Aggregates, crystals, gels, and amyloids: Intracellular and extracellular phenotypes at the crossroads of immunoglobulin physicochemical property and cell physiology

International Journal of Cell Biology

Volumn , Issue , 2013, Pages

  Hasegawa, Haruki ^a  

^a AMGEN INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CRYOGLOBULIN; IMMUNOGLOBULIN; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G; IMMUNOGLOBULIN HEAVY CHAIN; IMMUNOGLOBULIN LIGHT CHAIN; IMMUNOGLOBULIN M; PARAPROTEIN;

ADULT DISEASE; AMINO ACID SEQUENCE; AMYLOIDOSIS; ANTIBODY DETECTION; ANTIBODY ENGINEERING; ANTIBODY PRODUCTION; ANTIBODY SCREENING; BIOGENESIS; CARBOXY TERMINAL SEQUENCE; CELL PHENOTYPE; CELLULAR, SUBCELLULAR AND MOLECULAR BIOLOGICAL PHENOMENA AND FUNCTIONS; CRYSTAL STRUCTURE; CRYSTALLINE BODY; CRYSTALLIZATION; CYTOPLASM; DRUG MANUFACTURE; ENDOSOME; FANCONI RENOTUBULAR SYNDROME; GENE DELETION; HISTIOCYTOSIS; HUMAN; HYBRIDOMA CELL CULTURE; IMMUNOGLOBULIN PRODUCTION; LYMPHOCYTE; LYSOSOME; NONHUMAN; PHENOTYPE; PLASMA CELL; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN HOMEOSTASIS; REVIEW; RUSSELL BODY;

EID: 84875582175     PISSN: 16878876     EISSN: 16878884     Source Type: Journal    
DOI: 10.1155/2013/604867     Document Type: Review

References (232)

1. Tonegawa S., Somatic generation of antibody diversity. Nature 1983 302 5909 575 581 2-s2.0-0020534965
2. Berek C., Milstein C., The dynamic nature of the antibody repertoire. Immunological Reviews 1988 105 5 26 2-s2.0-0023821895
3. Russell W., An address on a characteristic organism of cancer. British Medical Journal 1890 2 1356 1360
4. Russell W., The parasite of cancer. The Lancet 1899 153 3948 1138 1141 2-s2.0-50549186548
5. Cowdry E. V., Nicholson F. M., Inclusion bodies in experimental herpetic infection of rabbits. The Journal of Experimental Medicine 1923 38 695 706
6. Michels N. A., The plasma cell. A critical review of its morphogensis, function and developmental capacity under normal and under abnormal conditions. Archives of Pathology 1931 11 775 793
7. McConnell G., Lang A., Russell's fuchsin bodies. The Journal of Medical Research 1921 42 99 103
8. Pearse A. G., The nature of Russell bodies and Kurloff bodies; observations on the. Journal of Clinical Pathology 1949 2 2 81 90 2-s2.0-78651004183
9. Lisco H., Russell bodies occurring in the lymph follicles of the intestinal tract of pigs. Anatomical Record 1942 82 59 66
10. Gray A., Doniach I., Ultrastructure of plasma cells containing Russell bodies in human stomach and thyroid. Journal of Clinical Pathology 1970 23 7 608 612 2-s2.0-0014856417
11. Iwamoto T., Witmer R., Light and electron microscopy on plasma cells and Russell bodies in the iris of a chronic uveitis patient. Investigative Ophthalmology 1969 8 6 563 582 2-s2.0-0014633853
12. King D. F., Eisenberg D., Russell's fuchsine body. 'The characteristic organism of cancer'. American Journal of Dermatopathology 1981 3 1 55 58 2-s2.0-0019431377 (Pubitemid 11114746)
13. Blom J., Mansa B., Wiik A., A study of Russell bodies in human monoclonal plasma cells by means of immunofluorescence and electron microscopy. Acta Pathologica et Microbiologica Scandinavica A 1976 84 4 335 349 2-s2.0-0017165492
14. WHITE R. G., Observations on the formation and nature of Russell bodies. British Journal of Experimental Pathology 1954 35 4 365 376 2-s2.0-0009511455
15. Oikawa K., Electron microscopic observation of inclusion bodies in plasma cells of multiple myeloma and Waldenstrom's macroglobulinemia. Tohoku Journal of Experimental Medicine 1975 117 3 257 281 2-s2.0-0016796679
16. Laszlo J., Gerber H. J., Sommer J. R., Composition and structure of cytoplasmic globules in leukemic lymphocytes. Blood 1967 29 1 77 86 2-s2.0-0014035204
17. Matthews J. B., The immunoglobulin nature of Russell bodies. British Journal of Experimental Pathology 1983 64 3 331 335 2-s2.0-0020524403 (Pubitemid 13032868)
18. Welsh R. A., Electron microscopic localization of Russell bodies in the human plasma cell. Blood 1960 16 1307 1312 2-s2.0-9944243843
19. Ortega L. G., Mellors R. C., Cellular sites of formation of gamma globulin. The Journal of Experimental Medicine 1957 106 5 627 640 2-s2.0-2442500462
20. Kopito R. R., Sitia R., Aggresomes and Russell bodies-symptoms of cellular indigestion? EMBO Reports 2000 1 3 225 231 2-s2.0-0034278759
21. Mott F., Observations on the brains of men and animals infected with various forms of trypanosomes. Preliminary note. Proceedings of the Royal Society of London B 1905 76 235 242
22. Rondanelli E. G., Gorini P., Strosselli E., Pecorari D., The nature of the endocytoplasmic globules of the morular cells of human bone marrow. Haematologica 1957 42 1027 1040
23. Jacob H., Lutcke A., Subacute sclerosing leukoencephalitis simulating acute epidemic encephalitis (acute encephalitic parkinsonism) with marked development of morular cells and Russell bodies. Journal of the Neurological Sciences 1971 12 137 153
24. Greenwood B. M., Whittle H. C., Cerebrospinal fluid IgM in patients with sleeping sickness. The Lancet 1973 2 7828 525 527 2-s2.0-0015895329
25. East J., de Sousa M. A., Parrott D. M., Immunopathology of New Zealand black (NZB) mice. Transplantation 1965 3 6 711 729 2-s2.0-0013815859
26. Shultz L. D., Coman D. R., Lyons B. L., Development of plasmacytoid cells with Russell bodies in autoimmune "viable motheaten" mice. American Journal of Pathology 1987 127 1 38 50 2-s2.0-0023276236 (Pubitemid 17062585)
27. Schweitzer P. A., Taylor S. E., Shultz L. D., Synthesis of abnormal immunoglobulins by hybridomas from autoimmune "viable motheaten" mutant mice. Journal of Cell Biology 1991 114 1 35 43 2-s2.0-0026076298 (Pubitemid 21909778)
28. van Greune C. H. J., Slazus A., Rossouw D. J., Circulating Russell-body-containing lymphoid cells in an immunocytoma patient. Acta Haematologica 1994 91 2 108 110 2-s2.0-0028300972 (Pubitemid 24192804)
29. Posnett D. N., Mouradian J., Mangraviti D. J., Wolf D. J., Mott cells in a patient with a lymphoproliferative disorder differentiation of a clone of B lymphocytes into mott cells. American Journal of Medicine 1984 77 1 125 130 2-s2.0-0021273670 (Pubitemid 14084916)
30. Bangle R. Jr., A morphologic and histochemical study of cytoplasmic russell bodies in. The American Journal of Pathology 1963 43 437 448 2-s2.0-0008565384
31. Pizzolitto S., Camilot D., DeMaglio G., Falconieri G., Russell body gastritis: expanding the spectrum of Helicobacter pylori-related diseases? Pathology Research and Practice 2007 203 6 457 460 2-s2.0-34249826041 10.1016/j.prp.2007.01.009 (Pubitemid 46852311)
32. Mori N., Abe M., Kojima M., Study of malignant lymphomas from the aspect of immunoglobulin production. Acta Pathologica Japonica 1979 29 5 705 722 2-s2.0-0018597738 (Pubitemid 10196760)
33. Stich M. H., Swiller A. I., Morrison M., The grape cell of multiple myeloma. American Journal of Clinical Pathology 1955 25 5 601 602 2-s2.0-77049199519
34. Zlotnick A., The morular cell and the grape cell in bone marrow and peripheral blood. Blood 1956 11 12 1140 1147 2-s2.0-77049283142
35. Zlotnick A., Gerichter C. B., Nir I., Experimental production of grape cells and their relation to the serum gamma globulin and seromucoids. Blood 1959 14 5 564 570 2-s2.0-70449257507
36. Miller F. R., The induced development and histogenesis of plasma cells. The Journal of Experimental Medicine 1931 54 3 333 347
37. Downey H., The origin and structure of the plasma cells of normal vertebrates, especially of the cold blooded vertebrates, and the eosinophils of the lung of amblystoma. Folia Haematologica 1911 11 275 314
38. Wight P. A., Burns R. B., Rothwell B., Mackenzie G. M., The Harderian gland of the domestic fowl. I. Histology, with reference to the genesis of plasma cells and Russell bodies. Journal of Anatomy 1971 110 2 307 315 2-s2.0-0015152335
39. Nowak J. S., Kai O., Peck R., Franklin R. M., The effects of cyclosporin A on the chicken immune system. European Journal of Immunology 1982 12 10 867 876 2-s2.0-0020412543 (Pubitemid 13253411)
40. Jiang Y., Hirose S., Hamano Y., Kodera S., Tsurui H., Abe M., Terashima K., Ishikawa S., Shirai T., Mapping of a gene for the increased susceptibility of B1 cells to mott cell formation in murine autoimmune disease. Journal of Immunology 1997 158 2 992 997 2-s2.0-0031567985 (Pubitemid 127492681)
41. Weiss S., Burrows P. D., Meyer J., Wabl M. R., A Mott cell hybridoma. European Journal of Immunology 1984 14 8 744 748 2-s2.0-0021262577 (Pubitemid 14064142)
42. Alanen A., Pira U., Lassila O., Mott cells are plasma cells defective in immunoglobulin secretion. European Journal of Immunology 1985 15 3 235 242 2-s2.0-0021797741 (Pubitemid 15077957)
43. Alanen A., Pira U., Colman A., Franklin R. M., Mott cells: a model to study immunoglobulin secretion. European Journal of Immunology 1987 17 11 1573 1577 2-s2.0-0023502153 (Pubitemid 18000194)
44. Schultz L. D., Coman D. R., Bailey C. L., 'Viable motheaten', a new allele at the motheaten locus. I. Pathology. American Journal of Pathology 1984 116 2 179 192 2-s2.0-0021200413 (Pubitemid 14053909)
45. Sidman C. L., Marshall J. D., Masiello N. C., Novel B-cell maturation factor from spontaneously autoimmune viable motheaten mice. Proceedings of the National Academy of Sciences of the United States of America 1984 81 22 I 7199 7202 2-s2.0-0021686827 (Pubitemid 15216724)
46. Lonberg N., Human antibodies from transgenic animals. Nature Biotechnology 2005 23 9 1117 1125 2-s2.0-27144532832 10.1038/nbt1135 (Pubitemid 41486393)
47. Zou X., Osborn M. J., Bolland D. J., Smith J. A., Corcos D., Hamon M., Oxley D., Hutchings A., Morgan G., Santos F., Kilshaw P. J., Taussig M. J., Corcoran A. E., Brüggemann M., Heavy chain-only antibodies are spontaneously produced in light chain-deficient mice. Journal of Experimental Medicine 2007 204 13 3271 3283 2-s2.0-37549052817 10.1084/jem.20071155
48. Matheson L. S., Osborn M. J., Smith J. A., Corcos D., Hamon M., Chaouaf R., Coadwell J., Morgan G., Oxley D., Brüggemann M., Light chain-deficient mice produce novel multimeric heavy-chain-only IgA by faulty class switching. International Immunology 2009 21 8 957 966 2-s2.0-70349481762 10.1093/intimm/dxp062
49. Kohler G., Immunoglobulin chain loss in hybridoma lines. Proceedings of the National Academy of Sciences of the United States of America 1980 77 4 2197 2199 2-s2.0-0019188771 (Pubitemid 10089625)
50. Hendershot L., Bole D., Kohler G., Kearney J. F., Assembly and secretion of heavy chains that do not associate posttranslationally with immunoglobulin heavy chain-binding protein. Journal of Cell Biology 1987 104 3 761 767 2-s2.0-0023096246 (Pubitemid 17024730)
51. Hamers-Casterman C., Atarhouch T., Muyldermans S., Robinson G., Hamers C., Songa E. B., Bendahman N., Hamers R., Naturally occurring antibodies devoid of light chains. Nature 1993 363 6428 446 448 2-s2.0-0027310612 10.1038/363446a0 (Pubitemid 23179389)
52. Nguyen V. K., Su C., Muyldermans S., Van Der Loo W., Heavy-chain antibodies in Camelidae; a case of evolutionary innovation. Immunogenetics 2002 54 1 39 47 2-s2.0-0036251627 10.1007/s00251-002-0433-0 (Pubitemid 34492951)
53. Corcos D., Osborn M. J., Matheson L. S., B-cell receptors and heavy chain diseases: guilty by association? Blood 2011 117 26 6991 6998 2-s2.0-79959837595 10.1182/blood-2011-02-336164
54. Cogne M., Preud'homme J. L., Guglielmi P., Immunoglobulin gene alterations in human heavy chain diseases. Research in Immunology 1989 140 5-6 487 502 2-s2.0-0024413178 (Pubitemid 19200266)
55. Cogne M., Silvain C., Khamlichi A. A., Preud'homme J. L., Structurally abnormal immunoglobulins in human immunoproliferative disorders. Blood 1992 79 9 2181 2195 2-s2.0-0026753369
56. Tarlinton D., Forster I., Rajewsky K., An explanation for the defect in secretion IgM Mott cells and their predominant occurrence in the Ly-1 B cell compartment. European Journal of Immunology 1992 22 2 531 539 2-s2.0-0026515437
57. Corcos D., Osborn M. J., Matheson L. S., Santos F., Zou X., Smith J. A., Morgan G., Hutchings A., Hamon M., Oxley D., Brüggemann M., Immunoglobulin aggregation leading to Russell body formation is prevented by the antibody light chain. Blood 2010 115 2 282 288 2-s2.0-75649140280 10.1182/blood-2009-07-234864
58. Valetti C., Grossi C. E., Milstein C., Sitia R., Russell bodies: a general response of secretory cells to synthesis of a mutant immunoglobulin which can neither exit from, nor be degraded in, the endoplasmic reticulum. Journal of Cell Biology 1991 115 4 983 994 2-s2.0-0026347810 (Pubitemid 21909947)
59. Mattioli L., Anelli T., Fagioli C., Tacchetti C., Sitia R., Valetti C., ER storage diseases: a role for ERGIC-53 in controlling the formation and shape of Russell bodies. Journal of Cell Science 2006 119 12 2532 2541 2-s2.0-33746032588 10.1242/jcs.02977 (Pubitemid 44070434)
60. Kaloff C. R., Haas I. G., Coordination of immunoglobulin chain folding and immunoglobulin chain assembly is essential for the formation of functional IgG. Immunity 1995 2 6 629 637 2-s2.0-0029022591
61. Lee Y. K., Brewer J. W., Hellman R., Hendershot L. M., BiP and immunoglobulin light chain cooperate to control the folding of heavy chain and ensure the fidelity of immunoglobulin assembly. Molecular Biology of the Cell 1999 10 7 2209 2219 2-s2.0-0032838622 (Pubitemid 29343130)
62. Feige M. J., Groscurth S., Marcinowski M., Shimizu Y., Kessler H., Hendershot L. M., Buchner J., An unfolded CH1 domain controls the assembly and secretion of IgG antibodies. Molecular Cell 2009 34 5 569 579 2-s2.0-66449119429 10.1016/j.molcel.2009.04.028
63. Meunier L., Usherwood Y. K., Tae Chung K., Hendershot L. M., A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Molecular Biology of the Cell 2002 13 12 4456 4469 2-s2.0-0036911213 10.1091/mbc.E02-05-0311 (Pubitemid 35471198)
64. Ronzoni R., Anelli T., Brunati M., Cortini M., Fagioli C., Sitia R., Pathogenesis of ER storage disorders: modulating russell body biogenesis by altering proximal and distal quality control. Traffic 2010 11 7 947 957 2-s2.0-77954714045 10.1111/j.1600-0854.2010.01071.x
65. Zou X., Ayling C., Xian J., Piper T. A., Barker P. J., Brüggemann M., Truncation of the heavy chain alters BCR signalling and allows recruitment of CD5+ B cells. International Immunology 2001 13 12 1489 1499 2-s2.0-0035207048 (Pubitemid 33138109)
66. Zou X., Smith J. A., Corcos D., Matheson L. S., Osborn M. J., Brüggemann M., Removal of the BiP-retention domain in C permits surface deposition and developmental progression without L-chain. Molecular Immunology 2008 45 13 3573 3579 2-s2.0-47049101691 10.1016/j.molimm.2008.05.003
67. Jack H. M., Beck-Engeser G., Sloan B., Mei Lie Wong, Wabl M., A different sort of Mott cell. Proceedings of the National Academy of Sciences of the United States of America 1992 89 24 11688 11691 2-s2.0-0027096270 10.1073/pnas.89.24.11688 (Pubitemid 23004708)
68. Stoops J., Byrd S., Hasegawa H., Russell body inducing threshold depends on the variable domain sequences of individual human IgG clones and the cellular protein homeostasis. Biochimica et Biophysica Acta 2012 1823 10 1643 1657
69. Hendershot L. M., Immunoglobulin heavy chain and binding protein complexes are dissociated in vivo by light chain addition. Journal of Cell Biology 1990 111 3 829 837 2-s2.0-0025007007 10.1083/jcb.111.3.829 (Pubitemid 20263767)
70. Jayaram N., Bhowmick P., Martin A. C., Germline VH/VL pairing in antibodies. Protein Engineering, Design & Selection 2012 25 523 530 10.1093/protein/gzs043
71. Hamel P. A., Klein M. H., Dorrington K. J., The role of the V(L)- and V(H)-segments in the preferential reassociation of immunoglobulin subunits. Molecular Immunology 1986 23 5 503 510 2-s2.0-0022557571 (Pubitemid 16113212)
72. Hamel P. A., Klein M. H., Smith-Gill S. J., Dorrington K. J., Relative noncovalent association constant between immunoglobulin H and L chains is unrelated to their expression or antigen-binding activity. Journal of Immunology 1987 139 9 3012 3020 2-s2.0-0023618288 (Pubitemid 17157473)
73. Chen C., Martin T. M., Stevens S., Rittenberg M. B., Defective secretion of an immunoglobulin caused by mutations in the heavy chain complementarity determining region 2. Journal of Experimental Medicine 1994 180 2 577 586 2-s2.0-0028357638 10.1084/jem.180.2.577 (Pubitemid 24224134)
74. Whitcomb E. A., Martin T. M., Rittenberg M. B., Restoration of ig secretion: mutation of germline-encoded residues in T15L chains leads to secretion of free light chains and assembled antibody complexes bearing secretion-impaired heavy chains. Journal of Immunology 2003 170 4 1903 1909 2-s2.0-0037442011 (Pubitemid 36197408)
75. Dul J. L., Argon Y., A single amino acid substitution in the variable region of the light chain specifically blocks immunoglobulin secretion. Proceedings of the National Academy of Sciences of the United States of America 1990 87 20 8135 8139 2-s2.0-0025134871
76. Dul J. L., Burrone O. R., Argon Y., A conditional secretory mutant in an Ig L chain is caused by replacement of tyrosine/phenylalanine 87 with histidine. Journal of Immunology 1992 149 6 1927 1933 2-s2.0-0026768470
77. Wu G. E., Hozumi N., Murialdo H., Secretion of a 2 immunoglobulin chain is prevented by a single amino acid substitution in its variable region. Cell 1983 33 1 77 83 2-s2.0-0020641571 (Pubitemid 13096436)
78. Wiens G. D., Lekkerkerker A., Veltman I., Rittenberg M. B., Mutation of a single conserved residue in VH complementarity-determining region 2 results in a severe Ig secretion defect. Journal of Immunology 2001 167 4 2179 2186 2-s2.0-0035881257 (Pubitemid 32747528)
79. Glaus A., Uber multiples myelozytom mit egnartigen, zum teil cristallahnlichen zelleingnlagerungen kombiniert mit elastolyse und ausgedehnter amyloidose und verkalkung. Virchows Archiv für Pathologische Anatomie und Physiologie und für Klinische Medizin 1917 223 3 301 339 2-s2.0-0001691926 10.1007/BF02034325
80. Wada R., Ebina Y., Kurotaki H., Yagihashi S., Intracytoplasmic immunoglobulin crystals in follicular lymphoma. Human Pathology 2002 33 11 1141 1144 2-s2.0-0036857142 10.1053/hupa.2002.129206 (Pubitemid 35416714)
81. Zettergren L., Intracellular protein crystallization. Acta Pathologica et Microbiologica Scandinavica 1949 26 5 696 704 2-s2.0-76549230121
82. Goldberg A. F., Deane H. W., A comparative study of some staining properties of crystals in a lympho-plasmocytoid cell, of Russell bodies in plasmocytes, and of amyloids-with special emphasis on their isoelectric points. Blood 1960 16 1708 1721 2-s2.0-70449300815
83. Goldberg A. F., An unusual lymphomatous disease associated with intracytoplasmic crystals in lymphoplasmocytoid cells. Blood 1960 16 1693 1707 2-s2.0-0011857742
84. Hurez D., Flandrin G., Preud'homme J. L., Seligmann M., Unreleased intracellular monoclonal macroglobulin in chronic lymphocytic leukaemia. Clinical and Experimental Immunology 1972 10 2 223 234 2-s2.0-0015298757
85. Cawley J. C., Barker C. R., Britchford R. D., Smith J. L., Intracellular IgA immunoglobulin crystals in chronic lymphocytic leukaemia. Clinical and Experimental Immunology 1973 13 3 407 416 2-s2.0-0015595941
86. Cawley J. C., Smith J., Goldstone A. H., IgA and IgM cytoplastic inclusions in a series of cases of chronic lymphocytic leukaemia. Clinical and Experimental Immunology 1976 23 1 78 82 2-s2.0-0016871330
87. Feremans W. W., Neve P., Caudron M., IgM lambda cytoplasmic crystals in three cases of immunocytoma: a clinical, cytochemical, and ultrastructural study. Journal of Clinical Pathology 1978 31 3 250 258 2-s2.0-0017871002 (Pubitemid 8319621)
88. Ralfkiaer E., Hou-Jensen K., Geisler C., Cytoplasmic inclusion in lymphocytes of chronic lymphocytic leukemia. A report of 10 cases. Virchows Archiv A Pathological Anatomy and Histology 1982 395 2 227 236 2-s2.0-0020004627 (Pubitemid 12100707)
89. White V., Boyko W. J., Chronic lymphocytic leukemia with IgM and IgG cytoplasmic inclusions. Archives of Pathology and Laboratory Medicine 1983 107 11 580 582 2-s2.0-0020610659 (Pubitemid 13017251)
90. den Ottolander G. J., Brederoo P., Schuurman R. K. B., Intracellular immunoglobulin G "pseudocrystals" in a patient with chronic B-cell leukemia. Cancer 1986 58 1 43 51 2-s2.0-0022602874 (Pubitemid 16093101)
91. Tsuchikawa K., Yokomichi H., Satoh I., Suzuki C., Watanabe Y., Tajima G., A study of intracytoplasmic inclusions in myeloma cells from two patients with multiple myeloma. Tohoku Journal of Experimental Medicine 1987 153 1 11 20 2-s2.0-0023619820 (Pubitemid 17167827)
92. De Man J. C., Meiners W. B., Crystals of protein nature in the cytoplasm of lymphatic cells in a case of lymphoreticular malignancy. Blood 1962 20 492 500 2-s2.0-73049180361
93. Stefani S., Chandra S., Schrek R., Endoplasmic reticulum associated structures in lymphocytes from patients with chronic lymphocytic leukemia. Blood 1977 50 1 125 139 2-s2.0-0017640646 (Pubitemid 8124757)
94. Clark C., Rydell R. E., Kaplan M. E., Frequent association of IgMlambda with crystalline inclusions in chronic lymphatic leukemic lymphocytes. The New England Journal of Medicine 1973 289 3 113 117 2-s2.0-0015930061
95. McCann S. R., Whelan A., Greally J., Intracellular light chain inclusions in chronic lymphocytic leukaemia. British Journal of Haematology 1978 38 3 367 371 2-s2.0-0017873835
96. Reason D. C., A murine hybridoma with large cytoplasmic inclusions of light chains. Journal of Experimental Medicine 1987 165 2 578 583 2-s2.0-0023111850 (Pubitemid 17019838)
97. Jack H. M., Sloan B., Grisham G., Reason D., Wabl M., Large cytoplasmic inclusion body -chain has unusual intrachain disulfide bonding. Journal of Immunology 1993 150 11 4928 4933 2-s2.0-0027215782 (Pubitemid 23150359)
98. Steiner L. A., Amino acid sequence of the heavy-chain variable region of the crystallizable human myeloma protein dob. Biochemistry 1979 18 19 4068 4080 2-s2.0-0018639040 (Pubitemid 10199710)
99. Steiner L. A., The crystallizable human myeloma protein Dob has a hinge-region deletion. Biochemistry 1979 18 19 4054 4067 2-s2.0-0018795180
100. Deutsch H. F., Suzuki T., A crystalline G1 human monoclonal protein with an excessive H chain deletion. Annals of the New York Academy of Sciences 1971 190 472 486 2-s2.0-0015247398
101. Tasso D., Gulbahce H. E., Berger M. J., McKenna R. W., Pambuccian S. E., Intracytoplasmic crystalline and globular inclusions in small lymphocytic lymphoma in transformation. Diagnostic Cytopathology 2012 40 42 44
102. Hasegawa H., Wendling J., He F., Trilisky E., Stevenson R., Franey H., Kinderman F., Li G., Piedmonte D. M., Osslund T., Shen M., Ketchem R. R., In vivo crystallization of human IgG in the endoplasmic reticulum of engineered chinese hamster ovary (CHO) cells. Journal of Biological Chemistry 2011 286 22 19917 19931 2-s2.0-79957624386 10.1074/jbc.M110.204362
103. Casey J. R., Grinstein S., Orlowski J., Sensors and regulators of intracellular pH. Nature Reviews Molecular Cell Biology 2010 11 1 50 61 2-s2.0-72949121897 10.1038/nrm2820
104. Paroutis P., Touret N., Grinstein S., The pH of the secretory pathway: measurement, determinants, and regulation. Physiology 2004 19 207 215 2-s2.0-4544382386 (Pubitemid 39481936)
105. Schröder M., Kaufman R. J., The mammalian unfolded protein response. Annual Review of Biochemistry 2005 74 739 789 2-s2.0-22244446505 10.1146/annurev.biochem.73.011303.074134 (Pubitemid 40995523)
106. Bernales S., Papa F. R., Walter P., Intracellular signaling by the unfolded protein response. Annual Review of Cell and Developmental Biology 2006 22 487 508 2-s2.0-33751159209 10.1146/annurev.cellbio.21.122303.120200
107. Vitale A., Ceriotti A., Protein quality control mechanisms and protein storage in the endoplasmic reticulum. A conflict of interests? Plant Physiology 2004 136 3 3420 3426 2-s2.0-16544394131 10.1104/pp.104.050351 (Pubitemid 41075781)
108. Vitale A., Boston R. S., Endoplasmic reticulum quality control and the unfolded protein response: insights from plants. Traffic 2008 9 10 1581 1588 2-s2.0-51849097747 10.1111/j.1600-0854.2008.00780.x
109. Rutkowski D. T., Hegde R. S., Regulation of basal cellular physiology by the homeostatic unfolded protein response. Journal of Cell Biology 2010 189 5 783 794 2-s2.0-77953153048 10.1083/jcb.201003138
110. Neumann V., Multiple plasma-cell myeloma with crystalline deposits in the tumour cells and in the kidneys. The Journal of Pathology and Bacteriology 1949 61 2 165 169 2-s2.0-0002825039
111. Jones D., Bhatia V. K., Krausz T., Pinkus G. S., Crystal-storing histiocytosis: a disorder occurring in plasmacytic tumors expressing immunoglobulin kappa light chain. Human Pathology 1999 30 12 1441 1448 2-s2.0-0033427260 (Pubitemid 30032920)
112. Schillinger F., Hopfner C., Montagnac R., Milcent T., IgG kappa light-chain myeloma with Fanconi's syndrome and crystalline inclusions. Immunohistochemical and ultrastructural studies. Presse Medicale 1993 22 14 675 679 2-s2.0-0027336026 (Pubitemid 23147165)
113. Messiaen T., Deret S., Mougenot B., Bridoux F., Dequiedt P., Dion J. J., Makdassi R., Meeus F., Pourrat J., Touchard G., Vanhille P., Zaoui P., Aucouturier P., Ronco P. M., Adult Fanconi syndrome secondary to light chain gammopathy: clinicopathologic heterogeneity and unusual features in 11 patients. Medicine 2000 79 3 135 154 2-s2.0-17044458969 10.1097/00005792-200005000-00002 (Pubitemid 30327529)
114. Toly-Ndour C., Peltier J., Piedagnel R., Acute renal failure with lambda light chain-derived crystals in a patient with IgD myeloma. Nephrology, Dialysis, Transplantation 2011 26 3057 3059
115. Thorner P. S., Bedard Y. C., Fernandes B. J., -Light-chain nephropathy with Fanconi's syndrome. Archives of Pathology and Laboratory Medicine 1983 107 12 654 657 2-s2.0-0021083172
116. Rocca A., Khamlichi A. A., Touchard G., Mougenot B., Ronco P., Denoroy L., Deret S., Preud'Homme J. L., Aucouturier P., Cogne M., Sequences of V I subgroup light chains in Fanconi's syndrome: light chain V region gene usage restriction and peculiarities in myeloma-associated Fanconi's syndrome. Journal of Immunology 1995 155 6 3245 3252 2-s2.0-0028984139
117. Bridoux F., Sirac C., Hugue V., Decourt C., Thierry A., Quellard N., Abou-Ayache R., Goujon J. M., Cogné M., Touchard G., Fanconi's syndrome induced by a monoclonal V 3 light chain in Waldenström's macroglobulinemia. American Journal of Kidney Diseases 2005 45 4 749 757 2-s2.0-20144388799 10.1053/j.ajkd.2004.12.020 (Pubitemid 40460763)
118. Déret S., Denoroy L., Lamarine M., Vidal R., Mougenot B., Frangione B., Stevens F. J., Ronco P. M., Aucouturier P., Kappa light chain-associated Fanconi's syndrome: molecular analysis of monoclonal immunoglobulin light chains from patients with and without intracellular crystals. Protein Engineering 1999 12 4 363 369 2-s2.0-17144454246 (Pubitemid 29209948)
119. Aucouturier P., Bauwens M., Khamlichi A. A., Denoroy L., Spinelli S., Touchard G., Preud'homme J. L., Cogne M., Monoclonal Ig L chain and L chain V domain fragment crystallization in myeloma-associated Fanconi's syndrome. Journal of Immunology 1993 150 8 I 3561 3568 2-s2.0-0027207650 (Pubitemid 23129737)
120. Leboulleux M., Lelongt B., Mougenot B., Touchard G., Makdassi R., Rocca A., Noel L. H., Ronco P. M., Aucouturier P., Protease resistance and binding of Ig light chains in myeloma-associated tubulopathies. Kidney International 1995 48 1 72 79 2-s2.0-0028997093
121. Terashima K., Takahashi K., Kojima M., e t al., Kappa-type light chain crystal storage histiocytosis. Acta Pathologica Japonica 1978 28 1 111 138 2-s2.0-0018097512 (Pubitemid 8294934)
122. Yamamoto T., Hishida A., Honda N., Ito I., Shirasawa H., Nagase M., Crystal-storing histiocytosis and crystalline tissue deposition in multiple myeloma. Archives of Pathology and Laboratory Medicine 1991 115 4 351 354 2-s2.0-0025854427
123. Dogan S., Barnes L., Cruz-Vetrano W. P., Crystal-storing histiocytosis: report of a case, review of the literature (80 cases) and a proposed classification. Head and Neck Pathology 2012 6 111 120
124. Lebeau A., Zeindl-Eberhart E., Müller E. C., Müller-Höcker J., Jungblut P. R., Emmerich B., Löhrs U., Generalized crystal-storing histiocytosis associated with monoclonal gammopathy: molecular analysis of a disorder with rapid clinical course and review of the literature. Blood 2002 100 5 1817 1827 2-s2.0-0036720517 (Pubitemid 34925162)
125. El Hamel C., Thierry A., Trouillas P., Bridoux F., Carrion C., Quellard N., Goujon J. M., Aldigier J. C., Gombert J. M., Cogné M., Touchard G., Crystal-storing histiocytosis with renal Fanconi syndrome: pathological and molecular characteristics compared with classical myeloma-associated Fanconi syndrome. Nephrology Dialysis Transplantation 2010 25 9 2982 2990 2-s2.0-77956246123 10.1093/ndt/gfq129
126. Schoengen A., Schreiner T., Anselstetter V., Binder T., Galle J., Weber L., Heimpel H., Cryocrystalglobulinemia: pH-dependent precipitation of a monoclonal IgG-kappa-immunoglobulin. Blut 1989 58 5 255 260 2-s2.0-0024397434 (Pubitemid 19143324)
127. Schaefer H. E., Gammopathy-related crystal-storing histiocytosis, pseudo- and pseudo-pseudo-Gaucher cells: critical commentary and mini-review. Pathology Research and Practice 1996 192 11 1152 1162 2-s2.0-0030484499
128. Montoyo H. P., Vaccaro C., Hafner M., Ober R. J., Mueller W., Ward E. S., Conditional deletion of the MHC class l-related receptor FcRn reveals the sites of IgG homeostasis in mice. Proceedings of the National Academy of Sciences of the United States of America 2009 106 8 2788 2793 2-s2.0-62449200475 10.1073/pnas.0810796106
129. Akilesh S., Christianson G. J., Roopenian D. C., Shaw A. S., Neonatal FcR expression in bone marrow-derived cells functions to protect serum IgG from catabolism. Journal of Immunology 2007 179 7 4580 4588 2-s2.0-39549088649
130. Wang W., Lu P., Fang Y., Monoclonal antibodies with identical Fc sequences can bind to FcRn differentially with pharmacokinetic consequences. Drug Metabolism and Disposition 2011 39 1469 1477
131. Merlini G., Stone M. J., Dangerous small B-cell clones. Blood 2006 108 8 2520 2530 2-s2.0-33750616035 10.1182/blood-2006-03-001164
132. Glenner G. G., Terry W., Harada M., Isersky C., Page D., Amyloid fibril proteins: proof of homology with immunoglobulin light chains by sequence analyses. Science 1971 172 3988 1150 1151 2-s2.0-0015219685
133. Merlini G., Bellotti V., Molecular mechanisms of amyloidosis. The New England Journal of Medicine 2003 349 6 583 596 2-s2.0-0042709605 10.1056/NEJMra023144 (Pubitemid 36951371)
134. Isobe T., Osserman E. F., Patterns of amyloidosis and their association with plasma-cell dyscrasia, monoclonal immunoglobulins and Bence-Jones proteins. The New England Journal of Medicine 1974 290 9 473 477 2-s2.0-0016403647
135. Perfetti V., Casarini S., Palladini G., Vignarelli M. C., Klersy C., Diegoli M., Ascari E., Merlini G., Analysis of V -J expression in plasma cells from primary (AL) amyloidosis and normal bone marrow identifies 3r ( III) as a new amyloid-associated germline gene segment. Blood 2002 100 3 948 953 2-s2.0-0036682487 10.1182/blood-2002-01-0114 (Pubitemid 34832622)
136. Solomon A., Frangione B., Franklin E. C., Bence Jones proteins and light chains of immunoglobulins. Preferential association of the V( VI) subgroup of human light chains with amyloidosis AL(). The Journal of Clinical Investigation 1982 70 2 453 460 2-s2.0-0019951737 (Pubitemid 12042646)
137. Comenzo R. L., Zhang Y., Martinez C., Osman K., Herrera G. A., The tropism of organ involvement in primary systemic amyloidosis: contributions of Ig VL germ line gene use and clonal plasma cell burden. Blood 2001 98 3 714 720 2-s2.0-0035437144 10.1182/blood.V98.3.714
138. Steinrauf L. K., Chiang M. Y., Shiuan D., Molecular structure of the amyloid-forming protein kappa I Bre. Journal of Biochemistry 1999 125 2 422 429 2-s2.0-0033032082 (Pubitemid 29112311)
139. Abraham R. S., Geyer S. M., Price-Troska T. L., Allmer C., Kyle R. A., Gertz M. A., Fonseca R., Immunoglobulin light chain variable (V) region genes influence clinical presentation and outcome in light chain-associated amyloidosis (AL). Blood 2003 101 10 3801 3808 2-s2.0-0038264427 10.1182/blood-2002-09-2707 (Pubitemid 36857849)
140. Stevens F. J., Myatt E. A., Chang C. H., Westholm F. A., Eulitz M., Weiss D. T., Murphy C., Solomon A., Schiffer M., A molecular model for self-assembly of amyloid fibrils: immunoglobulin light chains. Biochemistry 1995 34 34 10697 10702 2-s2.0-0029094974 10.1021/bi00034a001
141. Stevens P. W., Raffen R., Hanson D. K., Deng Y. L., Berrios-Hammond M., Westholm F. A., Murphy C., Eulitz M., Wetzel R., Solomon A., Schiffer M., Stevens F. J., Recombinant immunoglobulin variable domains generated from synthetic genes provide a system for in vitro characterization of light-chain amyloid proteins. Protein Science 1995 4 3 421 432 2-s2.0-0028969576
142. Pokkuluri P. R., Solomon A., Weiss D. T., Stevens F. J., Schiffer M., Tertiary structure of human 6 light chains. Amyloid 1999 6 3 165 171 2-s2.0-0032820889 (Pubitemid 29483007)
143. Helms L. R., Wetzel R., Specificity of abnormal assembly in immunoglobulin light chain deposition disease and amyloidosis. Journal of Molecular Biology 1996 257 1 77 86 2-s2.0-0029966282 10.1006/jmbi.1996.0148 (Pubitemid 26114019)
144. Alim M. A., Yamaki S., Hossain S., Takeda K., Kozima M., Izumi T., Takashi I., Shinoda T., Structural relationship of -type light chains with AL amyloidosis: multiple deletions found in a V IV protein. Clinical and Experimental Immunology 1999 118 3 344 348 2-s2.0-0032693531 10.1046/j.1365-2249.1999.00939.x
145. Bellotti V., Mangione P., Merlini G., Review: immunoglobulin light chain amyloidosis-the archetype of structural and pathogenic variability. Journal of Structural Biology 2000 130 2-3 280 289 2-s2.0-0033855656 10.1006/jsbi.2000.4248
146. Hurle M. R., Helms L. R., Li L., Chan W., Wetzel R., A role for destabilizing amino acid replacements in light-chain amyloidosis. Proceedings of the National Academy of Sciences of the United States of America 1994 91 12 5446 5450 2-s2.0-0028305304 10.1073/pnas.91.12.5446 (Pubitemid 24174344)
147. Wall J., Schell M., Murphy C., Hrncic R., Stevens F. J., Solomon A., Thermodynamic instability of human 6 light chains: correlation with fibrillogenicity. Biochemistry 1999 38 42 14101 14108 2-s2.0-0345426278 10.1021/bi991131j (Pubitemid 29504243)
148. Raffen R., Dieckman L. J., Szpunar M., Wunschl C., Pokkuluri P. R., Dave
149. Kim Y. S., Wall J. S., Meyer J., Murphy C., Randolph T. W., Manning M. C., Solomon A., Carpenter J. F., Thermodynamic modulation of light chain amyloid fibril formation. Journal of Biological Chemistry 2000 275 3 1570 1574 2-s2.0-0034695564 10.1074/jbc.275.3.1570 (Pubitemid 30060770)
150. Eulitz M., Weiss D. T., Solomon A., Immunoglobulin heavy-chain-associated amyloidosis. Proceedings of the National Academy of Sciences of the United States of America 1990 87 17 6542 6546 2-s2.0-0025114431
151. Solomon A., Weiss D. T., Murphy C., Primary amyloidosis associated with a novel heavy-chain fragment (AH amyloidosis). American Journal of Hematology 1994 45 2 171 176 2-s2.0-0028273425 (Pubitemid 24092587)
152. Buxbaum J., Gallo G., Nonamyloidotic monoclonal immunoglobulin deposition disease: light- chain, heavy-chain, and light- and heavy-chain deposition diseases. Hematology/Oncology Clinics of North America 1999 13 6 1235 1248 2-s2.0-0033372474 (Pubitemid 30017397)
153. Buxbaum J., Mechanisms of disease: monoclonal immunoglobulin deposition. Hematology/Oncology Clinics of North America 1992 6 2 323 346 2-s2.0-0026585875
154. Ganeval D., Noel L. H., Preud Homme J. L., Light-chain deposition disease: its relation with AL-type amyloidosis. Kidney International 1984 26 1 1 9 2-s2.0-0021636859 (Pubitemid 14060581)
155. Denoroy L., Deret S., Aucouturier P., Overrepresentation of the V (IV) subgroup in light chain deposition disease. Immunology Letters 1994 42 1-2 63 66 2-s2.0-0028168934 10.1016/0165-2478(94)90036-1
156. Khamlichi A. A., Rocca A., Touchard G., Aucouturier P., Preud'Homme J. L., Cogne M., Role of light chain variable region in myeloma with light chain deposition disease: evidence from an experimental model. Blood 1995 86 10 3655 3659 2-s2.0-0028834450
157. Khamlichi A. A., Aucouturier P., Silvain C., Bauwens M., Touchard G., Preud'Homme J. L., Nau F., Cogne M., Primary structure of a monoclonal chain in myeloma with light chain deposition disease. Clinical and Experimental Immunology 1992 87 1 122 126 2-s2.0-0026599691
158. Cogne M., Preud'homme J. L., Bauwens M., Touchard G., Aucouturier P., Structure of a monoclonal kappa chain of the V ( (IV)) subgroup in the kidney and plasma cells in light chain deposition disease. Journal of Clinical Investigation 1991 87 6 2186 2190 2-s2.0-0025944664
159. Decourt C., Cogné M., Rocca A., Structural peculiarities of a truncated Y (III) immunoglobulin light chain in myeloma with light chain deposition disease. Clinical and Experimental Immunology 1996 106 2 357 361 2-s2.0-0029832842 (Pubitemid 26359905)
160. Rocca A., Khamlichi A. A., Aucouturier P., Noel L. H., Denoroy L., Preud'homme J. L., Cogne M., Primary structure of a variable region of the V( I) subgroup (ISE) in light chain deposition disease. Clinical and Experimental Immunology 1993 91 3 506 509 2-s2.0-0027509410 (Pubitemid 23074160)
161. Déret S., Chomilier J., Huang D. B., Preud'homme J. L., stevens F. J., Aucouturier P., Molecular modeling of immunoglobulin light chains implicates hydrophobic residues in non-amyloid light chain deposition disease. Protein Engineering 1997 10 10 1191 1197 2-s2.0-0345136937 (Pubitemid 28046179)
162. Prelli F., Frangione B., Franklin's disease: Ig γ 2 H chain mutant BUR. Journal of Immunology 1992 148 3 949 952 2-s2.0-0026555251
163. Aucouturier P., Khamlichi A. A., Touchard G., Justrabo E., Cogne M., Chauffert B., Martin F., Preud'homme J. L., Brief report: heavy-chain deposition disease. The New England Journal of Medicine 1993 329 19 1389 1393 2-s2.0-0027443918 10.1056/NEJM199311043291905 (Pubitemid 23317349)
164. Kambham N., Markowitz G. S., Appel G. B., Kleiner M. J., Aucouturier P., D'Agati V. D., Heavy chain deposition disease: the disease spectrum. American Journal of Kidney Diseases 1999 33 5 954 962 2-s2.0-0032929888 (Pubitemid 29214696)
165. Khamlichi A. A., Aucouturier P., Preud'Homme J. L., Cogne M., Structure of abnormal heavy chains in human heavy-chain-deposition disease. European Journal of Biochemistry 1995 229 1 54 60 2-s2.0-0028939110 10.1111/j.1432-1033. 1995.tb20436.x
166. Daliani D., Weber D., Alexanian R., Light-heavy chain deposition disease progressing to multiple myeloma. American Journal of Hematology 1995 50 4 296 298 2-s2.0-0029621914 10.1002/ajh.2830500413 (Pubitemid 26008882)
167. Lin J., Markowitz G. S., Valeri A. M., Kambhan N., Sherman W. H., Appel G. B., D'Agati V. D., Renal monoclonal immunoglobulin deposition disease: the disease spectrum. Journal of the American Society of Nephrology 2001 12 7 1482 1492 2-s2.0-0034911594 (Pubitemid 32666331)
168. Buxbaum J. N., Chuba J. V., Hellman G. C., Solomon A., Gallo G. R., Monoclonal immunoglobulin deposition disease: light chain and light and heavy chain deposition diseases and their relation to light chain amyloidosis. Clinical features, immunopathology, and molecular analysis. Annals of Internal Medicine 1990 112 6 455 464 2-s2.0-0025259913 (Pubitemid 20098527)
169. Ronco P., Plaisier E., Aucouturier P., Monoclonal immunoglobulin light and heavy chain deposition diseases: molecular models of common renal diseases. Contributions to Nephrology 2011 169 221 231 2-s2.0-79551501148 10.1159/000314778
170. Shihabi Z. K., Cryoglobulins: an important but neglected clinical test. Annals of Clinical and Laboratory Science 2006 36 4 395 408 2-s2.0-33751249357 (Pubitemid 44786686)
171. Modarressi A., Kuriyan M., Harvey G., Strair R., Heat insoluble cryoglobulin associated with gangrene in multiple myeloma. Journal of Clinical Apheresis 2003 18 4 190 193 2-s2.0-0346156115 10.1002/jca.10073 (Pubitemid 38036676)
172. Ishimura E., Nishizawa Y., Shoji S., Okumura M., Nishitani H., Kim-C. W., Watanabe Y., Wakasa K., Morii H., Kashgarian M., Heat-insoluble cryoglobulin in a patient with essential type I cryoglobulinemia and massive cryoglobulin-occlusive glomerulonephritis. American Journal of Kidney Diseases 1995 26 4 654 657 2-s2.0-0029149878
173. Wintrobe N. M., Buell M. V., Hypreproteinemia associated with multiple myeloma with report of case in which extraordinary hyperproteinemia was associated with thrombosis of retinal veins and symptom suggesting Raynauds disease. Bulletin of the Johns Hopkins Hospital 1933 52 156
174. Lerner A. B., Barnum C. P., Watson C. J., Studies of cryoglobulins the spontaneous precipitation of protein from serum at 5 degrees C in various disease states. The American Journal of the Medical Sciences 1947 214 416 421
175. Meltzer M., Franklin E. C., Cryoglobulinemia-A study of twenty-nine patients. I. IgG and IgM cryoglobulins and factors affecting cryoprecipitability. The American Journal of Medicine 1966 40 6 828 836 2-s2.0-0013920228
176. Brouet J. C., Clauvel J. P., Danon F., Biologic and clinical significance of cryoglobulins. A report of 86 cases. American Journal of Medicine 1974 57 5 775 788 2-s2.0-0016262898
177. Dammacco F., Miglietta A., Lobreglio G., Bonomo L., Cryoglobulins and pyroglobulins: an overview. La Ricerca in Clinica e in Laboratorio 1986 16 2 247 267 2-s2.0-0022705313 10.1007/BF02909348
178. Cream J. J., Cryoglobulins in vasculitis. Clinical and Experimental Immunology 1972 10 1 117 126 2-s2.0-0015255650
179. Ramos-Casals M., Stone J. H., Cid M. C., Bosch X., The Cryoglobulinaemias. The Lancet 2012 379 348 360
180. Alpers C. E., Smith K. D., Cryoglobulinemia and renal disease. Current Opinion in Nephrology and Hypertension 2008 17 3 243 249 2-s2.0-42149162826 10.1097/MNH.0b013e3282f8afe2 (Pubitemid 351535926)
181. Middaugh C. R., Gerber-Jenson B., Hurvitz A., Physicochemical characterization of six monoclonal cryoimmunoglobulins: possible basis for cold-dependent insolubility. Proceedings of the National Academy of Sciences of the United States of America 1978 75 7 3440 3444 2-s2.0-0342526327 (Pubitemid 8395088)
182. Aizawa Y., Zawadzki Z. A., Monoclonal IgG1 immunoglobulinaemia with strictly pH dependent cryoprecipitability. Clinical and Experimental Immunology 1979 37 2 267 275 2-s2.0-0018361916 (Pubitemid 9234403)
183. Nishimura Y., Nakamura H., Human monoclonal cryoimmunoglobulins. I. Molecular properties of IgG3 (Jir protein) and the cryo-coprecipitability of its molecular fragments by papain. Journal of Biochemistry 1984 95 1 255 265 2-s2.0-0021322573 (Pubitemid 14177973)
184. Lawson E. Q., Brandau D. T., Trautman P. A., Aziz S. E., Middaugh C. R., Kinetics of the precipitation of cryoimmunoglobulins. Molecular Immunology 1987 24 9 897 905 2-s2.0-0023196484 (Pubitemid 17149494)
185. Wang Y., Lomakin A., Hideshima T., Pathological crystallization of human immunoglobulins. Proceedings of the National Academy of Sciences of the United States of America 2012 109 13359 13361
186. Podell D. N., Packman C. H., Maniloff J., Abraham G. N., Characterization of monoclonal IgG cryoglobulins: fine-structural and morphological analysis. Blood 1987 69 2 677 681 2-s2.0-0023157851 (Pubitemid 17022046)
187. Putnam F. W., Abnormal human serum globulins. II. Physical constants and amino end groups. The Journal of Biological Chemistry 1958 233 6 1448 1454 2-s2.0-70449237119
188. Cummings N. A., Decreased tyrosine/tryptophan ratio in a 6.6S cryoglobulin, as determined by a spectrophotometric technique. Biochemical and Biophysical Research Communications 1968 33 1 165 171 2-s2.0-0014409908
189. Uki J., Young C. A., Suzuki T., A 22S cryomacroglobulin with antibody like activity. I. Physico chemical characterization and modification of its cryoproperties. Molecular Immunology 1974 11 11 729 740 2-s2.0-0016123787
190. Wang A. C., Wells J. V., Fudenberg H. H., Gergely J., Chemical analyses of cryoglobulins. Molecular Immunology 1974 11 7 341 345 2-s2.0-0016222480 10.1016/0161-5890(74)90085-6
191. Abdelmoula M., Spertini F., Shibata T., Gyotoku Y., Luzuy S., Lambert P. H., Izui S., IgG3 is the major source of cryoglobulins in mice. Journal of Immunology 1989 143 2 526 532 2-s2.0-0024403599 (Pubitemid 19191547)
192. Panka D. J., Salant D. J., Jacobson B. A., Minto A. W., Marshak-Rothstein A., The effect of V(H) residues 6 and 23 on IgG3 cryoprecipitation and glomerular deposition. European Journal of Immunology 1995 25 1 279 284 2-s2.0-0028985386 10.1002/eji.1830250146
193. Wang A. C., Molecular basis for cryoprecipitation. Springer Seminars in Immunopathology 1988 10 1 21 34 2-s2.0-0023678332
194. Kuroda Y., Kuroki A., Kikuchi S., Funase T., Nakata M., Izui S., A critical role for sialylation in cryoglobulin activity of marine IgG3 monoclonal antibodies. Journal of Immunology 2005 175 2 1056 1061 2-s2.0-23244454433 (Pubitemid 41094991)
195. Pruzanski W., Jancelewicz Z., Underdown B., Immunological and physicochemical studies of IgA1() cryogelglobulinaemia. Clinical and Experimental Immunology 1973 15 2 181 191 2-s2.0-0015857330
196. Saha A., Chowdhury P., Sambury S., Smart K., Rose B., Studies on cryoprecipitation. IV. Enzymic fragments of a human cryoglobulin. Journal of Biological Chemistry 1970 245 10 2730 2736 2-s2.0-0014962103
197. Vialtel P., Kells D. I. C., Pinteric L., Nucleation-controlled polymerization of human monoclonal immunoglobulin G cryoglobulins. Journal of Biological Chemistry 1982 257 7 3811 3818 2-s2.0-0019997930 (Pubitemid 12077157)
198. Middaugh C. R., Kehoe J. M., Prystowsky M. B., Molecular basis for temperature-dependent insolubility of cryoglobulins. IV. Structural studies of the IgM monoclonal cryoglobulin McE. Molecular Immunology 1978 15 3 171 187 2-s2.0-0018090929 10.1016/0161-5890(78)90146-3 (Pubitemid 8308828)
199. Andersen B. R., Tesar J. T., Schmid F. R., Haisty W. K., Hartz W. H., Biological and physical properties of a human m-cryoglobulin and its monomer subunit. Clinical and Experimental Immunology 1971 9 6 795 807 2-s2.0-0015189567
200. Saluk P. H., Clem W., Studies on the cryoprecipitation of a human IgG3 cryoglobulin: the effects of temperature induced conformational changes on the primary interaction. Molecular Immunology 1975 12 1 29 37 2-s2.0-0016434337
201. Scoville C. D., Abraham G. N., Turner D. H., Spectroscopic and kinetic analysis of a monoclonal IgG cryoglobulin. Effect of mild reduction on cryoprecipitation. Biochemistry 1979 18 12 2610 2615 2-s2.0-0018357674 (Pubitemid 9203286)
202. Dotten D. A., Pruzanski W., Olin J., Brown T. C., Cryocrystalglobulinemia. Canadian Medical Association Journal 1976 114 10 909 912 2-s2.0-0017065188
203. Papo T., Musset L., Bardin T., Bucki B., Jorgensen C., Dion E., Quillard A., De Gennes C., Sany J., Godeau P., Piette J. C., Cryocrystalglobulinemia as a cause of systemic vasculopathy and widespread erosive arthropathy. Arthritis and Rheumatism 1996 39 2 335 340 2-s2.0-13344282086 10.1002/art.1780390225 (Pubitemid 26065277)
204. Ball N. J., Wickert W., Marx L. H., Thaell J. F., Crystalglobulinemia syndrome. A manifestation of multiple myeloma. Cancer 1993 71 1231 1234 (Pubitemid 23054911)
205. Rengers J. U., Touchard G., Decourt C., Deret S., Michel H., Cogné M., Heavy and light chain primary structures control IgG3 nephritogenicity in an experimental model for cryocrystalglobulinemia. Blood 2000 95 11 3467 3472 2-s2.0-0034210619 (Pubitemid 30428478)
206. Martin W. J., Mathieson D. R., Pyroglobulinemia (heat-coagulable globulin in the blood). Mayo Clinic Proceedings 1953 28 20 545 554 2-s2.0-12444293597
207. Ohno T., Furukawa H., Kanoh T., Uchino H., The physicochemical properties and the process of pyrogel formation of IgD pyroglobulin. Clinica Chimica Acta 1986 160 3 235 243 2-s2.0-0022974421 (Pubitemid 17182776)
208. Caulin-Glaser T., Prelli F., Franklin E. C., Structural studies on an IgM- pyroglobulin. Journal of Laboratory and Clinical Medicine 1982 99 6 845 851 2-s2.0-0019953204
209. Tichy M., Hrncir Z., Maly J., Monoclonal cryoglobulins and pyroglobulins. Neoplasma 1984 31 4 381 384 2-s2.0-0021182816 (Pubitemid 14046547)
210. Sugai S., IgA pyroglobulin, hyperviscosity syndrome and coagulation abnormality in a patient with multiple myeloma. Blood 1972 39 2 224 237 2-s2.0-0015292719
211. Gallango M. L., Suinaga R., Ramirez M., IgE pyroglobulinemia in multiple myeloma. Clinica Chimica Acta 1988 176 2 151 156 2-s2.0-0023733791
212. Zinneman H. H., Seal U. S., The role of hydrophobic bonding in the thermoprecipitation of a pyroglobulin. Revue Europeenne D'études Cliniques et Biologiques 1971 16 7 668 672 2-s2.0-0015100594
213. McCann S. R., Zinneman H. H., Oken M. M., Sinha A. A., IgM pyroglobulinemia with erythrocytosis presenting as hyperviscosity syndrome. II. Biochemical properties and mechanisms of pyrogel formation. American Journal of Medicine 1976 61 3 321 325 2-s2.0-0017142321
214. Watanabe A., Kitamura M., Shimizu M., Immunoglobulin A (IgA) with properties of both cryoglobulin and pyroglobulin. Clinica Chimica Acta 1974 52 2 231 237 2-s2.0-0016229814
215. Moriyama T., Torimoto Y., Kohgo Y., Ikeda H., Matsuno K., Immunochemical characterization of monoclonal protein in the serum of a patient with Waldenstrom's macroglobulinemia showing both pyroglobulin and cryoglobulin properties. Clinica Chimica Acta 2000 296 1-2 171 180 2-s2.0-0034051866 10.1016/S0009-8981(00)00257-6 (Pubitemid 30243149)
216. Chaparro-Riggers J., Liang H., DeVay R. M., Increasing serum half-life and extending cholesterol lowering in vivo by engineering antibody with pH-sensitive binding to PCSK9. The Journal of Biological Chemistry 2012 287 11090 11097
217. Igawa T., Ishii S., Tachibana T., Maeda A., Higuchi Y., Shimaoka S., Moriyama C., Watanabe T., Takubo R., Doi Y., Wakabayashi T., Hayasaka A., Kadono S., Miyazaki T., Haraya K., Sekimori Y., Kojima T., Nabuchi Y., Aso Y., Kawabe Y., Hattori K., Antibody recycling by engineered pH-dependent antigen binding improves the duration of antigen neutralization. Nature Biotechnology 2010 28 11 1203 1207 2-s2.0-78149320579 10.1038/nbt.1691
218. Chen J., Liu C. C., Li Q., Nowak C., Bu G., Wang J., Two structural and functional domains of MESD required for proper folding and trafficking of LRP5/6. Structure 2011 19 3 313 323 2-s2.0-79952470911 10.1016/j.str.2011.01.010
219. Lee D., Walsh J. D., Mikhailenko I., Yu P., Migliorini M., Wu Y., Krueger S., Curtis J. E., Harris B., Lockett S., Blacklow S. C., Strickland D. K., Wang Y. X., RAP uses a histidine switch to regulate its interaction with LRP in the ER and golgi. Molecular Cell 2006 22 3 423 430 2-s2.0-33744802244 10.1016/j.molcel.2006.04.011 (Pubitemid 44308133)
220. Dafforn T. R., Della M., Miller A. D., The molecular interactions of heat shock protein 47 (Hsp47) and their implications for collagen biosynthesis. Journal of Biological Chemistry 2001 276 52 49310 49319 2-s2.0-0035966068 10.1074/jbc.M108896200
221. Carter P. J., Potent antibody therapeutics by design. Nature Reviews Immunology 2006 6 5 343 357 2-s2.0-33646352962 10.1038/nri1837
222. Holliger P., Hudson P. J., Engineered antibody fragments and the rise of single domains. Nature Biotechnology 2005 23 9 1126 1136 2-s2.0-27144432842 10.1038/nbt1142 (Pubitemid 41486394)
223. Kipriyanov S. M., Le Gall F., Generation and production of engineered antibodies. Applied Biochemistry and Biotechnology B 2004 26 1 39 60 2-s2.0-0842330081 10.1385/MB:26:1:39 (Pubitemid 38174858)
224. Ewert S., Huber T., Honegger A., Plückthun A., Biophysical properties of human antibody variable domains. Journal of Molecular Biology 2003 325 3 531 553 2-s2.0-0037227517 10.1016/S0022-2836(02)01237-8 (Pubitemid 36062681)
225. Abboud N., Chow S. K., Saylor C., Janda A., Ravetch J. V., Scharff M. D., Casadevall A., A requirement for Fc γ R in antibody-mediated bacterial toxin neutralization. Journal of Experimental Medicine 2010 207 11 2395 2405 2-s2.0-78149323035 10.1084/jem.20100995
226. Janda A., Eryilmaz E., Nakouzi A., Cowburn D., Casadevall A., Variable region identical immunoglobulins differing in isotype express different paratopes. The Journal of Biological Chemistry 2012 287 35409 35417
227. Torres M., Casadevall A., The immunoglobulin constant region contributes to affinity and specificity. Trends in Immunology 2008 29 2 91 97 2-s2.0-38749103119 10.1016/j.it.2007.11.004
228. Tudor D., Yu H., Maupetit J., Isotype modulates epitope specificity, affinity, and antiviral activities of anti-HIV-1 human broadly neutralizing 2F5 antibody. Proceedings of the National Academy of Sciences of the United States of America 2012 109 12680 12685
229. Suzuki T., Ishii-Watabe A., Tada M., Kobayashi T., Kanayasu-Toyoda T., Kawanishi T., Yamaguchi T., Importance of neonatal FcR in regulating the serum half-life of therapeutic proteins containing the Fc domain of human IgG1: a comparative study of the affinity of monoclonal antibodies and Fc-fusion proteins to human neonatal FcR. Journal of Immunology 2010 184 4 1968 1976 2-s2.0-77949884124 10.4049/jimmunol.0903296
230. Kaneko E., Niwa R., Optimizing therapeutic antibody function: progress with fc domain engineering. BioDrugs 2011 25 1 1 11 2-s2.0-78651360674 10.2165/11537830-000000000-00000
231. Igawa T., Tsunoda H., Kuramochi T., Sampei Z., Ishii S., Hattori K., Engineering the variable region of therapeutic IgG antibodies. mAbs 2011 3 3 243 252 2-s2.0-79955665534 10.4161/mabs.3.3.15299
232. Taleb N., The Black Swan: The Impact of the Highly Improbable 2007 1st New York, NY, USA Random House