Natural protective glue protein, sericin bioengineered by silkworms: Potential for biomedical and biotechnological applications

Progress in Polymer Science (Oxford)

Volumn 33, Issue 10, 2008, Pages 998-1012

  Kundu, Subhas C ^a   Dash, Biraja C ^a   Dash, Rupesh ^a   Kaplan, David L ^b  

^a INDIAN INSTITUTE OF TECHNOLOGY   (India)

^b Tufts University   (United States)

Author keywords

Anticancer drugs; Biomaterial; Cosmetics; Fibroin; Sericin; Silk proteins

Indexed keywords

ADHESION; ADHESIVES; AMINES; AMINO ACIDS; APPLICATIONS; BIOLOGICAL MATERIALS; CARBON FIBER REINFORCED PLASTICS; CELL ADHESION; CELL CULTURE; DRUG DELIVERY; GLUES; GLUING; HYDROPHILICITY; ORGANIC ACIDS; PLATING; PROTEINS; SILK; TISSUE ENGINEERING;

ANTICANCER DRUGS; COSMETICS; FIBROIN; SERICIN; SILK PROTEINS;

FIBERS;

ADHESION; ADHESIVES; AMINES; AMINO ACIDS; COSMETICS; FIBERS; FIBROIN; GLUE; GLUING; ORGANIC ACIDS; PLATING; PROTEINS; SILK; WATER; WETTABILITY;

EID: 55649095103     PISSN: 00796700     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.progpolymsci.2008.08.002     Document Type: Review

References (174)

1. Geier P.W. The life history of codling moth, Cydia pomonella (L.) (Lepidoptera: Tortricidae), in the Australian capital territory. Aust J Zool 11 (1963) 323-367
2. Johnson C.D., Romero J., and Raimundez-Urrutia E. Ecology of Amblycerus crassipunctatus Ribeiro-Costa (Coleoptera: Bruchidae) in seeds of Humiriaceae, a new host family for bruchids, with an ecological comparison to other species of Amblycerus. Coleopts Bull 55 (2001) 37-48
3. Jones D. The endocrine basis for developmentally stationary prepupae in larvae of Trichoplusia ni pseudoparasitized by Chelonus insularis. J Comp Physiol B 155 (1985) 235-240
4. Kauffman W.C., and Kennedy G.G. Toxicity of allelochemicals from the wild insect-resistant tomato Lycopersicon hirsutum f. glabratum to Campoletis sonorensis, a parasitoid of Heliothis zea. J Chem Ecol 15 (1989) 2051-2060
5. Zhao H.P., Feng X.Q., Cui W.Z., and Zou F.Z. Mechanical properties of silkworm cocoon pelades. Eng Fract Mech 74 (2007) 1953-1962
6. Jolly M.S., Sen S.K., and Ahsan M.M. Tasar culture. 1st ed. (1974), Ambika Publishers, Mumbai
7. Vollrath F. Biology of spider silks. Int J Biol Macromol 24 (1999) 81-88
8. Altman G.H., Diaz F., Jakuba C., Calabro T., Horan R.L., Chen J., et al. Silk-based biomaterials. Biomaterials 24 (2003) 401-416
9. Kaplan D., Adams W.W., Farmer B., and Viney C. Silk polymers: materials science and biotechnology (1994), Wiley Publishers, New York
10. Kaplan D.L., Mello S.M., Arcidiacono S., Fossey S., Senecal K., and Muller W. Silk. In: McGrath K., and Kaplan D.L. (Eds). Protein based materials (1998), Birkhauser, Boston 103-131
11. Kaplan DL, Fossey S, Viney C, Muller W. Self-organization (assembly) in biosynthesis of silk fibers-a hierarchical problem. In: Aksay IA, Baer E, Sarika ya M, Tirrell DA, editors. Hierarchically structured materials. Materials Res Symp Proc 1992;255:19-29.
12. Vollrath F., and Knight D.P. Liquid crystalline spinning of spider silk. Nature 410 (2001) 541-548
13. Jolly M.S., and Sen S.K. Patterns of follicular imprints in egg shell-a species-specific character in Antheraea. Bull Entomol 10 (1969) 32-38
14. Jolly M.S., Narasimhanna M.N., and Wartkar V.B. Arrangement of tubercular setae in Antheraea species (Lepidoptera: Saturniidae). Entomologist 103 (1970) 18-23
15. Sinha A.K., Sinha R.K., Goel A.K., Sinha B.R., Sinha R.P., and Thangavelu K. A review on the breeding and genetic aspects of tropical tasar silkworm, Antheraea mylitta D. Proc Con Cytol Genet 4 (1994) 7-16
16. Souche Y.S., and Patole M. Sequence analysis of mitochondrial 16S ribosomal RNA gene fragment from seven mosquito species. J Biosci 25 (2000) 361-366
17. Tan Y.D., Wan C., Zhu Y., Lu C., Xiang Z., and Deng H.W. An amplified fragment length polymorphism map of the silkworm. Genetics 157 (2001) 1227-1284
18. Reddy K.D., Abraham E.G., and Nagaraju J. Microsatellites of silkworm, Bombyx mori: abundance, polymorphism and strain characterization. Genome 42 (1999) 1057-1065
19. Nagaraju J., Kathirvel M., Muthulakshmi M., Subbiah E.V., and Kumar L.D. FISSR-PCR: a simple and sensitive assay for high throughput genotyping and genetic mapping. Mol Cell Probes 16 (2002) 67-72
20. Mahendran B., Padhi B.K., Ghosh S.K., and Kundu S.C. Genetic variation in ecoraces of tropical tasar silkworm, Antheraea mylitta D. using RFLP technique. Curr Sci 90 (2005) 100-103
21. Mahendran B., Acharya C., Dash R., Ghosh S.K., and Kundu S.C. Repetitive DNA in tropical tasar silkworm Antheraea mylitta. Gene 370 (2006) 51-57
22. Mahendran B., Ghosh S.K., and Kundu S.C. Molecular phylogeny of silk producing insects based on internal transcribed spacer DNA1. J Biochem Mol Biol 39 (2006) 522-529
23. Mahendran B., Ghosh S.K., and Kundu S.C. Molecular phylogeny of silk-producing insects based on 16S ribosomal RNA and cytochrome oxidase subunit I genes. J Genet 85 (2006) 31-38
24. Saha M., and Kundu S.C. Molecular identification of tropical tasar silkworm (Antheraea mylitta) ecoraces with RAPD and SCAR markers. Biochem Genet 44 (2006) 72-85
25. Cheng T.C., Xia Q.Y., Qian J.F., Liu C., Lin Y., Zha X.F., et al. Mining single nucleotide polymorphism from EST data of silkworm, Bombyx mori, inbred strain Dazao. Insect Biochem Mol Biol 34 (2004) 523-530
26. Shimada T., Kurimoto Y., and Kobayashi M. Phylogenetic relationship of silkmoths inferred from sequence data of the arylophorin gene. Mol Phylogenet Evol 4 (1995) 223-234
27. Prasad M.D., Muthulakshmi M., Madhu M., Archak S., Mita K., and Nagaraju J. Survey and analysis of microsatellites in the silkworm, Bombyx mori: frequency, distribution, mutations, marker potential and their conservation in heterologous species. Genetics 169 (2005) 197-214
28. Li A., Zhao Q., Tang S., Zhang Z., Pan S., and Shen G. Molecular phylogeny of the domesticated silkworm, Bombyx mori, based on the sequences of mitochondrial cytochrome b genes. J Genet 84 (2005) 137-142
29. Evans WC. Trease and Evan's pharmacognosy. 14th ed. Saunders, London; 1996.
30. Jolly M.S., Sen S.K., Sonwalkar T.N., and Prasad G.K. Manuals on sericulture. FAO Agric Ser Bull 4 (1987) 1-8
31. Sinohara H., Asano Y., and Fukui A. Glycopeptides from silk fibroin of Bombyx mori. Biochim Biophys Acta 237 (1971) 273-279
32. Gamo T., Inokuchi T., and Laufer H. Polypeptides of fibroin and sericin secreted from the different section of the silk gland in Bombyx mori. Insect Biochem Mol Biol 7 (1977) 285-295
33. Prudhomme J.C., Couble P., Garel J.P., and Daillie J. Silk synthesis in V: Comprehensive insect physiology. Biochem Pharmacol 10 (1985) 571-594
34. Sprague K.U. The Bombyx mori silk proteins: characterization of large polypeptides. J Biochem 14 (1975) 925-931
35. Couble P., Moine A., Garel A., and Prudhomme J.C. Developmental variation of a non-fibroin mRNA of Bombyx mori silk gland, encoding a low molecular silk protein. Dev Biol 97 (1983) 398-407
36. Zhou C., Confalonieri F., Medina N., Zivanovic Y., Esnault C., Yang T., et al. Fine organization of Bombyx mori fibroin heavy chain gene. Nucleic Acids Res 28 (2000) 2413-2419
37. Kikuchi Y., Mori K., Suzuki S., Yamaguchi K., and Mizuno S. Structure of the Bombyx mori fibroin light chain-encoding gene: upstream sequence elements common to the light and heavy chain. Gene 110 (1992) 151-158
38. Tanaka K., Kajiyama N., Ishikura K., Waga S., Kikuchi A., Ohtomo K., et al. Determination of the side of disulfide linkage between heavy and light chains of fibroin produced by Bombyx mori. Biochim Biophys Acta 1432 (1999) 92-103
39. Couble P., Chevillard M., Moine A., Ravel-Chapuis P., and Prudhomme J.C. Structural organization of the P25 gene of Bombyx mori and comparative analysis of its 5′ flanking DNA with that of the fibroin gene. Nucleic Acids Res 13 (1985) 1801-1814
40. Chevillard M., Deleage G., and Couble P. Amino acid sequence and putative conformational characteristics of the 25 kDa silk protein of Bornbyx mori. Sericologia 26 (1986) 435-449
41. Chevillard M., Couble P., and Prudhomme J.C. Complete nucleotide sequence of the gene encoding the Bombyx mori silk protein P25 and predicted amino acid sequence of the protein. Nucleic Acids Res 14 (1986) 6341-6342
42. Shimura K., Kikuchi A., Ohotomo K., Katagata Y., and Hyodo A. Studies on silk fibroin of Bombyx mori-I. Fractionation of fibroin prepared from the posterior silk gland. J Biochem 80 (1976) 693-701
43. Shimura K., Kikuchi A., Katagata Y., and Ohotomo K. The occurrence of small component proteins in the cocoon fibroin of Bombyx mori. J Seric Sci Jap 51 (1982) 20-26
44. Maekawa H., and Suzuki Y. Repeated turn-off and turn-on of fibroin gene transcription during silk gland development of Bombyx mori. Dev Biol 78 (1980) 394-406
45. Kimura K., Oyama F., Ueda H., Mizuno S., and Shimura K. Molecular cloning of the fibroin light chain complementary DNA and its use in the study of the expression of the light chain gene in the posterior silk gland of Bombyx mori. Experientia 41 (1985) 1167-1171
46. Datta A., Ghosh A.K., and Kundu S.C. Purification and characterisation of fibroin from the tropical saturniid silkworm, Antheraea mylitta. Insect Biochem Mol Biol 31 (2001) 1013-1018
47. Lotz B., and Colonna-Cesari F. The chemical structure and the crystalline structures of Bombyx mori silk fibroin. Biochimie 61 (1979) 205-214
48. Jin H.J., and Kaplan D.L. Mechanism of silk processing in insects and spiders. Nature 424 (2003) 1057-1061
49. Sinohara H. Glycopeptides isolated from sericin of the silkworm, Bombyx mori. Comp Biochem Physiol 6311 (1979) 87-91
50. Tokutake S. Isolation of the smallest component of silk protein. Biochem J 187 (1980) 413-417
51. Takasu Y., Yamada H., and Tsubouchi K. Isolation of three main sericin components from the cocoon of the silkworm, Bombyx mori. Biosci Biotechnol Biochem 66 (2002) 2715-2718
52. Michaille J.J., Couble P., Prudhomme J.C., and Garel A. A single gene produces multiple sericin messenger RNAs in the silk gland of Bombyx mori. Biochimie 68 (1986) 1165-1173
53. Tsukada M., and Bertholon G. Preliminary study of the physicochemical characteristics of silk sericin. Bull Sci Inst Text Fr 10 (1981) 141-154
54. Zurovec M., Yang C., Kodroak D., and Sehnal F. Identification of a novel type of silk protein and regulation of its expression. J Biol Chem 273 (1998) 15423-15428
55. Ahmad R., Kamra A., and Hasnain S.E. Fibroin silk proteins from the nonmulberry silkworm Philosamia ricini are biochemically and immunochemically distinct from those of the mulberry silkworm Bombyx mori. DNA Cell Biol 23 (2004) 149-154
56. Dash R., Ghosh S.K., Kaplan D.L., and Kundu S.C. Purification and biochemical characterization of a 70 kDa sericin from tropical tasar silkworm, Antheraea mylitta. Comp Biochem Physiol B: Biochem Mol Biol 147 (2007) 129-134
57. Yamada H., and Tsubouchi K. Characterisation of silk proteins in the cocoon fibers of Cricula trifenestrata. Int J Wild Silkmoth Silk 6 (2001) 17-51
58. Dash R., Mukherjee S., and Kundu S.C. Isolation, purification and characterization of silk protein sericin from cocoon peduncles of tropical tasar silkworm, Antheraea mylitta. Int J Biol Macromol 38 (2006) 255-258
59. Sehnal F., and Akai H. Insects silk glands: their types, development and function, and effects of environmental factors and morphogenetic hormones on them. Int J Insect Morphol Embryol 19 (1990) 79-132
60. Michaille J.J., Garel A., and Prudhomme J.C. The expression of five middle silkgland genes is territorially regulated during the larval development of Bombyx mori. Insect Biochem Mol Biol 19 (1989) 19-27
61. Okamoto H., Ishikawa E., and Suzuki Y. Structural analysis of sericin genes. Homologies with fibroin gene in the 5′ flanking nucleotide sequences. J Biol Chem 257 (1982) 15192-15199
62. Garel D.G., and Prudhomme J.C. Structure and organization of the Bombyx mori sericin 1 gene and of the sericin 1 deduced from the sequence of the Ser 1B cDNA. Insect Biochem Mol Biol 27 (1997) 469-477
63. Couble P., Michaille J.J., Garel A., Couble M.L., and Prudhomme J.C. Developmental switches of sericin mRNA splicing in individual cells of Bombyx mori silk gland. Dev Biol 124 (1987) 431-440
64. Grzelak K. Control of expression of silk protein genes. Comp Biochem Physiol B: Biochem Mol Biol 110 (1995) 61-68
65. Ishikawa E., and Suzuki Y. Tissue- and stage-specific expression of sericin genes in the middle silk gland of Bombyx mori. Dev Growth Differ 27 (1985) 73-82
66. Hui C.C., Suzuki Y., Kikuchi Y., and Mizuno S. Homeodomain binding sites in the 5′ flanking region of the Bombyx mori silk fibroin light-chain gene. J Mol Biol 213 (1990) 395-398
67. Matsuno K., Takiya S., Hui C.C., Suzuki T., Fukuta M., Ueno K., et al. Transcriptional stimulation via SC site of Bombyx sericin-1 gene through an interaction with a DNA binding protein SGF-3. Nucleic Acids Res 19 (1990) 1853-1858
68. Fukuta M., Matsuno K., Hui C.C., Nagata T., Takiya S., Xu P.X., et al. Molecular cloning of a POU domain-containing factor involved in the regulation of the Bombyx sericin-1 gene. J Biol Chem 268 (1993) 19471-19475
69. Mach V., Takiya S., Ohno K., Handa H., Imai T., and Suzuki Y. Silk gland factor-1 involved in the regulation of Bombyx sericin-1 gene contains fork head motif. J Biol Chem 270 (1995) 9340-9346
70. Garel A., Nony P., and Prudhomme J.C. Structural features of mag, a gypsy-like retrotransposon of Bombyx mori, with unusual short terminal repeats. Genetica 93 (1994) 125-137
71. Hamada Y., Yamashita O., and Suzuki Y. Haemolymph control of sericin gene expression studied by organ transplantation. Cell Differ 20 (1987) 65-76
72. Takasu Y., Yamada H., Tamura T., Sezutsu H., Mita K., and Tsubouchi K. Identification and characterization of a novel sericin gene expressed in the anterior middle silk gland of the silkworm Bombyx mori. Insect Biochem Mol Biol 37 (2007) 1234-1240
73. Teramoto H., Kakazu A., and Asakura T. Native structure and degradation pattern of silk sericin studied by 13C NMR spectroscopy. Macromolecules 39 (2006) 6-8
74. Lucas F., and Rudall K.M. Comprehensive biochemistry 26B (1968), Elsevier Science Publishers, Amsterdam 475-558
75. Huang J., Valluzzi R., Bini E., Vernaglia B., and Kaplan D.L. Cloning, expression, and assembly of sericin-like protein. J Biochem 278 (2003) 6117-6123
76. Zhu L.J., Arai M., and Hirabayashi K. Gelation of silk sericin and physical properties of the gel. Nippon Sanshigaku Zasshi 64 (1995) 415-419
77. Wu J.H., Wang Z., and Xu S.Y. Preparation and characterization of sericin powder extracted from silk industry wastewater. Food Chem 103 (2007) 1255-1262
78. Teramoto H., and Miyazawa M. Molecular orientation of silk sericin film as revealed by ATR-infrared spectroscopy. Biomacromolecules 6 (2005) 2049-2057
79. Teramoto H., Nakajima K., and Takabayashi C. Preparation of elastic silk sericin hydrogel. Biosci Biotechnol Biochem 69 (2005) 845-847
80. Teramoto H., Kakazu A., Yamauchi K., and Asakura T. Role of hydroxyl side chains in Bombyx mori silk sericin in stabilizing its solid structure. Macromolecules 40 (2007) 1562-1569
81. Fabiani C., Pizzichini M., Spadoni M., and Zeddita G. Treatment of waste water from silk degumming processes for protein recovery and water reuse. Desalination 105 (1996) 1-9
82. Mandal B.B., and Kundu S.C. A novel method for dissolution and stabilization of non-mulberry silk gland protein fibroin using anionic surfactant sodium dodecyl sulfate. Biotechnol Bioeng 99 (2008) 1482-1489
83. Mandal B.B., and Kundu S.C. Non-bioengineered silk gland fibroin protein: characterization and evaluation of matrices for potential tissue engineering applications. Biotechnol Bioeng 100 (2008) 1237-1250
84. Zhang Y.Q. Applications of natural silk protein sericin in biomaterials. Biotechnol Adv 20 (2002) 91-100
85. Padamwar M.N., and Pawar A.P. Silk sericin and its application: a review. J Sci Ind Res India 63 (2004) 323-329
86. Voegeli R., Meier J., and Blust R. Sericin silk protein: unique structure and properties. Cosmet Toilet 108 (1993) 101-108
87. Yamada H, Fuha Y, Yuri O, Obayashi M, Arashima T. Collagen formation promoters containing sericin or its hydrolyzates and antiaging cosmetics. Jpn Kokai Tokkyo Koho, JP 10226653 A2; 1998. p. 8.
88. Ogawa A, Yamada H. Antiaging cosmetic containing sericin or hydrolysates and saccharomyces extracts. Jpn Kokai Tokkyo Koho Jap 11193210 A2; 1999. p. 9.
89. Henne W, Hoppe U. Light and screening composition. Ger Offen DE 3408406 A1; 1985. p. 14.
90. Padamwar MN, Daithankar AV, Pisal SS, Pawar AP. Evaluation of moisturizing efficiency of silk protein. II. Silk sericin. Sixty Second World Congress of FIP Nice; 2002.
91. Kirikawa M, Kasaharu T, Kishida K, Akiyama D. Silk protein micropowders for coating with excellent feeling, antistaticity and moisture absorbability and releasability and there manufacture. Jpn Kokai Tokkyo Koho Jap 2000044598 A2; 2000. p. 8.
92. Yasuda N, Yamada H, Nomura M. Sericin from silk as dermatitis inhibitor. Jpn Kokai Tokkyo Koho Jap 10245345 A2; 1998. p. 4.
93. Yoshioka M, Segawa A, Veda A, Omi S. UV absorbing compositions containing fine capsules. Jpn Kokai Tokkyo Koho Jap; 2001. p. 14.
94. Yamada H, Yamasaki K, Zozaki K. Nail cosmetics containing sericin. PCT Int Appl WO 2001015660 A1; 2001. p. 15.
95. Hoppe U, Koerbaecher K, Roeckl M. Hair and bath preparations containing sericin. Ger Offen DE 3233388 A1; 1984. p. 15.
96. Hata O. Cosmetics containing sericin hydrolysates. Jpn Kokai Tokkyo Koho Jap 62036308 A2; 1987. p. 7.
97. Engel W, Hoppe U. Aqueous hair preparations containing sericin and pelargonic acids. Ger Offen DE 3603595 A1; 1987. p. 4.
98. Yamada H, Yuri O. Sericin coated powders for cosmetics. Jpn Kokai Tokkyo Koho Jap 10226626 A2; 1998. p. 9.
99. Yamada H, Yamazuki K, Nozaki K. Skin moisturizing and conditioning cosmetics containing sericin and saccharides. Jpn Kokai Tokkyo Koho Jap 2001064148 A2; 2001. p. 6.
100. Sakamoto K, Yamakishi K. Sericin containing cleaning composition. Jpn Kokai Tokkyo Koho Jap 2000073090 A2; 2000. p. 4.
101. Miyashita T. Sweat and sebum absorbing cosmetics containing cellulose fibres. Jpn Kokai Tokkyo Koho Jap 11152206 A2; 1999. p. 3.
102. Panilaitis B., Altman G.H., Chen J., Jin H.J., Karageorgiou V., and Kaplan D.L. Macrophage responses to silk. Biomaterials 24 (2003) 3079-3085
103. Zaoming W., Codina R., Fernandez-Caldas E., and Lockey R.F. Partial characterization of the silk allergens in mulberry silk extract. J Allergy Clin Immunol 6 (1996) 237-241
104. Dewair M., Baur X., and Ziegler K. Use of immunoblot technique for detection of human IgE and IgG antibodies to individual silk proteins. J Allergy Clin Immunol 76 (1985) 537-542
105. Soong H.K., and Kenyon K.R. Adverse reactions to virgin silk sutures in cataract surgery. Ophthalmology 91 (1984) 479-483
106. Suzuki N., Fuzimura A., Nagai T., Mizumoto I., Itami T., Hatate H., et al. Antioxidative activity of animal and vegetable dietary fibers. Biofactors 21 (2004) 329-333
107. Kato N., Sato S., Yamanaka A., Yamada H., Fuwa N., and Nomura M. Silk protein, sericin, inhibits lipid peroxidation and tyrosinase activity. Biosci Biotechnol Biochem 62 (1998) 45-47
108. Bindu P.C., Jaisankar P., Hauer F., Gutzeit H.O., and Kundu S.C. Biological relevance of host plant-derived terpenoid in the cocoons of the tropical tasar silkworm Antheraea mylitta. Biochem Syst Ecol 34 (2006) 698-704
109. Zhaorigetu S., Yanaka N., Sasaki M., Watanabe H., and Kato N. Inhibitory effects of silk protein, sericin on UVB-induced acute damage and tumor promotion by reducing oxidative stress in the skin of hairless mouse. J Photochem Photobiol B 71 (2003) 11-17
110. Sasaki M. Silk protein, sericin, suppresses colon carcinogenesis induced by 1,2-dimethylhydrazine in mice. Oncol Rep 7 (2000) 1049-1052
111. Zhaorigetu S., Masahiro S., Watanabe H., and Kato N. Supplemental silk protein, sericin, suppresses colon tumorigenesis in 1,2-dimethylhydrazine-treated mice by reducing oxidative stress and cell proliferation. Biosci Biotechnol Biochem 65 (2001) 2181-2186
112. Dash R., Mandal M., Ghosh Sudip K., and Kundu S.C. Silk sericin protein of tropical tasar silkworm inhibits UVB induced apoptosis in human skin keratinocytes. Mol Cell Biochem 311 (2008) 111-119
113. Dash R., Acharya C., Bindu P.C., and Kundu S.C. Antioxidant potential of silk protein sericin against hydrogen peroxide-induced oxidative stress in skin fibroblasts. Biochem Mol Biol Rep 41 (2008) 236-241
114. Sasaki M., Yamada H., and Kato N. A resistant protein, sericin improves atropine-induced constipation in rats. Food Sci Tech Res 6 (2000) 280-283
115. Sasaki M., Yamada H., and Kato N. Consumption of silk protein, sericin elevates intestinal absorption of zinc, iron, magnesium and calcium in rats. Nutr Res 20 (2000) 1505-1511
116. Tamada Y., Sano M., Niwa K., Imai T., and Yoshino G. Sulfation of silk sericin and anticoagulant activity of sulfated sericin. J Biomater Sci Polym Ed 15 (2004) 971-980
117. Monti P., Freddi G., Arosio C., Tsukada M., Arai T., and Taddei P. Vibrational spectroscopic study of sulphated silk proteins. J Mol Struct 834-836 (2007) 202-206
118. Takeuchi A., Ohtsuki C., Kamitakahara M., Ogata S.L., Tanihara M., Miyazaki T., et al. Apatite deposition on silk sericin in a solution mimicking extracellular fluid: effects of fabrication process of sericin film and fluid. Key Eng Mater 254-256 (2004) 403-406
119. Takeuchi A., Ohtsuki C., Miyazaki T., Kamitakahara M., Ogata S.I., Yamazaki M., et al. Heterogeneous nucleation of hydroxyapatite on protein: structural effect of silk sericin. J Roy Soc Interface 2 (2005) 373-378
120. Morooka H., Fuwa N., and Osada K. Effects on sericin processed sportswear on physiological response and fatigue. Sen'i Gakkaishi 62 (2006) 48-53
121. Tsubouchi K. Occlusive dressing consisting essentially of silk fibroin and silk sericin and its production. Japan Patent 11-070160A; 1999.
122. Veronese F.M., and Morpurgo M. Bioconjugation in pharmaceutical chemistry. Farmaco 54 (1999) 497-516
123. Vicent M.J., and Duncan R. Polymer conjugates: nanosized medicines for treating cancer. Trends Biotechnol 24 (2006) 39-47
124. Zhang Y.Q., Tao M.L., Shen W.D., Zhou Y.Z., Ding Y., Ma Y., et al. Immobilization of l-asparaginase on the microparticles of the natural silk sericin protein and its characters. Biomaterials 25 (2004) 3751-3759
125. Zhang Y.Q., Tao M.L., Shen W.D., Mao J.P., and Chen Y.H. Synthesis of silk sericin peptides-l-asparaginase (SS-ASNase) bioconjugates and their characterization. J Chem Technol Biotechnol 81 (2006) 136-145
126. Zhang Y.Q., Ma Y., Xia Y.Y., Shen W.D., Mao J.P., and Xue R.Y. Silk sericin-insulin bioconjugates: synthesis, characterization and biological activity. J Control Release 115 (2006) 307-315
127. Anghileri A., Lantto R., Kruus K., Arosio C., and Freddi G. Tyrosinase-catalyzed grafting of sericin peptides onto chitosan and production of protein-polysaccharide bioconjugates. J Biotechnol 127 (2007) 508-519
128. Mathe G., Amiel J.L., Clarysse A., Hayat M., and Schwarzenberg L. The place of the l-asparaginase in the treatment of acute leukemias. Recent Results Cancer 33 (1970) 278-287
129. Jaffe N., Traggis D., Das L., Frauenberger G., Hann H.W., Kim B.S., et al. Favorable remission induction rate with twice weekly doses of l-asparaginase. Cancer Res 33 (1973) 1-4
130. Cho K.Y., Moon J.Y., Lee Y.W., Lee K.G., Yeo J.H., Kweon H.Y., et al. Preparation of self-assembled silk sericin nanoparticles. Int J Biol Macromol 32 (2003) 36-42
131. Wei D.Q., Li G.J., Tao J.L., Liu Z.H., and Zhang X.M. Investigation of the graft copolymerization of styrene onto silk sericin. Acta Polym Sin 6 (1989) 740-744
132. Yao Y.Q., Bian P.F., Chen W.X., Ling R.G., and Shen Z.Y. Synthesis and properties of degradable graft copolymer of vinyl acetate and sericin. Chem J Chinese U 24 (2003) 2327-2329
133. Nakamura K., and Hatakeyama H. Graft copolymerization of vinyl monomers on to sericin. Sen'i Gakkaishi 40 (1984) 327-331
134. Song Y., Jin Y., Sun J., and Wei D. Graft copolymerization of methyl acrylate onto silk sericin initiated by tert-butyl hydroperoxide. Polym Int 55 (2006) 1350-1354
135. Song Y., and Wei D. Preparation and characterization of graft copolymers of silk sericin and methyl methacrylate. Polym Polym Compos 14 (2006) 169-174
136. Cortez J., Anghieri A., Bonner P.L.R., Griffinc M., and Freddi G. Transglutaminase mediated grafting of silk proteins onto wool fabrics leading to improved physical and mechanical properties. Enzyme Microb Technol 40 (2006) 1698-1704
137. Yoshii F, Kume T, Makuuchi K, Sato F. Hydrogel composition containing silk protein. Japan Patent 2000-169736A; 2000.
138. Wang S., Goto Y., Ohkoshi Y., and Nagura M. Structures and physical properties of poly(vinyl alcohol)/sericin blend hydrogel membranes. J Seric Sci Jpn 67 (1998) 295-302
139. Nakamura K, Koga Y. Sericin-containing polymeric hydrous gel and method for producing the same. Japan Patent 2001-106794A; 2001.
140. Jun L., Yaw J., Li Y., Hirabayashi K., and Arai M. Studies on physical properties of sericin gel. Cnye Kexe 23 (1997) 47-52
141. Hirabayashi K., Arai M., and Chu L.J. Gelation of silk sericin. Nippon Sanshigaku Zasshi 58 (1989) 81-82
142. Hu G., and Zhu J. Characteristics and structure of gel with fibroin and sericin. Gongxueyuan Xuebao 14 (1997) 154-158
143. Zhu L.J., Hizahayashi K., and Aari M. Gelation of sericin and its structure and properties. Canye Kexue 17 (1991) 33-38
144. Padamwar M.N., and Pawar A.P. Preparation and evaluation of sericin gels containing choline salicylate. Indian Drugs 40 (2003) 526-531
145. Kweon H.Y., Yeo J.H., Lee K.G., Lee Y.W., Park Y.H., Nahm J.H., et al. Effects of poloxamer on the gelation of silk sericin. Macromol Rapid Commun 21 (2000) 1302-1305
146. Nagura M., Ohnishi R., Gitoh Y., and Ohkoshi Y. Structure and physical properties of cross-linked sericin membranes. J Seric Sci Jpn 70 (2001) 149-153
147. Xie R.J., Li M.J., Lu S.Z., Sheng W.H., and Xie Y.F. Preparation of sericin film and its cytocompatibility. Key Eng Mater 342-343 (2007) 241-244
148. Yang J., Zhu P., and Wu D. Surface pressure-area curves compression isotherm of sericin Langmuir monolayer. Surf Interface Anal 39 (2007) 375-376
149. Wu W., Li W., Wang L.Q., Tu K., and Sun W. Synthesis and characterization of pH- and temperature-sensitive silk sericin/poly(N-isopropylacrylamide) interpenetrating polymer networks. Polym Int 55 (2006) 513-519
150. Tao W., Li M., and Xie R. Preparation and structure of porous silk sericin materials. Macromol Mater Eng 290 (2005) 188-194
151. Ahn J.S., Choi H.K., Lee K.H., Nahm J.H., and Cho C.S. Novel mucoadhesive polymer prepared by template polymerization of acrylic acid in the presence of silk sericin. J Appl Polym Sci 80 (2001) 274-280
152. Minoura N., Aiba S., Higuchi M., Gotoh Y., Tsukada M., and Imai Y. Attachment and growth of fibroblast cells on silk fibroin. Biochem Biophys Res Commun 208 (1995) 511-516
153. Minoura N., Aiba S., Gotoh Y., Tsukada M., and Imai Y. Attachment and growth of cultured fibroblast cells on silk protein matrices. J Biomed Mater Res B 29 (1995) 1215-1221
154. Gotoh Y., Tsukada M., and Minoura N. Effect of the chemical modification of the arginyl residue in Bombyx mori silk fibroin on the attachment and growth of fibroblast cells. J Biomed Mater Res 39 (1998) 351-357
155. Inouye K., Kurokawa M., Nishikawa S., and Tsukada M. Use of Bombyx mori silk fibroin as a substratum for cultivation of animal cells. J Biochem Biophys Methods 37 (1998) 159-164
156. Sofia S., McCarthy M.B., Gronowicz G., and Kaplan D.L. Functionalized silk-based biomaterials for bone formation. J Biomed Mater Res 54 (2001) 139-148
157. Chen J., Altman G.H., Karageorgiou V., Horan R., Collette A., Volloch V., et al. Human bone marrow stromal cell and ligament fibroblast responses on RGD-modified silk fibers. J Biomed Mater Res A 67 (2003) 559-570
158. Karageorgiou V., Meinel L., Hofmann S., Malhotra A., Volloch V., and Kaplan D.L. Bone morphogenetic protein-2 decorated silk fibroin films induce osteogenic differentiation of human bone marrow stromal cells. J Biomed Mater Res A 71 (2004) 528-537
159. Meinel L., Fajardo R., Hofmann S., Langer R., Chen J., Snyder B., et al. Silk implants for the healing of critical size bone defects. Bone 37 (2005) 688-698
160. Kim H.J., Kim U.J., Vunjak-Novakovic G., Min B.H., and Kaplan D.L. Influence of macroporous protein scaffolds on bone tissue engineering from bone marrow stem cells. Biomaterials 26 (2005) 4442-4452
161. Wang Y., Blasioli D.J., Kim H.J., Kim H.S., and Kaplan D.L. Cartilage tissue engineering with silk scaffolds and human articular chondrocytes. Biomaterials 27 (2006) 4434-4442
162. Nagura M, Yamashita M, Ohtorii A, Gotoh Y, Ohkoshi Y, Teramoto A, et al. Cell attachment and growth on sericin membranes. Transactions-7th World Biomaterials Congress; 2004. p. 1207.
163. Tsubouchi K., Igarashi Y., Takasu Y., and Yamada H. Sericin enhances attachment of cultured human skin fibroblasts. Biosci Biotechnol Biochem 69 (2005) 403-405
164. Vepari Charu, and Kaplan D.L. Silk as a biomaterial. Prog Polym Sci 32 (2007) 991-1007
165. Terada S., Nishimura T., Sasaki M., Yamada H., and Miki M. Sericin, a protein derived from silkworms, accelerates the proliferation of several mammalian cell lines including a hybridoma. Cytotechnology 40 (2002) 3-12
166. Takahashi M., Tsujimoto K., Yamada H., Takagi H., and Nakamori S. The silk protein, sericin, protects against cell death caused by acute serum deprivation in insect cell culture. Biotechnol Lett 25 (2003) 1805-1809
167. Ogawa A., Terada S., Kanayama T., Miki M., Morikawa M., and Kimura T. Improvement of islet culture with sericin. J Biosci Bioeng 98 (2004) 217-219
168. Fraga D.W., Sabek O., Hathaway D.K., and Gaber O. A comparison of media supplements methods for the extended culture of human islet tissue. Transplantation 65 (1998) 1060-1066
169. Takahashi M., Tsujimoto K., Kato Y., Yamada H., Takagi H., and Nakamori S. A sericin-derived peptide protects Sf9 insect cells from death caused by acute serum deprivation. Biotechnol Lett 27 (2005) 893-897
170. Sasaki M., Kato Y., Yamada H., and Terada S. Development of a novel serum free freezing medium for mammalian cells using the silk protein sericin. Biotechnol Appl Biochem 42 (2005) 183-188
171. Tomita M., Munetsuna H., Sato T., Adachi T., Hino R., Hayashi M., et al. Transgenic silkworms produce recombinant human type III procollagen in cocoons. Nat Biotechnol 21 (2003) 52-56
172. Hino R., Tomita M., and Yoshizato K. The generation of germline transgenic silkworms for the production of biologically active recombinant fusion proteins of fibroin and human basic fibroblast growth factor. Biomaterials 27 (2006) 5715-5724
173. Ogawa S., Tomita M., Shimizu K., and Yoshizato K. Generation of a transgenic silkworm that secretes recombinant proteins in the sericin layer of cocoon: production of recombinant human serum albumin. J Biotechnol 128 (2007) 531-544
174. Tomita M., Hino R., Ogawa S., Iizuka M., Adachi T., Shimizu K., et al. A germline transgenic silkworm that secretes recombinant proteins in the sericin layer of cocoon. Transgenic Res 16 (2007) 449-465