. Hum. Mutat. 2008, 29:1435-1442.
21. Choi J.W., Sutor S.L., Lindquist L., Evans G.L., Madden B.J., Bergen H.R., Hefferan T.E., Yaszemski M.J., Bram R.J. Severe osteogenesis imperfecta in cyclophilin B-deficient mice. PLoS Genet. 2009, 5:e1000750.
22. Willaert A., Malfait F., Symoens S., Gevaert K., Kayserili H., Megarbane A., Mortier G., Leroy J.G., Coucke P.J., De Paepe A. Recessive osteogenesis imperfecta caused by LEPRE1 mutations: clinical documentation and identification of the splice form responsible for prolyl 3-hydroxylation. J. Med. Genet. 2009, 46:233-241.
23. Van Dijk F.S., Nesbitt I.M., Nikkels P.G., Dalton A., Bongers E.M., van de Kamp J.M., Hilhorst-Hofstee Y., Den Hollander N.S., Lachmeijer A.M., Marcelis C.L., Tan-Sindhunata G.M., van Rijn R.R., Meijers-Heijboer H., Cobben J.M., Pals G. CRTAP mutations in lethal and severe osteogenesis imperfecta: the importance of combining biochemical and molecular genetic analysis. Eur. J. Hum. Genet. 2009, 17:1560-1569.
24. Van Dijk F.S., Nesbitt I.M., Zwikstra E.H., Nikkels P.G., Piersma S.R., Fratantoni S.A., Jimenez C.R., Huizer M., Morsman A.C., Cobben J.M., van Roij M.H., Elting M.W., Verbeke J.I., Wijnaendts L.C., Shaw N.J., Hogler W., McKeown C., Sistermans E.A., Dalton A., Meijers-Heijboer H., Pals G. PPIB mutations cause severe osteogenesis imperfecta. Am. J. Hum. Genet. 2009, 85:521-527.
25. Marini J.C., Cabral W.A., Barnes A.M. Null mutations in LEPRE1 and CRTAP cause severe recessive osteogenesis imperfecta. Cell Tissue Res. 2010, 339:59-70.
26. Pyott S.M., Schwarze U., Christiansen H.E., Pepin M.G., Leistritz D.F., Dineen R., Harris C., Burton B.K., Angle B., Kim K., Sussman M.D., Weis M., Eyre D.R., Russell D.W., McCarthy K.J., Steiner R.D., Byers P.H. Mutations in PPIB (cyclophilin B) delay type I procollagen chain association and result in perinatal lethal to moderate osteogenesis imperfecta phenotypes. Hum. Mol. Genet. 2011, 20:1595-1609.
27. Valli M., Barnes A., Gallanti A., Cabral W., Viglio S., Weis M., Makareeva E., Eyre D., Leikin S., Antoniazzi F., Marini J., Mottes M. Deficiency of CRTAP in non-lethal recessive osteogenesis imperfecta reduces collagen deposition into matrix. Clin. Genet. 2012, 82:453-459.
28. Takagi M., Ishii T., Barnes A.M., Weis M., Amano N., Tanaka M., Fukuzawa R., Nishimura G., Eyre D.R., Marini J.C., Hasegawa T. A novel mutation in LEPRE1 that eliminates only the KDEL ER-retrieval sequence causes non-lethal osteogenesis imperfecta. PLoS One 2012, 7:e36809.
29. Drogemuller C., Becker D., Brunner A., Haase B., Kircher P., Seeliger F., Fehr M., Baumann U., Lindblad-Toh K., Leeb T. A missense mutation in the SERPINH1 gene in Dachshunds with osteogenesis imperfecta. PLoS Genet. 2009, 5:e1000579.
30. Christiansen H.E., Schwarze U., Pyott S.M., AlSwaid A., Al Balwi M., Alrasheed S., Pepin M.G., Weis M.A., Eyre D.R., Byers P.H. Homozygosity for a missense mutation in SERPINH1, which encodes the collagen chaperone protein HSP47, results in severe recessive osteogenesis imperfecta. Am. J. Hum. Genet. 2010, 86:389-398.
31. Alanay Y., Avaygan H., Camacho N., Utine G.E., Boduroglu K., Aktas D., Alikasifoglu M., Tuncbilek E., Orhan D., Bakar F.T., Zabel B., Superti-Furga A., Bruckner-Tuderman L., Curry C.J., Pyott S., Byers P.H., Eyre D.R., Baldridge D., Lee B., Merrill A.E., Davis E.C., Cohn D.H., Akarsu N., Krakow D. Mutations in the gene encoding the RER protein FKBP65 cause autosomal-recessive osteogenesis imperfecta. Am. J. Hum. Genet. 2010, 86:551-559.
32. Kelley B.P., Malfait F., Bonafe L., Baldridge D., Homan E., Symoens S., Willaert A., Elcioglu N., Van Maldergem L., Verellen-Dumoulin C., Gillerot Y., Napierala D., Krakow D., Beighton P., Superti-Furga A., De Paepe A., Lee B. Mutations in FKBP10 cause recessive osteogenesis imperfecta and Bruck syndrome. J. Bone Miner. Res. 2011, 26:666-672.
33. Shaheen R., Al-Owain M., Faqeih E., Al-Hashmi N., Awaji A., Al-Zayed Z., Alkuraya F.S. Mutations in FKBP10 cause both Bruck syndrome and isolated osteogenesis imperfecta in humans. Am. J. Med. Genet. A 2011, 155A:1448-1452.
34. Zhang Z.L., Zhang H., Ke Y.H., Yue H., Xiao W.J., Yu J.B., Gu J.M., Hu W.W., Wang C., He J.W., Fu W.Z. The identification of novel mutations in COL1A1, COL1A2, and LEPRE1 genes in Chinese patients with osteogenesis imperfecta. J. Bone Miner. Metab. 2012, 30:69-77.
35. Venturi G., Monti E., Dalle Carbonare L., Corradi M., Gandini A., Valenti M.T., Boner A., Antoniazzi F. A novel splicing mutation in FKBP10 causing osteogenesis imperfecta with a possible mineralization defect. Bone 2012, 50:343-349.
36. Barnes A.M., Cabral W.A., Weis M., Makareeva E., Mertz E.L., Leikin S., Eyre D., Trujillo C., Marini J.C. Absence of FKBP10 in recessive type XI osteogenesis imperfecta leads to diminished collagen cross-linking and reduced collagen deposition in extracellular matrix. Hum. Mutat. 2012, 33:1589-1598.
37. Setijowati E.D., van Dijk F.S., Cobben J.M., van Rijn R.R., Sistermans E.A., Faradz S.M., Kawiyana S., Pals G. A novel homozygous 5 bp deletion in FKBP10 causes clinically Bruck syndrome in an Indonesian patient. Eur. J. Med. Genet. 2012, 55:17-21.
38. Steinlein O.K., Aichinger E., Trucks H., Sander T. Mutations in FKBP10 can cause a severe form of isolated Osteogenesis imperfecta. BMC Med. Genet. 2011, 12:152.
39. Schwarze U., Cundy T., Pyott S.M., Christiansen H.E., Hegde M.R., Bank R.A., Pals G., Ankala A., Conneely K., Seaver L., Yandow S.M., Raney E., Babovic-Vuksanovic D., Stoler J., Ben-Neriah Z., Segel R., Lieberman S., Siderius L., Al-Aqeel A., Hannibal M., Hudgins L., McPherson E., Clemens M., Sussman M.D., Steiner R.D., Mahan J., Smith R., Anyane-Yeboa K., Wynn J., Chong K., Uster T., Aftimos S., Sutton V.R., Davis E.C., Kim L.S., Weis M.A., Eyre D., Byers P.H. Mutations in FKBP10, which result in Bruck syndrome and recessive forms of osteogenesis imperfecta, inhibit the hydroxylation of telopeptide lysines in bone collagen. Hum. Mol. Genet. 2013.
40. Hyry M., Lantto J., Myllyharju J. Missense mutations that cause Bruck syndrome affect enzymatic activity, folding, and oligomerization of lysyl hydroxylase 2. J. Biol. Chem. 2009, 284:30917-30924.
41. Puig-Hervas M.T., Temtamy S., Aglan M., Valencia M., Martinez-Glez V., Ballesta-Martinez M.J., Lopez-Gonzalez V., Ashour A.M., Amr K., Pulido V., Guillen-Navarro E., Lapunzina P., Caparros-Martin J.A., Ruiz-Perez V.L. Mutations in PLOD2 cause autosomal-recessive connective tissue disorders within the Bruck syndrome-Osteogenesis imperfecta phenotypic spectrum. Hum. Mutat. 2012, 33:1444-1449.
42. Ishikawa Y., Vranka J.A., Boudko S.P., Pokidysheva E., Mizuno K., Zientek K., Keene D.R., Rashmir-Raven A.M., Nagata K., Winand N.J., Bächinger H.P. Mutation in cyclophilin B that causes hyperelastosis cutis in American Quarter Horse does not affect peptidylprolyl cis-trans isomerase activity but shows altered cyclophilin B-protein interactions and affects collagen folding. J. Biol. Chem. 2012, 287:22253-22265.
43. Braakman I., Bulleid N.J. Protein folding and modification in the mammalian endoplasmic reticulum. Annu. Rev. Biochem. 2011, 80:71-99.
44. Makareeva E., Aviles N.A., Leikin S. Chaperoning osteogenesis: new protein-folding disease paradigms. Trends Cell Biol. 2010, 21:168-176.
45. Forlino A., Cabral W.A., Barnes A.M., Marini J.C. New perspectives on osteogenesis imperfecta. Nat. Rev. Endocrinol. 2011, 7:540-557.
46. Myllyla R., Kuutti-Savolainen E.R., Kivirikko K.I. The role of ascorbate in the prolyl hydroxylase reaction. Biochem. Biophys. Res. Commun. 1978, 83:441-448.
47. Nietfeld J.J., Kemp A. The function of ascorbate with respect to prolyl 4-hydroxylase activity. Biochim. Biophys. Acta 1981, 657:159-167.
48. Gorres K.L., Raines R.T. Prolyl 4-hydroxylase. Crit. Rev. Biochem. Mol. Biol. 2010, 45:106-124.
49. Berg R.A., Prockop D.J. The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen. Biochem. Biophys. Res. Commun. 1973, 52:115-120.
50. Jimenez S., Harsch M., Rosenbloom J. Hydroxyproline stabilizes the triple helix of chick tendon collagen. Biochem. Biophys. Res. Commun. 1973, 52:106-114.
51. Rosenbloom J., Harsch M., Jimenez S. Hydroxyproline content determines the denaturation temperature of chick tendon collagen. Arch. Biochem. Biophys. 1973, 158:478-484.
52. Myllyharju J. Prolyl 4-hydroxylases, key enzymes in the synthesis of collagens and regulation of the response to hypoxia, and their roles as treatment targets. Ann. Med. 2008, 40:402-417.
53. Kresina T.F., Miller E.J. Isolation and characterization of basement membrane collagen from human placental tissue. Evidence for the presence of two genetically distinct collagen chains. Biochemistry 1979, 18:3089-3097.
54. Kefalides N.A. Basement membranes: structural and biosynthetic considerations. J. Invest. Dermatol. 1975, 65:85-92.
55. Gryder R.M., Lamon M., Adams E. Sequence position of 3-hydroxyproline in basement membrane collagen. Isolation of glycyl-3-hydroxyprolyl-4-hydroxyproline from swine kidney. J. Biol. Chem. 1975, 250:2470-2474.
56. Tiainen P., Pasanen A., Sormunen R., Myllyharju J. Characterization of recombinant human prolyl 3-hydroxylase isoenzyme 2, an enzyme modifying the basement membrane collagen IV. J. Biol. Chem. 2008, 283:19432-19439.
57. Van der Slot A.J., Zuurmond A.M., Bardoel A.F., Wijmenga C., Pruijs H.E., Sillence D.O., Brinckmann J., Abraham D.J., Black C.M., Verzijl N., DeGroot J., Hanemaaijer R., TeKoppele J.M., Huizinga T.W., Bank R.A. Identification of PLOD2 as telopeptide lysyl hydroxylase, an important enzyme in fibrosis. J. Biol. Chem. 2003, 278:40967-40972.
58. Takaluoma K., Lantto J., Myllyharju J. Lysyl hydroxylase 2 is a specific telopeptide hydroxylase, while all three isoenzymes hydroxylate collagenous sequences. Matrix Biol. 2007, 26:396-403.
59. Yamauchi M., Sricholpech M. Lysine post-translational modifications of collagen. Essays Biochem. 2012, 52:113-133.
60. Myllyharju J. Intracellular Post-Translational Modifications of Collagens, Collagen 2005, 247:115-147. Springer, Berlin Heidelberg.
61. Helaakoski T., Vuori K., Myllyla R., Kivirikko K.I., Pihlajaniemi T. Molecular cloning of the alpha-subunit of human prolyl 4-hydroxylase: the complete cDNA-derived amino acid sequence and evidence for alternative splicing of RNA transcripts. Proc. Natl. Acad. Sci. U.S.A. 1989, 86:4392-4396.
62. John D.C., Grant M.E., Bulleid N.J. Cell-free synthesis and assembly of prolyl 4-hydroxylase: the role of the beta-subunit (PDI) in preventing misfolding and aggregation of the alpha-subunit. EMBO J. 1993, 12:1587-1595.
63. Walmsley A.R., Batten M.R., Lad U., Bulleid N.J. Intracellular retention of procollagen within the endoplasmic reticulum is mediated by prolyl 4-hydroxylase. J. Biol. Chem. 1999, 274:14884-14892.
64. Annunen P., Helaakoski T., Myllyharju J., Veijola J., Pihlajaniemi T., Kivirikko K.I. Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) and characterization of the type II enzyme tetramer. The alpha(I) and alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer. J. Biol. Chem. 1997, 272:17342-17348.
65. Annunen P., Autio-Harmainen H., Kivirikko K.I. The novel type II prolyl 4-hydroxylase is the main enzyme form in chondrocytes and capillary endothelial cells, whereas the type I enzyme predominates in most cells. J. Biol. Chem. 1998, 273:5989-5992.
66. Holster T., Pakkanen O., Soininen R., Sormunen R., Nokelainen M., Kivirikko K.I., Myllyharju J. Loss of assembly of the main basement membrane collagen, type IV, but not fibril-forming collagens and embryonic death in collagen prolyl 4-hydroxylase I null mice. J. Biol. Chem. 2007, 282:2512-2519.
67. Nokelainen M., Nissi R., Kukkola L., Helaakoski T., Myllyharju J. Characterization of the human and mouse genes for the alpha subunit of type II prolyl 4-hydroxylase. Identification of a previously unknown alternatively spliced exon and its expression in various tissues. Eur. J. Biochem. 2001, 268:5300-5309.
68. Kukkola L., Hieta R., Kivirikko K.I., Myllyharju J. Identification and characterization of a third human, rat, and mouse collagen prolyl 4-hydroxylase isoenzyme. J. Biol. Chem. 2003, 278:47685-47693.
69. Vranka J., Stadler H.S., Bächinger H.P. Expression of prolyl 3-hydroxylase genes in embryonic and adult mouse tissues. Cell Struct. Funct. 2009, 34:97-104.
70. Mordechai S., Gradstein L., Pasanen A., Ofir R., El Amour K., Levy J., Belfair N., Lifshitz T., Joshua S., Narkis G., Elbedour K., Myllyharju J., Birk O.S. High myopia caused by a mutation in LEPREL1, encoding prolyl 3-hydroxylase 2. Am. J. Hum. Genet. 2011, 89:438-445.
71. Shah R., Smith P., Purdie C., Quinlan P., Baker L., Aman P., Thompson A.M., Crook T. The prolyl 3-hydroxylases P3H2 and P3H3 are novel targets for epigenetic silencing in breast cancer. Br. J. Cancer 2009, 100:1687-1696.
72. Yeowell H.N., Walker L.C. Tissue specificity of a new splice form of the human lysyl hydroxylase 2 gene. Matrix Biol. 1999, 18:179-187.
73. Rautavuoma K., Takaluoma K., Passoja K., Pirskanen A., Kvist A.P., Kivirikko K.I., Myllyharju J. Characterization of three fragments that constitute the monomers of the human lysyl hydroxylase isoenzymes 1-3. The 30-kDa N-terminal fragment is not required for lysyl hydroxylase activity. J. Biol. Chem. 2002, 277:23084-23091.
74. Kivirikko K.I., Myllyla R. Posttranslational enzymes in the biosynthesis of collagen: intracellular enzymes. Methods Enzymol. 1982, 82(Pt A):245-304.
75. Heikkinen J., Risteli M., Lampela O., Alavesa P., Karppinen M., Juffer A.H., Myllylä R. Dimerization of human lysyl hydroxylase 3 (LH3) is mediated by the amino acids 541-547. Matrix Biol. 2011, 30:27-33.
76. Suokas M., Lampela O., Juffer A.H., Myllyla R., Kellokumpu S. Retrieval-independent localization of lysyl hydroxylase in the endoplasmic reticulum via a peptide fold in its iron-binding domain. Biochem. J. 2003, 370:913-920.
77. Suokas M., Myllyla R., Kellokumpu S. A single C-terminal peptide segment mediates both membrane association and localization of lysyl hydroxylase in the endoplasmic reticulum. J. Biol. Chem. 2000, 275:17863-17868.
78. Sricholpech M., Perdivara I., Nagaoka H., Yokoyama M., Tomer K.B., Yamauchi M. Lysyl hydroxylase 3 glucosylates galactosylhydroxylysine residues in type I collagen in osteoblast culture. J. Biol. Chem. 2012, 286:8846-8856.
79. Wang C., Kovanen V., Raudasoja P., Eskelinen S., Pospiech H., Myllyla R. The glycosyltransferase activities of lysyl hydroxylase 3 (LH3) in the extracellular space are important for cell growth and viability. J. Cell. Mol. Med. 2009, 13:508-521.
80. Wang C., Luosujärvi H., Heikkinen J., Risteli M., Uitto L., Myllylä R. The third activity for lysyl hydroxylase 3: galactosylation of hydroxylysyl residues in collagens in vitro. Matrix Biol. 2002, 21:559-566.
81. Ruotsalainen H., Sipila L., Vapola M., Sormunen R., Salo A.M., Uitto L., Mercer D.K., Robins S.P., Risteli M., Aszodi A., Fassler R., Myllyla R. Glycosylation catalyzed by lysyl hydroxylase 3 is essential for basement membranes. J. Cell Sci. 2006, 119:625-635.
82. Heikkinen J., Risteli M., Wang C., Latvala J., Rossi M., Valtavaara M., Myllyla R. Lysyl hydroxylase 3 is a multifunctional protein possessing collagen glucosyltransferase activity. J. Biol. Chem. 2000, 275:36158-36163.
83. Schegg B., Hulsmeier A.J., Rutschmann C., Maag C., Hennet T. Core glycosylation of collagen is initiated by two beta(1-O)galactosyltransferases. Mol. Cell. Biol. 2009, 29:943-952.
84. Salo A.M., Sipilä L., Sormunen R., Ruotsalainen H., Vainio S., Myllylä R. The lysyl hydroxylase isoforms are widely expressed during mouse embryogenesis, but obtain tissue- and cell-specific patterns in the adult. Matrix Biol. 2006, 25:475-483.
85. Valtavaara M., Szpirer C., Szpirer J., Myllyla R. Primary structure, tissue distribution, and chromosomal localization of a novel isoform of lysyl hydroxylase (lysyl hydroxylase 3). J. Biol. Chem. 1998, 273:12881-12886.
86. Ruotsalainen H., Sipila L., Kerkela E., Pospiech H., Myllyla R. Characterization of cDNAs for mouse lysyl hydroxylase 1, 2 and 3, their phylogenetic analysis and tissue-specific expression in the mouse. Matrix Biol. 1999, 18:325-329.
87. Takaluoma K., Hyry M., Lantto J., Sormunen R., Bank R.A., Kivirikko K.I., Myllyharju J., Soininen R. Tissue-specific changes in the hydroxylysine content and cross-links of collagens and alterations in fibril morphology in lysyl hydroxylase 1 knock-out mice. J. Biol. Chem. 2007, 282:6588-6596.
88. Rautavuoma K., Takaluoma K., Sormunen R., Myllyharju J., Kivirikko K.I., Soininen R. Premature aggregation of type IV collagen and early lethality in lysyl hydroxylase 3 null mice. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:14120-14125.
89. Yapicioglu H., Ozcan K., Arikan O., Satar M., Narli N., Ozbsek M.H. Bruck syndrome: osteogenesis imperfecta and arthrogryposis multiplex congenita. Ann. Trop. Paediatr. 2009, 29:159-162.
90. Ha-Vinh R., Alanay Y., Bank R.A., Campos-Xavier A.B., Zankl A., Superti-Furga A., Bonafe L. Phenotypic and molecular characterization of Bruck syndrome (osteogenesis imperfecta with contractures of the large joints) caused by a recessive mutation in PLOD2. Am. J. Med. Genet. A 2004, 131:115-120.
91. Liefhebber J.M., Punt S., Spaan W.J., van Leeuwen H.C. The human collagen beta(1-O)galactosyltransferase, GLT25D1, is a soluble endoplasmic reticulum localized protein. BMC Cell Biol. 2010, 11:33.
92. Perrin-Tricaud C., Rutschmann C., Hennet T. Identification of domains and amino acids essential to the collagen galactosyltransferase activity of GLT25D1. PLoS One 2011, 6:e29390.
93. Lamande S.R., Chessler S.D., Golub S.B., Byers P.H., Chan D., Cole W.G., Sillence D.O., Bateman J.F. Endoplasmic reticulum-mediated quality control of type I collagen production by cells from osteogenesis imperfecta patients with mutations in the pro alpha 1 (I) chain carboxyl-terminal propeptide which impair subunit assembly. J. Biol. Chem. 1995, 270:8642-8649.
94. Pace J.M., Kuslich C.D., Willing M.C., Byers P.H. Disruption of one intra-chain disulphide bond in the carboxyl-terminal propeptide of the proalpha1(I) chain of type I procollagen permits slow assembly and secretion of overmodified, but stable procollagen trimers and results in mild osteogenesis imperfecta. J. Med. Genet. 2001, 38:443-449.
95. Wilson R., Lees J.F., Bulleid N.J. Protein disulfide isomerase acts as a molecular chaperone during the assembly of procollagen. J. Biol. Chem. 1998, 273:9637-9643.
96. Bottomley M.J., Batten M.R., Lumb R.A., Bulleid N.J. Quality control in the endoplasmic reticulum: PDI mediates the ER retention of unassembled procollagen C-propeptides. Curr. Biol. 2001, 11:1114-1118.
97. Koide T., Nagata K. Collagen Biosynthesis 2005, 247:85-114. Springer Berlin/ Heidelberg.
98. Beck K., Boswell B.A., Ridgway C.C., Bächinger H.P. Triple helix formation of procollagen type I can occur at the rough endoplasmic reticulum membrane. J. Biol. Chem. 1996, 271:21566-21573.
99. Boudko S.P., Engel J., Bächinger H.P. The crucial role of trimerization domains in collagen folding. Int. J. Biochem. Cell Biol. 2012, 44:21-32.
100. Bourhis J.M., Mariano N., Zhao Y., Harlos K., Exposito J.Y., Jones E.Y., Moali C., Aghajari N., Hulmes D.J. Structural basis of fibrillar collagen trimerization and related genetic disorders. Nat. Struct. Mol. Biol. 2012, 19:1031-1036.
101. Ellgaard L., Ruddock L.W. The human protein disulphide isomerase family: substrate interactions and functional properties. EMBO Rep. 2005, 6:28-32.
102. Jessop C.E., Watkins R.H., Simmons J.J., Tasab M., Bulleid N.J. Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins. J. Cell Sci. 2009, 122:4287-4295.
103. Bernard M.P., Myers J.C., Chu M.L., Ramirez F., Eikenberry E.F., Prockop D.J. Structure of a cDNA for the pro alpha 2 chain of human type I procollagen. Comparison with chick cDNA for pro alpha 2(I) identifies structurally conserved features of the protein and the gene. Biochemistry 1983, 22:1139-1145.
104. Bernard M.P., Chu M.L., Myers J.C., Ramirez F., Eikenberry E.F., Prockop D.J. Nucleotide sequences of complementary deoxyribonucleic acids for the pro alpha 1 chain of human type I procollagen. Statistical evaluation of structures that are conserved during evolution. Biochemistry 1983, 22:5213-5223.
105. Lamande S.R., Bateman J.F. The type I collagen pro alpha 1(I) COOH-terminal propeptide N-linked oligosaccharide. Functional analysis by site-directed mutagenesis. J. Biol. Chem. 1995, 270:17858-17865.
106. Bächinger H.P., Bruckner P., Timpl R., Engel J. The role of cis-trans isomerization of peptide bonds in the coil leads to and comes from triple helix conversion of collagen. Eur. J. Biochem. 1978, 90:605-613.
107. Bächinger H.P., Bruckner P., Timpl R., Prockop D.J., Engel J. Folding mechanism of the triple helix in type-III collagen and type-III pN-collagen. Role of disulfide bridges and peptide bond isomerization. Eur. J. Biochem. 1980, 106:619-632.
108. 13C NMR: application to collagen. Proc. Natl. Acad. Sci. U.S.A. 1984, 81:4800-4803.
109. Bruckner P., Eikenberry E.F. Formation of the triple helix of type I procollagen in cellulo. Temperature-dependent kinetics support a model based on cis in equilibrium trans isomerization of peptide bonds. Eur. J. Biochem. 1984, 140:391-395.
110. Bächinger H.P. The influence of peptidyl-prolyl cis-trans isomerase on the in vitro folding of type III collagen. J. Biol. Chem. 1987, 262:17144-17148.
111. Steinmann B., Bruckner P., Superti-Furga A. Cyclosporin A slows collagen triple-helix formation in vivo: indirect evidence for a physiologic role of peptidyl-prolyl cis-trans-isomerase. J. Biol. Chem. 1991, 266:1299-1303.
112. Rulten S.L., Kinloch R.A., Tateossian H., Robinson C., Gettins L., Kay J.E. The human FK506-binding proteins: characterization of human FKBP19. Mamm. Genome 2006, 17:322-331.
113. Kozlov G., Bastos-Aristizabal S., Maattanen P., Rosenauer A., Zheng F., Killikelly A., Trempe J.F., Thomas D.Y., Gehring K. Structural basis of cyclophilin B binding by the calnexin/calreticulin P-domain. J. Biol. Chem. 2010, 285:35551-35557.
114. Smith T., Ferreira L.R., Hebert C., Norris K., Sauk J.J. Hsp47 and cyclophilin B traverse the endoplasmic reticulum with procollagen into pre-Golgi intermediate vesicles. A role for Hsp47 and cyclophilin B in the export of procollagen from the endoplasmic reticulum. J. Biol. Chem. 1995, 270:18323-18328.
115. Horibe T., Yosho C., Okada S., Tsukamoto M., Nagai H., Hagiwara Y., Tujimoto Y., Kikuchi M. The chaperone activity of protein disulfide isomerase is affected by cyclophilin B and cyclosporin A in vitro. J. Biochem. 2002, 132:401-407.
116. Patterson C.E., Schaub T., Coleman E.J., Davis E.C. Developmental regulation of FKBP65. An ER-localized extracellular matrix binding-protein. Mol. Biol. Cell 2000, 11:3925-3935.
117. Zeng B., MacDonald J.R., Bann J.G., Beck K., Gambee J.E., Boswell B.A., Bächinger H.P. Chicken FK506-binding protein, FKBP65, a member of the FKBP family of peptidylprolyl cis-trans isomerases, is only partially inhibited by FK506. Biochem. J. 1998, 330(Pt 1):109-114.
118. Ishikawa Y., Vranka J., Wirz J., Nagata K., Bächinger H.P. The rough endoplasmic reticulum-resident FK506-binding protein FKBP65 is a molecular chaperone that interacts with collagens. J. Biol. Chem. 2008, 283:31584-31590.
119. Shaheen R., Al-Owain M., Sakati N., Alzayed Z.S., Alkuraya F.S. FKBP10 and Bruck syndrome: phenotypic heterogeneity or call for reclassification?. Am. J. Hum. Genet. 2010, 87:306-307. author reply 308.
120. Baumann M., Giunta C., Krabichler B., Ruschendorf F., Zoppi N., Colombi M., Bittner R.E., Quijano-Roy S., Muntoni F., Cirak S., Schreiber G., Zou Y., Hu Y., Romero N.B., Carlier R.Y., Amberger A., Deutschmann A., Straub V., Rohrbach M., Steinmann B., Rostasy K., Karall D., Bonnemann C.G., Zschocke J., Fauth C. Mutations in FKBP14 cause a variant of Ehlers-Danlos syndrome with progressive kyphoscoliosis, myopathy, and hearing loss. Am. J. Hum. Genet. 2012, 90:201-216.
121. Quijano-Roy S., Avila-Smirnow D., Carlier R.Y. Whole body muscle MRI protocol: pattern recognition in early onset NM disorders. Neuromuscul. Disord. 2012, 22(Suppl. 2):S68-84.
122. Steinmann B., Eyre D.R., Shao P. Urinary pyridinoline cross-links in Ehlers-Danlos syndrome type VI. Am. J. Hum. Genet. 1995, 57:1505-1508.
123. Giunta C., Randolph A., Al-Gazali L.I., Brunner H.G., Kraenzlin M.E., Steinmann B. Nevo syndrome is allelic to the kyphoscoliotic type of the Ehlers-Danlos syndrome (EDS VIA). Am. J. Med. Genet. A 2005, 133A:158-164.
124. Kraenzlin M.E., Kraenzlin C.A., Meier C., Giunta C., Steinmann B. Automated HPLC assay for urinary collagen cross-links: effect of age, menopause, and metabolic bone diseases. Clin. Chem. 2008, 54:1546-1553.
125. Tremmel D., Duarte M., Videira A., Tropschug M. FKBP22 is part of chaperone/folding catalyst complexes in the endoplasmic reticulum of Neurospora crassa. FEBS Lett. 2007, 581:2036-2040.
126. Budiman C., Koga Y., Takano K., Kanaya S. FK506-binding protein 22 from a psychrophilic bacterium, a cold shock-inducible peptidyl prolyl isomerase with the ability to assist in protein folding. Int. J. Mol. Sci. 2011, 12:5261-5284.
127. Jana B., Sau S. The helix located between the two domains of a mip-like peptidyl-prolyl cis-trans isomerase is crucial for its structure. Stability, and Protein Folding Ability, Biochemistry 2012, 51:7930-7939.
128. Nagata K., Saga S., Yamada K.M. A major collagen-binding protein of chick embryo fibroblasts is a novel heat shock protein. J. Cell Biol. 1986, 103:223-229.
129. Nagata K. HSP47 as a collagen-specific molecular chaperone: function and expression in normal mouse development. Semin. Cell Dev. Biol. 2003, 14:275-282.
130. Hirayoshi K., Kudo H., Takechi H., Nakai A., Iwamatsu A., Yamada K.M., Nagata K. HSP47: a tissue-specific, transformation-sensitive, collagen-binding heat shock protein of chicken embryo fibroblasts. Mol. Cell. Biol. 1991, 11:4036-4044.
131. Tasab M., Batten M.R., Bulleid N.J. Hsp47: a molecular chaperone that interacts with and stabilizes correctly-folded procollagen. EMBO J. 2000, 19:2204-2211.
132. Ono T., Miyazaki T., Ishida Y., Uehata M., Nagata K. Direct in vitro and in vivo evidence for interaction between Hsp47 protein and collagen triple helix. J. Biol. Chem. 2012, 287:6810-6818.
133. Satoh M., Hirayoshi K., Yokota S., Hosokawa N., Nagata K. Intracellular interaction of collagen-specific stress protein HSP47 with newly synthesized procollagen. J. Cell Biol. 1996, 133:469-483.
134. Saga S., Nagata K., Chen W.T., Yamada K.M. pH-dependent function, purification, and intracellular location of a major collagen-binding glycoprotein. J. Cell Biol. 1987, 105:517-527.
135. Thomson C.A., Ananthanarayanan V.S. Structure-function studies on hsp47: pH-dependent inhibition of collagen fibril formation in vitro. Biochem. J. 2000, 349(Pt 3):877-883.
136. Widmer C., Gebauer J.M., Brunstein E., Rosenbaum S., Zaucke F., Drogemuller C., Leeb T., Baumann U. Molecular basis for the action of the collagen-specific chaperone Hsp47/SERPINH1 and its structure-specific client recognition. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:13243-13247.
137. Yagi-Utsumi M., Yoshikawa S., Yamaguchi Y., Nishi Y., Kurimoto E., Ishida Y., Homma T., Hoseki J., Nishikawa Y., Koide T., Nagata K., Kato K. NMR and mutational identification of the collagen-binding site of the chaperone hsp47. PLoS One 2012, 7:e45930.
138. Natsume T., Koide T., Yokota S., Hirayoshi K., Nagata K. Interactions between collagen-binding stress protein HSP47 and collagen. Analysis of kinetic parameters by surface plasmon resonance biosensor. J. Biol. Chem. 1994, 269:31224-31228.
139. Nishikawa Y., Takahara Y., Asada S., Shigenaga A., Otaka A., Kitagawa K., Koide T. A structure-activity relationship study elucidating the mechanism of sequence-specific collagen recognition by the chaperone HSP47. Bioorg. Med. Chem. 2010, 18:3767-3775.
140. Koide T., Nishikawa Y., Asada S., Yamazaki C.M., Takahara Y., Homma D.L., Otaka A., Ohtani K., Wakamiya N., Nagata K., Kitagawa K. Specific recognition of the collagen triple helix by chaperone HSP47. II. The HSP47-binding structural motif in collagens and related proteins. J. Biol. Chem. 2006, 281:11177-11185.
141. Koide T., Asada S., Takahara Y., Nishikawa Y., Nagata K., Kitagawa K. Specific recognition of the collagen triple helix by chaperone HSP47: minimal structural requirement and spatial molecular orientation. J. Biol. Chem. 2006, 281:3432-3438.
142. Nagai N., Hosokawa M., Itohara S., Adachi E., Matsushita T., Hosokawa N., Nagata K. Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis. J. Cell Biol. 2000, 150:1499-1506.
143. Ishida Y., Yamamoto A., Kitamura A., Lamande S.R., Yoshimori T., Bateman J.F., Kubota H., Nagata K. Autophagic elimination of misfolded procollagen aggregates in the endoplasmic reticulum as a means of cell protection. Mol. Biol. Cell 2009, 20:2744-2754.
144. Jensen D., Schekman R. COPII-mediated vesicle formation at a glance. J. Cell Sci. 2011, 124:1-4.
145. Barlowe C., Orci L., Yeung T., Hosobuchi M., Hamamoto S., Salama N., Rexach M.F., Ravazzola M., Amherdt M., Schekman R. COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum. Cell 1994, 77:895-907.
146. Matsuoka K., Orci L., Amherdt M., Bednarek S.Y., Hamamoto S., Schekman R., Yeung T. COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes. Cell 1998, 93:263-275.
147. Nakano A., Luini A. Passage through the Golgi. Curr. Opin. Cell Biol. 2010, 22:471-478.
148. Emr S., Glick B.S., Linstedt A.D., Lippincott-Schwartz J., Luini A., Malhotra V., Marsh B.J., Nakano A., Pfeffer S.R., Rabouille C., Rothman J.E., Warren G., Wieland F.T. Journeys through the Golgi-taking stock in a new era. J. Cell Biol. 2009, 187:449-453.
149. Bonfanti L., Mironov A.A., Martinez-Menarguez J.A., Martella O., Fusella A., Baldassarre M., Buccione R., Geuze H.J., Mironov A.A., Luini A. Procollagen traverses the Golgi stack without leaving the lumen of cisternae: evidence for cisternal maturation. Cell 1998, 95:993-1003.
150. Stephens D.J., Pepperkok R. Imaging of procollagen transport reveals COPI-dependent cargo sorting during ER-to-Golgi transport in mammalian cells. J. Cell Sci. 2002, 115:1149-1160.
151. Canty E.G., Kadler K.E. Procollagen trafficking, processing and fibrillogenesis. J. Cell Sci. 2005, 118:1341-1353.
152. Malhotra V., Erlmann P. Protein export at the ER: loading big collagens into COPII carriers. EMBO J. 2011, 30:3475-3480.
153. Wilson D.G., Phamluong K., Li L., Sun M., Cao T.C., Liu P.S., Modrusan Z., Sandoval W.N., Rangell L., Carano R.A., Peterson A.S., Solloway M.J. Global defects in collagen secretion in a Mia3/TANGO1 knockout mouse. J. Cell Biol. 2011, 193:935-951.
154. Saito K., Chen M., Bard F., Chen S., Zhou H., Woodley D., Polischuk R., Schekman R., Malhotra V. TANGO1 facilitates cargo loading at endoplasmic reticulum exit sites. Cell 2009, 136:891-902.
155. Saito K., Yamashiro K., Ichikawa Y., Erlmann P., Kontani K., Malhotra V., Katada T. cTAGE5 mediates collagen secretion through interaction with TANGO1 at endoplasmic reticulum exit sites. Mol. Biol. Cell 2011, 22:2301-2308.
156. Stagg S.M., Gurkan C., Fowler D.M., LaPointe P., Foss T.R., Potter C.S., Carragher B., Balch W.E. Structure of the Sec13/31 COPII coat cage. Nature 2006, 439:234-238.
157. Stagg S.M., LaPointe P., Razvi A., Gurkan C., Potter C.S., Carragher B., Balch W.E. Structural basis for cargo regulation of COPII coat assembly. Cell 2008, 134:474-484.
158. Russell C., Stagg S.M. New insights into the structural mechanisms of the COPII coat. Traffic 2010, 11:303-310.
159. Bhattacharya N., J O.D., Stagg S.M. The structure of the Sec13/31 COPII cage bound to Sec23. J. Mol. Biol. 2012, 420:324-334.
160. Townley A.K., Feng Y., Schmidt K., Carter D.A., Porter R., Verkade P., Stephens D.J. Efficient coupling of Sec23-Sec24 to Sec13-Sec31 drives COPII-dependent collagen secretion and is essential for normal craniofacial development. J. Cell Sci. 2008, 121:3025-3034.
161. Kim S.D., Pahuja K.B., Ravazzola M., Yoon J., Boyadjiev S.A., Hammamoto S., Schekman R., Orci L., Kim J. SEC23-SEC31 the interface plays critical role for export of procollagen from the endoplasmic reticulum. J. Biol. Chem. 2012, 287:10134-10144.
162. Townley A.K., Schmidt K., Hodgson L., Stephens D.J. Epithelial organization and cyst lumen expansion require efficient Sec13-Sec31-driven secretion. J. Cell Sci. 2012, 125:673-684.
163. Jin L., Pahuja K.B., Wickliffe K.E., Gorur A., Baumgartel C., Schekman R., Rape M. Ubiquitin-dependent regulation of COPII coat size and function. Nature 2012, 482:495-500.
164. O'Donnell J., Maddox K., Stagg S. The structure of a COPII tubule. J. Struct. Biol. 2011, 173:358-364.
165. Venditti R., Scanu T., Santoro M., Di Tullio G., Spaar A., Gaibisso R., Beznoussenko G.V., Mironov A.A., Mironov A., Zelante L., Piemontese M.R., Notarangelo A., Malhotra V., Vertel B.M., Wilson C., De Matteis M.A. Sedlin controls the ER export of procollagen by regulating the Sar1 cycle. Science 2012, 337:1668-1672.
166. Zanetti G., Pahuja K.B., Studer S., Shim S., Schekman R. COPII and the regulation of protein sorting in mammals. Nat. Cell Biol. 2011, 14:20-28.
167. Canty E.G., Lu Y., Meadows R.S., Shaw M.K., Holmes D.F., Kadler K.E. Coalignment of plasma membrane channels and protrusions (fibripositors) specifies the parallelism of tendon. J. Cell Biol. 2004, 165:553-563.
168. Engvall E., Hessle H., Klier G. Molecular assembly, secretion, and matrix deposition of type VI collagen. J. Cell Biol. 1986, 102:703-710.
169. Kaufman R.J. Orchestrating the unfolded protein response in health and disease. J. Clin. Invest. 2002, 110:1389-1398.
170. Bettica P., Baylink D.J., Moro L. Galactosyl hydroxylysine and deoxypyridinoline: a methodological comparison. Eur. J. Clin. Chem. Clin. Biochem. 1993, 31:459-465.
171. Chu M.L., Conway D., Pan T.C., Baldwin C., Mann K., Deutzmann R., Timpl R. Amino acid sequence of the triple-helical domain of human collagen type VI. J. Biol. Chem. 1988, 263:18601-18606.
172. Bos K.J., Rucklidge G.J., Dunbar B., Robins S.P. Primary structure of the helical domain of porcine collagen X. Matrix Biol. 1999, 18:149-153.
173. Dreisewerd K., Rohlfing A., Spottke B., Urbanke C., Henkel W. Characterization of whole fibril-forming collagen proteins of types I, III, and V from fetal calf skin by infrared matrix-assisted laser desorption ionization mass spectrometry. Anal. Chem. 2004, 76:3482-3491.
174. Henkel W., Dreisewerd K. Cyanogen bromide peptides of the fibrillar collagens I, III, and V and their mass spectrometric characterization: detection of linear peptides, peptide glycosylation, and cross-linking peptides involved in formation of homo- and heterotypic fibrils. J. Proteome Res. 2007, 6:4269-4289.
175. Ruggiero F., Koch M. Making recombinant extracellular matrix proteins. Methods 2008, 45:75-85.
176. Chung H.J., Jensen D.A., Gawron K., Steplewski A., Fertala A. R992C (p.R1192C) Substitution in collagen II alters the structure of mutant molecules and induces the unfolded protein response. J. Mol. Biol. 2009, 390:306-318.
177. Chung H.J., Steplewski A., Uitto J., Fertala A. Fluorescent protein markers to tag collagenous proteins: the paradigm of procollagen VII. Biochem. Biophys. Res. Commun. 2009, 390:662-666.
178. Roulet M., Valkkila M., Chanut-Delalande H., Hamalainen E.R., Kessler E., Ala-Kokko L., Mannikko M., Bonod-Bidaud C., Ruggiero F. The collagen V homotrimer [alpha1(V)](3) production is unexpectedly favored over the heterotrimer [alpha1(V)](2)alpha2(V) in recombinant expression systems. J. Biomed. Biotechnol. 2010, 2010:376927.
179. Bruckner-Tuderman L., Schnyder U.W., Winterhalter K.H., Bruckner P. Tissue form of type VII collagen from human skin and dermal fibroblasts in culture. Eur. J. Biochem. 1987, 165:607-611.
180. Nischt R., Pottgiesser J., Krieg T., Mayer U., Aumailley M., Timpl R. Recombinant expression and properties of the human calcium-binding extracellular matrix protein BM-40. Eur. J. Biochem. 1991, 200:529-536.
181. Stephan S., Sherratt M.J., Hodson N., Shuttleworth C.A., Kielty C.M. Expression and supramolecular assembly of recombinant alpha1(viii) and alpha2(viii) collagen homotrimers. J. Biol. Chem. 2004, 279:21469-21477.
182. Kobayashi T., Uchiyama M. Effect of HSP47 expression levels on heterotrimer formation among type IV collagen alpha3, alpha4 and alpha5 chains. Biomed. Res. 2010, 31:371-377.
183. Makareeva E., Han S., Vera J.C., Sackett D.L., Holmbeck K., Phillips C.L., Visse R., Nagase H., Leikin S. Carcinomas contain a matrix metalloproteinase-resistant isoform of type I collagen exerting selective support to invasion. Cancer Res. 2010, 70:4366-4374.
184. Han S., Makareeva E., Kuznetsova N.V., DeRidder A.M., Sutter M.B., Losert W., Phillips C.L., Visse R., Nagase H., Leikin S. Molecular mechanism of type I collagen homotrimer resistance to mammalian collagenases. J. Biol. Chem. 2010, 285:22276-22281.
185. Hosokawa N., Hohenadl C., Satoh M., Kuhn K., Nagata K. HSP47, a collagen-specific molecular chaperone, delays the secretion of type III procollagen transfected in human embryonic kidney cell line 293: a possible role for HSP47 in collagen modification. J. Biochem. 1998, 124:654-662.
186. Langley R., Leung E., Morris C., Berg R., McDonald M., Weaver A., Parry D.A., Ni J., Su J., Gentz R., Spurr N., Krissansen G.W. Identification of multiple forms of 180-kDa ribosome receptor in human cells. DNA Cell Biol. 1998, 17:449-460.
187. Savitz A.J., Meyer D.I. Identification of a ribosome receptor in the rough endoplasmic reticulum. Nature 1990, 346:540-544.
188. Ueno T., Kaneko K., Sata T., Hattori S., Ogawa-Goto K. Regulation of polysome assembly on the endoplasmic reticulum by a coiled-coil protein, p180. Nucleic Acids Res. 2012, 40:3006-3017.
189. Ueno T., Kaneko K., Katano H., Sato Y., Mazitschek R., Tanaka K., Hattori S., Irie S., Sata T., Ogawa-Goto K. Expansion of the trans-Golgi network following activated collagen secretion is supported by a coiled-coil microtubule-bundling protein, p180, on the ER. Exp. Cell Res. 2010, 316:329-340.
190. Ueno T., Tanaka K., Kaneko K., Taga Y., Sata T., Irie S., Hattori S., Ogawa-Goto K. Enhancement of procollagen biosynthesis by p180 through augmented ribosome association on the endoplasmic reticulum in response to stimulated secretion. J. Biol. Chem. 2010, 285:29941-29950.
191. Sohaskey M.L., Jiang Y., Zhao J.J., Mohr A., Roemer F., Harland R.M. Osteopotentia regulates osteoblast maturation, bone formation, and skeletal integrity in mice. J. Cell Biol. 2010, 189:511-525.
192. Nikaido T., Yokoya S., Mori T., Hagino S., Iseki K., Zhang Y., Takeuchi M., Takaki H., Kikuchi S., Wanaka A. Expression of the novel transcription factor OASIS, which belongs to the CREB/ATF family, in mouse embryo with special reference to bone development. Histochem. Cell Biol. 2001, 116:141-148.
193. Murakami T., Saito A., Hino S., Kondo S., Kanemoto S., Chihara K., Sekiya H., Tsumagari K., Ochiai K., Yoshinaga K., Saitoh M., Nishimura R., Yoneda T., Kou I., Furuichi T., Ikegawa S., Ikawa M., Okabe M., Wanaka A., Imaizumi K. Signalling mediated by the endoplasmic reticulum stress transducer OASIS is involved in bone formation. Nat. Cell Biol. 2009, 11:1205-1211.
194. 2+ signaling and calcium binding chaperones of the endoplasmic reticulum. Cell Calcium 2002, 32:269-278.
195. Murphy L.A., Ramirez E.A., Trinh V.T., Herman A.M., Anderson V.C., Brewster J.L. Endoplasmic reticulum stress or mutation of an EF-hand Ca(2+)-binding domain directs the FKBP65 rotamase to an ERAD-based proteolysis. Cell Stress Chaperones 2011, 16:607-619.
196. 2+ handling of alveolar epithelial cells and in perinatal lung maturation. Development 2009, 136:2355-2361.
197. 2+ handling in intracellular stores. Nature 2007, 448:78-82.
198. Shaheen R., Alazami A.M., Alshammari M.J., Faqeih E., Alhashmi N., Mousa N., Alsinani A., Ansari S., Alzahrani F., Al-Owain M., Alzayed Z.S., Alkuraya F.S. Study of autosomal recessive osteogenesis imperfecta in Arabia reveals a novel locus defined by TMEM38B mutation. J. Med. Genet. 2013, 49:630-635.
199. Hatahet F., Ruddock L.W. Substrate recognition by the protein disulfide isomerases. FEBS J. 2007, 274:5223-5234.
200. Araki K., Nagata K. Functional in vitro analysis of the ERO1 protein and protein-disulfide isomerase pathway. J. Biol. Chem. 2011, 286:32705-32712.
201. Sato Y., Inaba K. Disulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals. FEBS J. 2012, 279:2262-2271.
202. Appenzeller-Herzog C., Ellgaard L. The human PDI family: versatility packed into a single fold. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 2008, 1783:535-548.
203. Wouters M.A., Fan S.W., Haworth N.L. Disulfides as redox switches: from molecular mechanisms to functional significance. Antioxid. Redox Signal. 2010, 12:53-91.
204. de Jong L., Albracht S.P., Kemp A. Prolyl 4-hydroxylase activity in relation to the oxidation state of enzyme-bound iron. The role of ascorbate in peptidyl proline hydroxylation. Biochim. Biophys. Acta 1982, 704:326-332.
205. Fujita Y., Gottlieb A., Peterkofsky B., Udenfriend S., Witkop B. The preparation of cis- and trans-4-H3-l-prolines and their use in studying the mechanism of enzymatic hydroxylation in chick embryos. J. Am. Chem. Soc. 1964, 86:4709-4716.
206. Groves J.T., McClusky G.A. Aliphatic hydroxylation via oxygen rebound. Oxygen transfer catalyzed by iron. J. Am. Chem. Soc. 1976, 98:859-861.
207. Zito E., Hansen H.G., Yeo G.S., Fujii J., Ron D. Endoplasmic reticulum thiol oxidase deficiency leads to ascorbic acid depletion and noncanonical scurvy in mice. Mol. Cell 2012, 48:39-51.
208. Cundy T. Recent advances in osteogenesis imperfecta. Calcif. Tissue Int. 2012, 90:439-449.
209. De Paepe A., Malfait F. The Ehlers-Danlos syndrome, a disorder with many faces. Clin. Genet. 2012, 82:1-11.
210. Parkin J.D., San Antonio J.D., Pedchenko V., Hudson B., Jensen S.T., Savige J. Mapping structural landmarks, ligand binding sites, and missense mutations to the collagen IV heterotrimers predicts major functional domains, novel interactions, and variation in phenotypes in inherited diseases affecting basement membranes. Hum. Mutat. 2011, 32:127-143.
211. Bateman J.F., Wilson R., Freddi S., Lamande S.R., Savarirayan R. Mutations of COL10A1 in Schmid metaphyseal chondrodysplasia. Hum. Mutat. 2005, 25:525-534.
212. Wilson R., Freddi S., Chan D., Cheah K.S., Bateman J.F. Misfolding of collagen X chains harboring Schmid metaphyseal chondrodysplasia mutations results in aberrant disulfide bond formation, intracellular retention, and activation of the unfolded protein response. J. Biol. Chem. 2005, 280:15544-15552.
213. Hovnanian A., Rochat A., Bodemer C., Petit E., Rivers C.A., Prost C., Fraitag S., Christiano A.M., Uitto J., Lathrop M., Barrandon Y., de Prost Y. Characterization of 18 new mutations in COL7A1 in recessive dystrophic epidermolysis bullosa provides evidence for distinct molecular mechanisms underlying defective anchoring fibril formation. Am. J. Hum. Genet. 1997, 61:599-610.
214. Lamande S.R., Bateman J.F., Hutchison W., McKinlay Gardner R.J., Bower S.P., Byrne E., Dahl H.H. Reduced collagen VI causes Bethlem myopathy: a heterozygous COL6A1 nonsense mutation results in mRNA decay and functional haploinsufficiency. Hum. Mol. Genet. 1998, 7:981-989.
215. De Paepe A., Nuytinck L., Hausser I., Anton-Lamprecht I., Naeyaert J.M. Mutations in the COL5A1 gene are causal in the Ehlers-Danlos syndromes I and II. Am. J. Hum. Genet. 1997, 60:547-554.
216. Pickup M.J., Pollanen M.S. Traumatic subarachnoid hemorrhage and the COL3A1 gene: emergence of a potential causal link. Forensic Sci. Med. Pathol. 2011, 7:192-197.
217. Hoornaert K.P., Marik I., Kozlowski K., Cole T., Le Merrer M., Leroy J.G., Coucke P.J., Sillence D., Mortier G.R. Czech dysplasia metatarsal type: another type II collagen disorder. Eur. J. Hum. Genet. 2007, 15:1269-1275.
218. Mortier G.R., Weis M., Nuytinck L., King L.M., Wilkin D.J., De Paepe A., Lachman R.S., Rimoin D.L., Eyre D.R., Cohn D.H. Report of five novel and one recurrent COL2A1 mutations with analysis of genotype-phenotype correlation in patients with a lethal type II collagen disorder. J. Med. Genet. 2000, 37:263-271.
219. Richards A.J., Morgan J., Bearcroft P.W., Pickering E., Owen M.J., Holmans P., Williams N., Tysoe C., Pope F.M., Snead M.P., Hughes H. Vitreoretinopathy with phalangeal epiphyseal dysplasia, a type II collagenopathy resulting from a novel mutation in the C-propeptide region of the molecule. J. Med. Genet. 2002, 39:661-665.
220. Chessler S.D., Byers P.H. BiP binds type I procollagen pro alpha chains with mutations in the carboxyl-terminal propeptide synthesized by cells from patients with osteogenesis imperfecta. J. Biol. Chem. 1993, 268:18226-18233.
221. Boot-Handford R.P., Briggs M.D. The unfolded protein response and its relevance to connective tissue diseases. Cell Tissue Res. 2010, 339:197-211.
222. Hopfer U., Fukai N., Hopfer H., Wolf G., Joyce N., Li E., Olsen B.R. Targeted disruption of Col8a1 and Col8a2 genes in mice leads to anterior segment abnormalities in the eye. FASEB J. 2005, 19:1232-1244.
223. Heinonen S., Mannikko M., Klement J.F., Whitaker-Menezes D., Murphy G.F., Uitto J. Targeted inactivation of the type VII collagen gene (Col7a1) in mice results in severe blistering phenotype: a model for recessive dystrophic epidermolysis bullosa. J. Cell Sci. 1999, 112(Pt 21):3641-3648.
224. Izu Y., Ansorge H.L., Zhang G., Soslowsky L.J., Bonaldo P., Chu M.L., Birk D.E. Dysfunctional tendon collagen fibrillogenesis in collagen VI null mice. Matrix Biol. 2011, 30:53-61.
225. Huang G., Ge G., Wang D., Gopalakrishnan B., Butz D.H., Colman R.J., Nagy A., Greenspan D.S. alpha3(V) collagen is critical for glucose homeostasis in mice due to effects in pancreatic islets and peripheral tissues. J. Clin. Invest. 2011, 121:769-783.
226. Wenstrup R.J., Florer J.B., Brunskill E.W., Bell S.M., Chervoneva I., Birk D.E. Type V collagen controls the initiation of collagen fibril assembly. J. Biol. Chem. 2004, 279:53331-53337.
227. Cosgrove D., Meehan D.T., Grunkemeyer J.A., Kornak J.M., Sayers R., Hunter W.J., Samuelson G.C. Collagen COL4A3 knockout: a mouse model for autosomal Alport syndrome. Genes Dev. 1996, 10:2981-2992.
228. Poschl E., Schlotzer-Schrehardt U., Brachvogel B., Saito K., Ninomiya Y., Mayer U. Collagen IV is essential for basement membrane stability but dispensable for initiation of its assembly during early development. Development 2004, 131:1619-1628.
229. Liu X., Wu H., Byrne M., Krane S., Jaenisch R. Type III collagen is crucial for collagen I fibrillogenesis and for normal cardiovascular development. Proc. Natl. Acad. Sci. U.S.A. 1997, 94:1852-1856.
230. Li S.W., Prockop D.J., Helminen H., Fassler R., Lapvetelainen T., Kiraly K., Peltarri A., Arokoski J., Lui H., Arita M., et al. Transgenic mice with targeted inactivation of the Col2 alpha 1 gene for collagen II develop a skeleton with membranous and periosteal bone but no endochondral bone. Genes Dev. 1995, 9:2821-2830.
231. Schnieke A., Harbers K., Jaenisch R. Embryonic lethal mutation in mice induced by retrovirus insertion into the alpha 1(I) collagen gene. Nature 1983, 304:315-320.
232. Lapunzina P., Aglan M., Temtamy S., Caparros-Martin J.A., Valencia M., Leton R., Martinez-Glez V., Elhossini R., Amr K., Vilaboa N., Ruiz-Perez V.L. Identification of a frameshift mutation in Osterix in a patient with recessive osteogenesis imperfecta. Am. J. Hum. Genet. 2010, 87:110-114.
233. Homan E.P., Rauch F., Grafe I., Lietman C., Doll J.A., Dawson B., Bertin T., Napierala D., Morello R., Gibbs R., White L., Miki R., Cohn D.H., Crawford S., Travers R., Glorieux F.H., Lee B. Mutations in SERPINF1 cause osteogenesis imperfecta type VI. J. Bone Miner. Res. 2011, 26:2798-2803.
234. Venturi G., Gandini A., Monti E., Dalle Carbonare L., Corradi M., Vincenzi M., Valenti M.T., Valli M., Pelilli E., Boner A., Mottes M., Antoniazzi F. Lack of expression of SERPINF1, the gene coding for pigment epithelium-derived factor, causes progressively deforming osteogenesis imperfecta with normal type I collagen. J. Bone Miner. Res. 2012, 27:723-728.
235. Cho T.J., Lee K.E., Lee S.K., Song S.J., Kim K.J., Jeon D., Lee G., Kim H.N., Lee H.R., Eom H.H., Lee Z.H., Kim O.H., Park W.Y., Park S.S., Ikegawa S., Yoo W.J., Choi I.H., Kim J.W. A single recurrent mutation in the 5'-UTR of IFITM5 causes osteogenesis imperfecta type V. Am. J. Hum. Genet. 2012, 91:343-348.
236. Semler O., Garbes L., Keupp K., Swan D., Zimmermann K., Becker J., Iden S., Wirth B., Eysel P., Koerber F., Schoenau E., Bohlander S.K., Wollnik B., Netzer C. A mutation in the 5'-UTR of IFITM5 creates an in-frame start codon and causes autosomal-dominant osteogenesis imperfecta type V with hyperplastic callus. Am. J. Hum. Genet. 2012, 91:349-357.
237. Shapiro J.R., Lietman C., Grover M., Lu J.T., Nagamani S.C., Dawson B.C., Baldridge D.M., Bainbridge M.N., Cohn D.H., Blazo M., Roberts T.T., Brennen F.S., Wu Y., Gibbs R.A., Melvin P., Campeau P.M., Lee B.H. Phenotypic variability of osteogenesis imperfecta type V caused by an IFITM5 mutation. J. Bone Miner. Res. 2013, Epub ahead of print.
238. Lindahl K., Barnes A.M., Fratzl-Zelman N., Whyte M.P., Hefferan T.E., Makareeva E., Brusel M., Yaszemski M.J., Rubin C.J., Kindmark A., Roschger P., Klaushofer K., McAlister W.H., Mumm S., Leikin S., Kessler E., Boskey A.L., Ljunggren O., Marini J.C. COL1 C-propeptide cleavage site mutations cause high bone mass osteogenesis imperfecta. Hum. Mutat. 2011, 32:598-609.