Wet extrusion of fibronectin-fibrinogen cables for application in tissue engineering
A method for the wet extrusion of human plasma‐derived fibronectin–fibrinogen cables is described. Solutions of fibronectin and fibrinogen with and without sodium alginate and carboxymethylcellulose (CMC) are tested. The rheological properties of the protein solutions changed from Newtonian to shear...
Saved in:
Published in | Biotechnology and bioengineering Vol. 73; no. 4; pp. 295 - 305 |
---|---|
Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
New York
John Wiley & Sons, Inc
20.05.2001
Wiley |
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | A method for the wet extrusion of human plasma‐derived fibronectin–fibrinogen cables is described. Solutions of fibronectin and fibrinogen with and without sodium alginate and carboxymethylcellulose (CMC) are tested. The rheological properties of the protein solutions changed from Newtonian to shear thinning non‐Newtonian in the presence of small quantities of these additives, the apparent viscosity increased, and the extrusion properties of the protein solutions improved. Cables were prepared using a capillary with a diameter of 1 mm and overall length of 18 mm. Cable diameter was reduced to about 0.5 mm by drawing using a series of rollers. Cables prepared with sodium alginate were found to have suitable properties, and those made with CMC were sticky and difficult to handle. Solutions containing no sodium alginate required a minimum total protein concentration of about 70 mg/mL for extrusion. Extruded cables were prepared with solutions containing 140 mg/mL total protein with 12.9 mg/mL alginate (high protein), and 46 mg/mL total protein with 47.6 mg/mL of sodium alginate (high alginate). The mechanical strength of the extruded cables was within the range suitable for application in tissue engineering. Extrusion of the protein solutions into cables was achieved in a coagulation bath. Cables with a mechanical strength of approximately 30 N/mm2, suitable for wound repair and nerve regeneration applications, were prepared with a coagulation bath containing 0.25 M HCl, 2% CaCl2 at a pH of <0.9. These cables also had a large average elongation at break of 52%, and showed an increase in cable length after breakage (permanent set) of 20%, demonstrating the potential for drawing the cables down to a fine diameter. © 2001 John Wiley & Sons, Inc. Biotechnol Bioeng 73: 295–305, 2001. |
---|---|
AbstractList | A method for the wet extrusion of human plasma-derived fibronectin-fibrinogen cables is described. Solutions of fibronectin and fibrinogen with and without sodium alginate and carboxymethylcellulose (CMC) are tested. The rheological properties of the protein solutions changed from Newtonian to shear thinning non-Newtonian in the presence of small quantities of these additives, the apparent viscosity increased, and the extrusion properties of the protein solutions improved. Cables were prepared using a capillary with a diameter of 1 mm and overall length of 18 mm. Cable diameter was reduced to about 0.5 mm by drawing using a series of rollers. Cables prepared with sodium alginate were found to have suitable properties, and those made with CMC were sticky and difficult to handle. Solutions containing no sodium alginate required a minimum total protein concentration of about 70 mg/mL for extrusion. Extruded cables were prepared with solutions containing 140 mg/mL total protein with 12.9 mg/mL alginate (high protein), and 46 mg/mL total protein with 47.6 mg/mL of sodium alginate (high alginate). The mechanical strength of the extruded cables was within the range suitable for application in tissue engineering. Extrusion of the protein solutions into cables was achieved in a coagulation bath. Cables with a mechanical strength of approximately 30 N/mm super(2), suitable for wound repair and nerve regeneration applications, were prepared with a coagulation bath containing 0.25 M HCl, 2% CaCl sub(2) at a pH of <0.9. These cables also had a large average elongation at break of 52%, and showed an increase in cable length after breakage (permanent set) of 20%, demonstrating the potential for drawing the cables down to a fine diameter. Abstract A method for the wet extrusion of human plasma‐derived fibronectin–fibrinogen cables is described. Solutions of fibronectin and fibrinogen with and without sodium alginate and carboxymethylcellulose (CMC) are tested. The rheological properties of the protein solutions changed from Newtonian to shear thinning non‐Newtonian in the presence of small quantities of these additives, the apparent viscosity increased, and the extrusion properties of the protein solutions improved. Cables were prepared using a capillary with a diameter of 1 mm and overall length of 18 mm. Cable diameter was reduced to about 0.5 mm by drawing using a series of rollers. Cables prepared with sodium alginate were found to have suitable properties, and those made with CMC were sticky and difficult to handle. Solutions containing no sodium alginate required a minimum total protein concentration of about 70 mg/mL for extrusion. Extruded cables were prepared with solutions containing 140 mg/mL total protein with 12.9 mg/mL alginate (high protein), and 46 mg/mL total protein with 47.6 mg/mL of sodium alginate (high alginate). The mechanical strength of the extruded cables was within the range suitable for application in tissue engineering. Extrusion of the protein solutions into cables was achieved in a coagulation bath. Cables with a mechanical strength of approximately 30 N/mm 2 , suitable for wound repair and nerve regeneration applications, were prepared with a coagulation bath containing 0.25 M HCl, 2% CaCl 2 at a pH of <0.9. These cables also had a large average elongation at break of 52%, and showed an increase in cable length after breakage (permanent set) of 20%, demonstrating the potential for drawing the cables down to a fine diameter. © 2001 John Wiley & Sons, Inc. Biotechnol Bioeng 73: 295–305, 2001. A method for the wet extrusion of human plasma-derived fibronectin-fibrinogen cables is described. Solutions of fibronectin and fibrinogen with and without sodium alginate and carboxymethylcellulose (CMC) are tested. The rheological properties of the protein solutions changed from Newtonian to shear thinning non-Newtonian in the presence of small quantities of these additives, the apparent viscosity increased, and the extrusion properties of the protein solutions improved. Cables were prepared using a capillary with a diameter of 1 mm and overall length of 18 mm. Cable diameter was reduced to about 0.5 mm by drawing using a series of rollers. Cables prepared with sodium alginate were found to have suitable properties, and those made with CMC were sticky and difficult to handle. Solutions containing no sodium alginate required a minimum total protein concentration of about 70 mg/mL for extrusion. Extruded cables were prepared with solutions containing 140 mg/mL total protein with 12.9 mg/mL alginate (high protein), and 46 mg/mL total protein with 47.6 mg/mL of sodium alginate (high alginate). The mechanical strength of the extruded cables was within the range suitable for application in tissue engineering. Extrusion of the protein solutions into cables was achieved in a coagulation bath. Cables with a mechanical strength of approximately 30 N/mm(2), suitable for wound repair and nerve regeneration applications, were prepared with a coagulation bath containing 0.25 M HCl, 2% CaCl(2) at a pH of <0.9. These cables also had a large average elongation at break of 52%, and showed an increase in cable length after breakage (permanent set) of 20%, demonstrating the potential for drawing the cables down to a fine diameter. A method for the wet extrusion of human plasma‐derived fibronectin–fibrinogen cables is described. Solutions of fibronectin and fibrinogen with and without sodium alginate and carboxymethylcellulose (CMC) are tested. The rheological properties of the protein solutions changed from Newtonian to shear thinning non‐Newtonian in the presence of small quantities of these additives, the apparent viscosity increased, and the extrusion properties of the protein solutions improved. Cables were prepared using a capillary with a diameter of 1 mm and overall length of 18 mm. Cable diameter was reduced to about 0.5 mm by drawing using a series of rollers. Cables prepared with sodium alginate were found to have suitable properties, and those made with CMC were sticky and difficult to handle. Solutions containing no sodium alginate required a minimum total protein concentration of about 70 mg/mL for extrusion. Extruded cables were prepared with solutions containing 140 mg/mL total protein with 12.9 mg/mL alginate (high protein), and 46 mg/mL total protein with 47.6 mg/mL of sodium alginate (high alginate). The mechanical strength of the extruded cables was within the range suitable for application in tissue engineering. Extrusion of the protein solutions into cables was achieved in a coagulation bath. Cables with a mechanical strength of approximately 30 N/mm2, suitable for wound repair and nerve regeneration applications, were prepared with a coagulation bath containing 0.25 M HCl, 2% CaCl2 at a pH of <0.9. These cables also had a large average elongation at break of 52%, and showed an increase in cable length after breakage (permanent set) of 20%, demonstrating the potential for drawing the cables down to a fine diameter. © 2001 John Wiley & Sons, Inc. Biotechnol Bioeng 73: 295–305, 2001. A method for the wet extrusion of human plasma-derived fibronectin-fibrinogen cables is described. Solutions of fibronectin and fibrinogen with and without sodium alginate and carboxymethylcellulose (CMC) are tested. The rheological properties of the protein solutions changed from Newtonian to shear thinning non-Newtonian in the presence of small quantities of these additives, the apparent viscosity increased, and the extrusion properties of the protein solutions improved. Cables were prepared using a capillary with a diameter of 1 mm and overall length of 18 mm. Cable diameter was reduced to about 0.5 mm by drawing using a series of rollers. Cables prepared with sodium alginate were found to have suitable properties, and those made with CMC were sticky and difficult to handle. Solutions containing no sodium alginate required a minimum total protein concentration of about 70 mg/mL for extrusion. Extruded cables were prepared with solutions containing 140 mg/mL total protein with 12.9 mg/mL alginate (high protein), and 46 mg/mL total protein with 47.6 mg/mL of sodium alginate (high alginate). The mechanical strength of the extruded cables was within the range suitable for application in tissue engineering. Extrusion of the protein solutions into cables was achieved in a coagulation bath. Cables with a mechanical strength of approximately 30 N/mm(2), suitable for wound repair and nerve regeneration applications, were prepared with a coagulation bath containing 0.25 M HCl, 2% CaCl(2) at a pH of <0.9. These cables also had a large average elongation at break of 52%, and showed an increase in cable length after breakage (permanent set) of 20%, demonstrating the potential for drawing the cables down to a fine diameter. |
Author | Shamlou, P. Ayazi Underwood, S. Afoke, A. MacLeod, A. J. Dunnill, P. Brown, R. A. |
Author_xml | – sequence: 1 givenname: S. surname: Underwood fullname: Underwood, S. organization: Advanced Centre for Biochemical Engineering, Department of Biochemical Engineering, Torrington Place, University College London, London WC1E 7JE, UK; telephone: 0207-380-7031; fax: 0207-209-0703 – sequence: 2 givenname: A. surname: Afoke fullname: Afoke, A. organization: Department of Technology and Design, University of Westminster, London, UK – sequence: 3 givenname: R. A. surname: Brown fullname: Brown, R. A. organization: Tissue Repair Unit, Department of Plastic Surgery, University College London, London, UK – sequence: 4 givenname: A. J. surname: MacLeod fullname: MacLeod, A. J. organization: Protein Fractionation Centre, Scottish National Blood Transfusion Service, Edinburgh, UK – sequence: 5 givenname: P. Ayazi surname: Shamlou fullname: Shamlou, P. Ayazi organization: Advanced Centre for Biochemical Engineering, Department of Biochemical Engineering, Torrington Place, University College London, London WC1E 7JE, UK; telephone: 0207-380-7031; fax: 0207-209-0703 – sequence: 6 givenname: P. surname: Dunnill fullname: Dunnill, P. email: p.dunnill@ucl.ac.uk organization: Advanced Centre for Biochemical Engineering, Department of Biochemical Engineering, Torrington Place, University College London, London WC1E 7JE, UK; telephone: 0207-380-7031; fax: 0207-209-0703 |
BackLink | http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1056661$$DView record in Pascal Francis https://www.ncbi.nlm.nih.gov/pubmed/11283912$$D View this record in MEDLINE/PubMed |
BookMark | eNqF0EFrFDEUB_AgFbutQj9BmYOIl9GXzCSZHLVoW1iU0tVCLyGTfVnSzma2yQy2394MO2gv4ikv8Mv_kf8ROQh9QEJOKHygAOxj64c8CPaCLCgoWQJTcEAWACDKiit2SI5SustX2QjxihxSyppKUbYgqxscCnwc4ph8H4reFc63MafbwYdymn3oNxgKa9oOU-H6WJjdrvPWDNMDH4rBpzRigWHjA2L2m9fkpTNdwjfzeUx-fP2yOrsol9_PL88-LUtbU85KrGvrGsEYk5SDgRYrjmtplXNSCcpUzRteS2bXyJHWoNbOCtkguKq1XNLqmLzb5-5i_zBiGvTWJ4tdZwL2Y9JSAgVO6_9C2lR5F4MM3--hjX1KEZ3eRb818UlT0FPVOletp6ozPZ0zx3aL679w7jaDtzMwyZrORROsT88CuRBi-kS5Z798h0__3Kc_X67mvbP3acDHP97Eey1kJbm--Xauf4qLW7FU1_qq-g2Fh6Uf |
CODEN | BIBIAU |
CitedBy_id | crossref_primary_10_1088_1748_6041_2_4_008 crossref_primary_10_3390_ma10060568 crossref_primary_10_1097_01_prs_0000299373_25294_65 crossref_primary_10_1039_D0RA10749B crossref_primary_10_1021_acsnano_7b07196 crossref_primary_10_1002_jbm_a_32572 crossref_primary_10_1155_2021_4907027 crossref_primary_10_1179_174328905X55632 crossref_primary_10_1186_s11671_018_2491_8 crossref_primary_10_1016_j_actbio_2005_09_008 crossref_primary_10_1002_term_284 crossref_primary_10_1016_j_biomaterials_2003_09_052 crossref_primary_10_1089_ten_tea_2008_0603 crossref_primary_10_1016_j_biotechadv_2010_01_004 crossref_primary_10_3389_fmolb_2021_783268 crossref_primary_10_1016_j_colsurfb_2013_07_016 crossref_primary_10_3390_molecules26030619 crossref_primary_10_1021_acs_biomac_8b01258 crossref_primary_10_1016_j_expneurol_2018_05_016 crossref_primary_10_1002_jbm_a_30989 crossref_primary_10_1002_sstr_202000137 crossref_primary_10_1179_1743280414Y_0000000049 crossref_primary_10_5115_acb_21_233 crossref_primary_10_1177_155892500800300204 crossref_primary_10_1016_S0009_2509_01_00392_X crossref_primary_10_1089_107632703764664693 |
Cites_doi | 10.1126/science.8493529 10.1016/S0007-1226(97)91325-4 10.1046/j.1469-7580.1998.19320273.x 10.1126/science.7008197 10.1038/385537a0 10.1016/S0142-9612(98)00015-5 10.1016/S0065-3233(08)60588-4 10.1002/bip.360261208 10.1111/j.1460-9568.1995.tb00643.x 10.1083/jcb.139.3.709 10.1016/0142-9612(94)90225-9 10.1007/s11626-997-0031-4 10.1038/nbt0695-565 10.1515/bchm2.1983.364.1.551 10.1016/0142-9612(93)90038-4 10.1002/jbm.820140203 10.1046/j.1524-475X.1997.50304.x 10.1016/S0266-7681(05)80148-2 10.1021/ja00076a077 10.1016/0005-2795(75)90294-9 10.1111/j.1460-9568.1997.tb01493.x 10.1002/(SICI)1097-0169(1999)42:4<331::AID-CM6>3.0.CO;2-7 10.1002/(SICI)1097-0169(200005)46:1<6::AID-CM2>3.0.CO;2-Z 10.1089/ten.1995.1.151 10.1016/S0266-7681(96)80058-1 10.1002/bip.360340808 10.1182/blood.V56.2.145.145 10.1007/s004490050586 |
ContentType | Journal Article |
Copyright | Copyright © 2001 John Wiley & Sons, Inc. 2001 INIST-CNRS Copyright 2001 John Wiley & Sons, Inc. |
Copyright_xml | – notice: Copyright © 2001 John Wiley & Sons, Inc. – notice: 2001 INIST-CNRS – notice: Copyright 2001 John Wiley & Sons, Inc. |
DBID | BSCLL IQODW CGR CUY CVF ECM EIF NPM AAYXX CITATION 7QO 8FD FR3 P64 7X8 |
DOI | 10.1002/bit.1062 |
DatabaseName | Istex Pascal-Francis Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef Biotechnology Research Abstracts Technology Research Database Engineering Research Database Biotechnology and BioEngineering Abstracts MEDLINE - Academic |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef Engineering Research Database Biotechnology Research Abstracts Technology Research Database Biotechnology and BioEngineering Abstracts MEDLINE - Academic |
DatabaseTitleList | Engineering Research Database CrossRef MEDLINE - Academic MEDLINE |
Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Engineering Chemistry Biology Anatomy & Physiology |
EISSN | 1097-0290 |
EndPage | 305 |
ExternalDocumentID | 10_1002_bit_1062 11283912 1056661 BIT1062 ark_67375_WNG_V6HZ6L9S_Q |
Genre | article Research Support, Non-U.S. Gov't Journal Article |
GrantInformation_xml | – fundername: Biotechnology and Biological Sciences Research Council – fundername: PFC Edinburgh |
GroupedDBID | --- -~X .3N .GA .GJ .Y3 05W 0R~ 10A 1L6 1OB 1OC 1ZS 23N 31~ 33P 3SF 3WU 4.4 4ZD 50Y 50Z 51W 51X 52M 52N 52O 52P 52S 52T 52U 52W 52X 53G 5GY 5RE 5VS 66C 702 7PT 8-0 8-1 8-3 8-4 8-5 8UM 930 A03 AAESR AAEVG AAHHS AAJUZ AANLZ AAONW AASGY AAXRX AAZKR ABCQN ABCUV ABCVL ABHUG ABIJN ABJNI ABPVW ACAHQ ACBWZ ACCFJ ACCZN ACGFO ACGFS ACIWK ACPOU ACPRK ACSMX ACXBN ACXME ACXQS ADAWD ADBBV ADDAD ADEOM ADIZJ ADKYN ADMGS ADOZA ADXAS ADZMN ADZOD AEEZP AEIGN AEIMD AENEX AEQDE AEUQT AEUYR AFBPY AFFNX AFFPM AFGKR AFPWT AFRAH AFVGU AFZJQ AGJLS AHBTC AI. AIAGR AIURR AIWBW AJBDE AJXKR ALAGY ALMA_UNASSIGNED_HOLDINGS ALUQN AMBMR AMYDB ASPBG ATUGU AUFTA AVWKF AZBYB AZFZN AZVAB BAFTC BDRZF BFHJK BHBCM BLYAC BMNLL BMXJE BNHUX BROTX BRXPI BSCLL BY8 CS3 D-E D-F DCZOG DPXWK DR1 DR2 DRFUL DRSTM DU5 EBS EJD F00 F01 F04 F5P FEDTE G-S G.N GNP GODZA H.T H.X HBH HHY HHZ HVGLF HZ~ IX1 J0M JPC KQQ LATKE LAW LC2 LC3 LEEKS LH4 LITHE LOXES LP6 LP7 LUTES LW6 LYRES MEWTI MK4 MRFUL MRSTM MSFUL MSSTM MXFUL MXSTM N04 N05 N9A NF~ NNB O66 O9- P2P P2W P2X P4D PQQKQ Q.N Q11 QB0 QRW R.K RBB RNS ROL RWI RX1 SUPJJ TN5 UB1 V2E VH1 W8V W99 WBKPD WH7 WIB WIH WIK WJL WNSPC WOHZO WQJ WRC WXSBR WYISQ XFK XG1 XPP XSW XV2 Y6R ZZTAW ~02 ~IA ~KM ~WT AITYG HGLYW OIG 08R 3EH AAPBV ABEML ACSCC EBD EMOBN HF~ IQODW LH6 NDZJH PALCI RIWAO RJQFR RYL SAMSI SV3 WSB ZGI ZXP CGR CUY CVF ECM EIF NPM AAYXX CITATION 7QO 8FD FR3 P64 7X8 |
ID | FETCH-LOGICAL-c4152-e44cf862227150a0be35ed7c9ff7961294585472cde5e1409dfc678e0f3bc5713 |
IEDL.DBID | DR2 |
ISSN | 0006-3592 |
IngestDate | Fri Aug 16 10:48:47 EDT 2024 Sat Aug 17 02:29:48 EDT 2024 Fri Aug 23 00:44:11 EDT 2024 Sat Sep 28 07:36:20 EDT 2024 Sun Oct 22 16:07:05 EDT 2023 Sat Aug 24 00:53:59 EDT 2024 Wed Jan 17 04:59:22 EST 2024 |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 4 |
Keywords | Tissue engineering Medical application Fibronectin Wet spinning Composite material Fibrinogen |
Language | English |
License | CC BY 4.0 Copyright 2001 John Wiley & Sons, Inc. |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c4152-e44cf862227150a0be35ed7c9ff7961294585472cde5e1409dfc678e0f3bc5713 |
Notes | istex:AC1702A38A6D422BC8E3D4367A671BF49EF26CAD ark:/67375/WNG-V6HZ6L9S-Q PFC Edinburgh Biotechnology and Biological Sciences Research Council ArticleID:BIT1062 ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
PMID | 11283912 |
PQID | 18345820 |
PQPubID | 23462 |
PageCount | 11 |
ParticipantIDs | proquest_miscellaneous_77010514 proquest_miscellaneous_18345820 crossref_primary_10_1002_bit_1062 pubmed_primary_11283912 pascalfrancis_primary_1056661 wiley_primary_10_1002_bit_1062_BIT1062 istex_primary_ark_67375_WNG_V6HZ6L9S_Q |
PublicationCentury | 2000 |
PublicationDate | 20 May 2001 |
PublicationDateYYYYMMDD | 2001-05-20 |
PublicationDate_xml | – month: 05 year: 2001 text: 20 May 2001 day: 20 |
PublicationDecade | 2000 |
PublicationPlace | New York |
PublicationPlace_xml | – name: New York – name: New York, NY – name: United States |
PublicationTitle | Biotechnology and bioengineering |
PublicationTitleAlternate | Biotechnol. Bioeng |
PublicationYear | 2001 |
Publisher | John Wiley & Sons, Inc Wiley |
Publisher_xml | – name: John Wiley & Sons, Inc – name: Wiley |
References | Ahmed Z, Idowu BD, Brown RA. 1999. Stabilisation of fibronectin mats with micromolar concentrations of copper. Biomaterials 20:201-210. Mosesson MW, Amrani DL. 1980. The structure and biologic activities of plasma fibronectin. Blood 56:145-158. Palecek SP, Loftus JC, Ginsberg MH, Lauffenburger DA, Horwitz AF. 1997. Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness. Nature 385:537-540. Brown RA, Blunn GW, Ejim OS. 1994. Preparation of orientated fibrous mats from fibronectin: composition and stability. Biomaterials 15:457-464. Homandberg GA. 1987. Characterization of the interactions of an amino-terminal fibronectin fragment with the native molecule: implications for polymerization of fibronectin. Biopolymers 26:2087-2098. Mosesson MW, Chen AB, Huseby RM. 1975. The cold-insoluble globulin of human plasma: studies of the essential structural features. Biochim Biophys Acta 386:509-524. Hobson MI, Brown R, Green CJ, Terenghi G. 1997. Inter-relationships between angiogenesis and nerve regeneration: a histochemical study. Br Plast Surg 50:125-131. Wojciak-Stothard B, Denyer M, Mishra M, Brown RA. 1997. Adhesion, orientation and movement of cells cultured on ultrathin fibronectin fibres. In Vitro Cell Dev Biol Anim 33:110-117. Sterne GD, Brown RA, Green CJ, Terenghi G. 1997a. Neurotrophin-3 delivered locally via fibronectin mats enhances peripheral nerve regeneration. Eur J Neurosci 9:1388-1396. Whitworth IH, Terenghi G, Green CJ, Brown RA, Stevens E, Tomlinson DR. 1995b. Targeted delivery of nerve growth factor via fibronectin conduits assists nerve regeneration in control and diabetic rats. Eur J Neurosci 7:2220-2225. Markovic Z, Engel J, Richter H, Hormann H. 1983. Determination of different domains in fibronectin on the basis of their stability against urea denaturation. Hoppe Seyler Physiol Z 364:551-561. Brown RA, Smith KD, McGrouther A. 1997. Strategies for cell engineering in tissue repair. Wound Rep Reg 5:212-221. Sterne GD, Brown RA, Green CJ, Terenghi G. 1998. NT-3 modulates NPY expression in primary sensory neurons following peripheral nerve injury. J Anat 193:273-281. Hubbell JA. 1995. Biomaterials in tissue engineering. Bio/Technology 13:565-576. Yannas IV, Burke JF, Gordon PL, Huang C, Rubenstein RH. 1980. Design of an artificial skin. II. Control of chemical composition. J Biomed Mater Res 14:107-131. Lundgren HP. 1949. Synthetic fibres made from proteins. Adv Prot Chem 5:305-351. Ahmed Z, Underwood S, Brown RA. 2000. Low concentrations of fibrinogen increase cell migration speed on fibronectin/fibrinogen composite cables. Cell Motil Cytoskel 46:6-16. Bell E, Ehrlich HP, Buttle DJ, Nakatsuji T. 1981. Living tissue formed in vitro and accepted as skin-equivalent tissue of full thickness. Science 211:1052-1054. Langer R, Vacanti JP, Vacanti CA, Atala A, Freed LE, Vunjak-Novakovic G. 1995. Tissue engineering: biomedical applications. Tissue Eng 1:151-161. Underwood S, Afoke A, Brown RA, MacLeod AJ, Dunnill P. 1999. The physical properties of a fibrillar fibronectin-fibrinogen material with potential use in tissue engineering. Bioproc Eng 20:239-248. Whitworth IH, Brown RA, Dore C, Green CJ, Terenghi G. 1995a. Orientated mats of fibronectin as a conduit material for use in peripheral nerve regeneration. J Hand Surg 20B:429-435. Sterne GD, Coulton GR, Brown RA, Green CJ, Terenghi G. 1997b. Neurotrophin-3-enhanced nerve regeneration selectively improves recovery of muscle fibres expressing myosin heavy chains 2b. J Cell Biol 139:709-715. Anderson JP, Cappello J, Martin DC. 1994. Morphology and primary crystal structure of a silk-like protein polymer synthesized by genetically engineered Escherichia coli bacteria. Biopolymers 34:1049-1058. Whitworth IH, Brown RA, Dore CJ, Anand P, Green CJ, Terenghi G. 1996. Nerve growth factor enhances nerve regeneration through fibronectin grafts. J Hand Surg 21B:514-522. Barrera DA, Zylstra E, Lansbury PT, Langer R. 1993. Synthesis and RGD modification of a new biodegradable copolymer: poly (lactic acid-co-lysine). J Am Chem Soc 115:11010-11011. Berger SA, Goldsmith W, Lewis ER. 1996. Introduction to bioengineering. Oxford: Oxford University Press. Langer R, Vacanti JP. 1993. Tissue engineering. Science 260:920-925. Ejim OS, Blunn GW, Brown RA. 1993. Production of artificial-orientated mats and strands from plasma fibronectin: a morphological study. Biomaterials 14:743-748. Ahmed Z, Brown RA. 1999. Adhesion, alignment, and migration of cultured Schwann cells on ultrathin fibronectin fibres. Cell Motil Cytoskel 42:331-343. 2000; 46 1995; 13 1997a; 9 1995b; 7 1949; 5 1995a; 20B 1993; 260 1996 1999; 42 1999; 20 1975; II 1997; 5 1995; 1 1993; 14 1998; 193 1980; 14 1997; 50 1983; 364 1997; 33 1981; 211 1996; 21B 1980; 56 1997; 385 1994; 34 1975; 386 1994; 15 1997b; 139 1993; 115 1987; 26 1989 Doolittle RF (e_1_2_1_11_1) 1975 Mosesson MW (e_1_2_1_20_1) 1980; 56 e_1_2_1_23_1 e_1_2_1_24_1 e_1_2_1_21_1 e_1_2_1_22_1 e_1_2_1_27_1 e_1_2_1_28_1 e_1_2_1_25_1 e_1_2_1_26_1 e_1_2_1_29_1 e_1_2_1_7_1 e_1_2_1_30_1 e_1_2_1_5_1 e_1_2_1_6_1 Yamada K (e_1_2_1_31_1) 1989 e_1_2_1_3_1 e_1_2_1_12_1 e_1_2_1_4_1 e_1_2_1_13_1 e_1_2_1_10_1 e_1_2_1_2_1 e_1_2_1_32_1 e_1_2_1_16_1 e_1_2_1_17_1 e_1_2_1_14_1 e_1_2_1_15_1 Berger SA (e_1_2_1_8_1) 1996 e_1_2_1_9_1 e_1_2_1_18_1 e_1_2_1_19_1 |
References_xml | – volume: 34 start-page: 1049 year: 1994 end-page: 1058 article-title: Morphology and primary crystal structure of a silk‐like protein polymer synthesized by genetically engineered bacteria publication-title: Biopolymers – volume: 139 start-page: 709 year: 1997b end-page: 715 article-title: Neurotrophin‐3‐enhanced nerve regeneration selectively improves recovery of muscle fibres expressing myosin heavy chains 2b publication-title: J Cell Biol – volume: 14 start-page: 107 year: 1980 end-page: 131 article-title: Design of an artificial skin. II. Control of chemical composition publication-title: J Biomed Mater Res – volume: 33 start-page: 110 year: 1997 end-page: 117 article-title: Adhesion, orientation and movement of cells cultured on ultrathin fibronectin fibres publication-title: In Vitro Cell Dev Biol Anim – volume: 46 start-page: 6 year: 2000 end-page: 16 article-title: Low concentrations of fibrinogen increase cell migration speed on fibronectin/fibrinogen composite cables publication-title: Cell Motil Cytoskel – volume: 386 start-page: 509 year: 1975 end-page: 524 article-title: The cold‐insoluble globulin of human plasma: studies of the essential structural features publication-title: Biochim Biophys Acta – volume: 14 start-page: 743 year: 1993 end-page: 748 article-title: Production of artificial‐orientated mats and strands from plasma fibronectin: a morphological study publication-title: Biomaterials – volume: 211 start-page: 1052 year: 1981 end-page: 1054 article-title: Living tissue formed in vitro and accepted as skin‐equivalent tissue of full thickness publication-title: Science – year: 1996 – volume: 1 start-page: 151 year: 1995 end-page: 161 article-title: Tissue engineering: biomedical applications publication-title: Tissue Eng – volume: 115 start-page: 11010 year: 1993 end-page: 11011 article-title: Synthesis and RGD modification of a new biodegradable copolymer: poly (lactic acid‐co‐lysine) publication-title: J Am Chem Soc – volume: 20B start-page: 429 year: 1995a end-page: 435 article-title: Orientated mats of fibronectin as a conduit material for use in peripheral nerve regeneration publication-title: J Hand Surg – volume: II start-page: 110 year: 1975 end-page: 161 – volume: 5 start-page: 212 year: 1997 end-page: 221 article-title: Strategies for cell engineering in tissue repair publication-title: Wound Rep Reg – volume: 5 start-page: 305 year: 1949 end-page: 351 article-title: Synthetic fibres made from proteins publication-title: Adv Prot Chem – start-page: 51 year: 1989 end-page: 68 – volume: 50 start-page: 125 year: 1997 end-page: 131 article-title: Inter‐relationships between angiogenesis and nerve regeneration: a histochemical study publication-title: Br Plast Surg – volume: 13 start-page: 565 year: 1995 end-page: 576 article-title: Biomaterials in tissue engineering publication-title: Bio/Technology – volume: 56 start-page: 145 year: 1980 end-page: 158 article-title: The structure and biologic activities of plasma fibronectin publication-title: Blood – volume: 260 start-page: 920 year: 1993 end-page: 925 article-title: Tissue engineering publication-title: Science – volume: 364 start-page: 551 year: 1983 end-page: 561 article-title: Determination of different domains in fibronectin on the basis of their stability against urea denaturation publication-title: Hoppe Seyler Physiol Z – volume: 385 start-page: 537 year: 1997 end-page: 540 article-title: Integrin–ligand binding properties govern cell migration speed through cell‐substratum adhesiveness publication-title: Nature – volume: 20 start-page: 239 year: 1999 end-page: 248 article-title: The physical properties of a fibrillar fibronectin–fibrinogen material with potential use in tissue engineering publication-title: Bioproc Eng – volume: 21B start-page: 514 year: 1996 end-page: 522 article-title: Nerve growth factor enhances nerve regeneration through fibronectin grafts publication-title: J Hand Surg – volume: 7 start-page: 2220 year: 1995b end-page: 2225 article-title: Targeted delivery of nerve growth factor via fibronectin conduits assists nerve regeneration in control and diabetic rats publication-title: Eur J Neurosci – volume: 15 start-page: 457 year: 1994 end-page: 464 article-title: Preparation of orientated fibrous mats from fibronectin: composition and stability publication-title: Biomaterials – volume: 26 start-page: 2087 year: 1987 end-page: 2098 article-title: Characterization of the interactions of an amino‐terminal fibronectin fragment with the native molecule: implications for polymerization of fibronectin publication-title: Biopolymers – volume: 20 start-page: 201 year: 1999 end-page: 210 article-title: Stabilisation of fibronectin mats with micromolar concentrations of copper publication-title: Biomaterials – volume: 9 start-page: 1388 year: 1997a end-page: 1396 article-title: Neurotrophin‐3 delivered locally via fibronectin mats enhances peripheral nerve regeneration publication-title: Eur J Neurosci – volume: 42 start-page: 331 year: 1999 end-page: 343 article-title: Adhesion, alignment, and migration of cultured Schwann cells on ultrathin fibronectin fibres publication-title: Cell Motil Cytoskel – volume: 193 start-page: 273 year: 1998 end-page: 281 article-title: NT‐3 modulates NPY expression in primary sensory neurons following peripheral nerve injury publication-title: J Anat – ident: e_1_2_1_16_1 doi: 10.1126/science.8493529 – ident: e_1_2_1_13_1 doi: 10.1016/S0007-1226(97)91325-4 – ident: e_1_2_1_24_1 doi: 10.1046/j.1469-7580.1998.19320273.x – ident: e_1_2_1_7_1 doi: 10.1126/science.7008197 – volume-title: Introduction to bioengineering year: 1996 ident: e_1_2_1_8_1 contributor: fullname: Berger SA – ident: e_1_2_1_22_1 doi: 10.1038/385537a0 – ident: e_1_2_1_3_1 doi: 10.1016/S0142-9612(98)00015-5 – ident: e_1_2_1_18_1 doi: 10.1016/S0065-3233(08)60588-4 – start-page: 110 year: 1975 ident: e_1_2_1_11_1 contributor: fullname: Doolittle RF – ident: e_1_2_1_14_1 doi: 10.1002/bip.360261208 – ident: e_1_2_1_29_1 doi: 10.1111/j.1460-9568.1995.tb00643.x – ident: e_1_2_1_25_1 doi: 10.1083/jcb.139.3.709 – ident: e_1_2_1_9_1 doi: 10.1016/0142-9612(94)90225-9 – ident: e_1_2_1_30_1 doi: 10.1007/s11626-997-0031-4 – ident: e_1_2_1_15_1 doi: 10.1038/nbt0695-565 – ident: e_1_2_1_19_1 doi: 10.1515/bchm2.1983.364.1.551 – ident: e_1_2_1_12_1 doi: 10.1016/0142-9612(93)90038-4 – ident: e_1_2_1_32_1 doi: 10.1002/jbm.820140203 – ident: e_1_2_1_10_1 doi: 10.1046/j.1524-475X.1997.50304.x – ident: e_1_2_1_28_1 doi: 10.1016/S0266-7681(05)80148-2 – ident: e_1_2_1_6_1 doi: 10.1021/ja00076a077 – ident: e_1_2_1_21_1 doi: 10.1016/0005-2795(75)90294-9 – ident: e_1_2_1_23_1 doi: 10.1111/j.1460-9568.1997.tb01493.x – ident: e_1_2_1_2_1 doi: 10.1002/(SICI)1097-0169(1999)42:4<331::AID-CM6>3.0.CO;2-7 – ident: e_1_2_1_4_1 doi: 10.1002/(SICI)1097-0169(200005)46:1<6::AID-CM2>3.0.CO;2-Z – ident: e_1_2_1_17_1 doi: 10.1089/ten.1995.1.151 – start-page: 51 volume-title: Fibronectin year: 1989 ident: e_1_2_1_31_1 contributor: fullname: Yamada K – ident: e_1_2_1_27_1 doi: 10.1016/S0266-7681(96)80058-1 – ident: e_1_2_1_5_1 doi: 10.1002/bip.360340808 – volume: 56 start-page: 145 year: 1980 ident: e_1_2_1_20_1 article-title: The structure and biologic activities of plasma fibronectin publication-title: Blood doi: 10.1182/blood.V56.2.145.145 contributor: fullname: Mosesson MW – ident: e_1_2_1_26_1 doi: 10.1007/s004490050586 |
SSID | ssj0007866 |
Score | 1.8728942 |
Snippet | A method for the wet extrusion of human plasma‐derived fibronectin–fibrinogen cables is described. Solutions of fibronectin and fibrinogen with and without... A method for the wet extrusion of human plasma-derived fibronectin-fibrinogen cables is described. Solutions of fibronectin and fibrinogen with and without... Abstract A method for the wet extrusion of human plasma‐derived fibronectin–fibrinogen cables is described. Solutions of fibronectin and fibrinogen with and... |
SourceID | proquest crossref pubmed pascalfrancis wiley istex |
SourceType | Aggregation Database Index Database Publisher |
StartPage | 295 |
SubjectTerms | Alginates - chemistry Biological and medical sciences Biomedical Engineering Biotechnology Carboxymethylcellulose Sodium - chemistry Coagulants - chemistry Culture Techniques Extracellular Matrix - chemistry fibrinogen Fibrinogen - chemistry Fibrinogen - ultrastructure fibronectin Fibronectins - chemistry Fibronectins - ultrastructure Fundamental and applied biological sciences. Psychology Glucuronic Acid Health. Pharmaceutical industry Hexuronic Acids Humans Industrial applications and implications. Economical aspects Microscopy, Electron, Scanning Miscellaneous protein fibers Rheology tissue engineering wet spinning |
Title | Wet extrusion of fibronectin-fibrinogen cables for application in tissue engineering |
URI | https://api.istex.fr/ark:/67375/WNG-V6HZ6L9S-Q/fulltext.pdf https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fbit.1062 https://www.ncbi.nlm.nih.gov/pubmed/11283912 https://search.proquest.com/docview/18345820 https://search.proquest.com/docview/77010514 |
Volume | 73 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3daxQxEB-kRbQPVa9-rFqNIH3bdj-SzeWxLdZTpKD2C30I2WwCR-me9O5AffJ_8D_0L3Emue3diQXxaXdhNiSTyeQ3yeQXgJfWllLlpp867lXKvStS1ZR5WjjTr3xujLCB7fOwGhzzt2fibJZVSWdhIj_E1YIbjYzgr2mAm3q8MycNrYfE_hzcL_HoER76MGeOkv24TUkBcylU0fHOZsVO9-PSTLRKSv1KmZFmjMrx8VaLv8HOZRQbpqGDO_C5a0DMPjnfnk7qbfv9D27H_2vhXVifoVO2G83pHtxwbQ82dluMzC--sS0W8kXDQnwPbu51b7f2u1vjerC2QHC4ASenbsLQ_V9OaVGOjTzzWKNRS162_fXjJ30N2xEaMbN0hmvMEEOzhU11NmzZJNgGc_OC78Pxwauj_UE6u8khtQQQ0BC49Rg7FYVEAGqy2pXCNdLSgrFCjKU4Ri1cFrZxwhEFV-MtzqIu82VtBcbRD2Clxco9AmYb6epM9a3CeFo03nCO0k1eEZFhnWcJvOh6VX-JhB06UjMXGhWqSaEJbIXuvhIwl-eU4CaFPj18rU-qwafqnfqo3yewuWQPCyUiDK7yBJ539qFRz7TXYlo3mo41ekrakcyul5CSLifNeQIPo2HNC0fMUKqcqhnM49p26L03R_R8_K-CT-B2zKET6B2fwgp2v9tEUDWpn4Xh8xvTBR6i |
link.rule.ids | 315,786,790,1382,27955,27956,46327,46751 |
linkProvider | Wiley-Blackwell |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1tb9MwED5Nm9DgAy8dGxmMGQntW7a8Oa7Fp20wOiiVgO5FCMlyHFuqJtJpbSXgE_-Bf7hfsrt4WVvEJMSnJJJj2Ze783Pny2OAl8akQsa6HdrMyTBzNgllmcZhYnU7d7HW3NRsn728c5S9O-WnC_Cq-RfG80PcJNzIMmp_TQZOCemdKWtoMSD6Z_K_S2jtnKzy9acpd5Ro-41KCplTLpOGeTZKdpo359aiJRLrd6qN1CMUj_PnWvwNeM7j2HohOngAX5sp-PqTs-3JuNg2P_9gd_zPOT6E-9cAle16jXoEC7ZqwcpuhcH5tx9si9Ulo3UuvgV39pq75f3m4LgW3JvhOFyB4xM7ZrgCXEwoL8eGjjkc0rAiR1td_vpNT4NqiHrMDP3GNWIIo9nMvjobVGxcqwez044fw9HBm_5-J7w-zCE0hBFQFzLjMHxKEoEYVEeFTbkthaGcsUSYJTMMXDKRmNJySyxcpTO4kNrIpYXhGEqvwmKFg3sCzJTCFpFsG4khNS-dzjJsXcY5cRkWcRTAi-azqnPP2aE8O3OiUKCKBBrAVv29bxroizOqcRNcnfTequO88yXvys_qYwAbcwox0yMi4TwOYLNREIVypu0WXdnhZKTQWdKmZHR7CyHofNI4C2DNa9a0c4QNqYxpmLV-3DoPtXfYp-v6vzbchOVO_0NXdQ9775_CXV9Sx9FZPoNFVAW7gRhrXDyvbekKrhUiwg |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1bb9MwFD5Cm7jsgUu3sQBjRkJ7y5Y4TlI_7kLpYKq47CZ4sBLHlqpp6bS20uCJ_8A_5Jdwjt2sLWIS4imJ5Fj2yefj79gnnwFea53kMi7aoRFWhsIaHsoqiUNuinZm46JItVP77GXdY_HuLD2bZFXSvzBeH-JmwY1GhvPXNMAvK7s9FQ0t-6T-TO53UWQJp8Br_9NUOipv-31KipiTVPJGeDbi282bc1PRIln1mlIjiyFax_pjLf7GO-dprJuHOo_ga9MDn35yvjUelVv6-x_ijv_XxcfwcEJP2Y7H0xO4Y-oWLO_UGJpffGObzCWMupX4Ftzdbe7u7zXHxrVgaUbhcBlOTs2Iof-_GtOqHBtYZrFFg5rcbP3rx0966tcDRDHT9BPXkCGJZjO76qxfs5EDBzPTilfguPPmaK8bTo5yCDUxBESC0BaDJ85zZKBFVJokNVWuacVYIsmSAsMWkXNdmdSQBldlNU6jJrJJqVMMpFdhocbGrQHTVW7KSLa1xIA6rWwhBJau4oyUDMs4CuBV81XVpVfsUF6bmSs0qCKDBrDpPvdNgeLqnDLc8lSd9t6qk6z7JTuUn9XHANbn8DBTI_LgLA5go8GHQjvTZktRm8F4qNBV0pZkdHuJPKfTSWMRwFMPrGnlSBoSGVMzHTxu7YfaPTii67N_LbgB9z7sd9ThQe_9c3jg8-lS9JQvYAGRYNaRYI3Kl24k_QYz_iFx |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Wet+extrusion+of+fibronectin-fibrinogen+cables+for+application+in+tissue+engineering&rft.jtitle=Biotechnology+and+bioengineering&rft.au=Underwood%2C+S&rft.au=Afoke%2C+A&rft.au=Brown%2C+R+A&rft.au=MacLeod%2C+A+J&rft.date=2001-05-20&rft.issn=0006-3592&rft.volume=73&rft.issue=4&rft.spage=295&rft.epage=305&rft_id=info:doi/10.1002%2Fbit.1062&rft.externalDBID=NO_FULL_TEXT |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0006-3592&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0006-3592&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0006-3592&client=summon |