Human Chondrocyte Morphology, Its Dedifferentiation, and Fibronectin Conformation on Different PLLA Microtopographies
Surfaces of poly(L-lactic acid) (PLLA) of well-defined microtopography were prepared by making use of the semicrystalline character of PLLA. Different thermal treatments before isothermal crystallization (which include nucleation steps) permit to obtain a controlled number of simultaneously growing...
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container_title | Tissue engineering. Part A |
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creator | Martínez, Elisa Costa Hernández, Jose Carlos Rodríguez Machado, Margarida Mano, João F. Ribelles, Jose Luis Gómez Pradas, Manuel Monleón Sánchez, Manuel Salmerón |
description | Surfaces of poly(L-lactic acid) (PLLA) of well-defined microtopography were prepared by making use of the semicrystalline character of PLLA. Different thermal treatments before isothermal crystallization (which include nucleation steps) permit to obtain a controlled number of simultaneously growing spherulites, which, in the end, modulate the topography at the microscale. Four qualitatively different surfaces were prepared. The dynamics of primary human chondrocyte adhesion and cytoskeleton organization was investigated on the different surfaces. Chondrocyte morphology is shown to be influenced by the microtopography of the system as obtained by scanning electron microscopy and atomic force microscopy (AFM). The cytoplasmatic distribution of a focal adhesion protein, tensin, is followed as a function of time. Since the effect of surface topography on cell morphology is a consequence of the process of interaction between the extracellular matrix (ECM) proteins, adsorbed on the surface of the material, and related cell adhesion molecules, the conformation of one ECM protein, fibronectin, adsorbed on the different substrates was investigated by means of AFM. |
doi_str_mv | 10.1089/ten.tea.2007.0270 |
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Different thermal treatments before isothermal crystallization (which include nucleation steps) permit to obtain a controlled number of simultaneously growing spherulites, which, in the end, modulate the topography at the microscale. Four qualitatively different surfaces were prepared. The dynamics of primary human chondrocyte adhesion and cytoskeleton organization was investigated on the different surfaces. Chondrocyte morphology is shown to be influenced by the microtopography of the system as obtained by scanning electron microscopy and atomic force microscopy (AFM). The cytoplasmatic distribution of a focal adhesion protein, tensin, is followed as a function of time. Since the effect of surface topography on cell morphology is a consequence of the process of interaction between the extracellular matrix (ECM) proteins, adsorbed on the surface of the material, and related cell adhesion molecules, the conformation of one ECM protein, fibronectin, adsorbed on the different substrates was investigated by means of AFM.</description><identifier>ISSN: 1937-3341</identifier><identifier>EISSN: 1937-335X</identifier><identifier>DOI: 10.1089/ten.tea.2007.0270</identifier><identifier>PMID: 18823278</identifier><language>eng</language><publisher>United States: Mary Ann Liebert, Inc</publisher><subject>Actins - metabolism ; Biocompatible Materials - chemistry ; Cartilage cells ; Cell Differentiation ; Chondrocytes - cytology ; Chondrocytes - metabolism ; Chondrocytes - ultrastructure ; Fibronectins - chemistry ; Health aspects ; Humans ; Lactic Acid - chemistry ; Methods ; Microfilament Proteins - metabolism ; Microscopy ; Microscopy, Atomic Force ; Microscopy, Electron, Scanning ; Polymers - chemistry ; Protein Conformation ; Tensins ; Tissue engineering ; Tissue Engineering - methods ; Topographical drawing</subject><ispartof>Tissue engineering. 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Part A</title><addtitle>Tissue Eng Part A</addtitle><description>Surfaces of poly(L-lactic acid) (PLLA) of well-defined microtopography were prepared by making use of the semicrystalline character of PLLA. Different thermal treatments before isothermal crystallization (which include nucleation steps) permit to obtain a controlled number of simultaneously growing spherulites, which, in the end, modulate the topography at the microscale. Four qualitatively different surfaces were prepared. The dynamics of primary human chondrocyte adhesion and cytoskeleton organization was investigated on the different surfaces. Chondrocyte morphology is shown to be influenced by the microtopography of the system as obtained by scanning electron microscopy and atomic force microscopy (AFM). The cytoplasmatic distribution of a focal adhesion protein, tensin, is followed as a function of time. Since the effect of surface topography on cell morphology is a consequence of the process of interaction between the extracellular matrix (ECM) proteins, adsorbed on the surface of the material, and related cell adhesion molecules, the conformation of one ECM protein, fibronectin, adsorbed on the different substrates was investigated by means of AFM.</description><subject>Actins - metabolism</subject><subject>Biocompatible Materials - chemistry</subject><subject>Cartilage cells</subject><subject>Cell Differentiation</subject><subject>Chondrocytes - cytology</subject><subject>Chondrocytes - metabolism</subject><subject>Chondrocytes - ultrastructure</subject><subject>Fibronectins - chemistry</subject><subject>Health aspects</subject><subject>Humans</subject><subject>Lactic Acid - chemistry</subject><subject>Methods</subject><subject>Microfilament Proteins - metabolism</subject><subject>Microscopy</subject><subject>Microscopy, Atomic Force</subject><subject>Microscopy, Electron, Scanning</subject><subject>Polymers - chemistry</subject><subject>Protein Conformation</subject><subject>Tensins</subject><subject>Tissue engineering</subject><subject>Tissue Engineering - methods</subject><subject>Topographical drawing</subject><issn>1937-3341</issn><issn>1937-335X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqNkkFv1DAQhSNERUvhB3BBEZU4dYPHTmLnuNpSWmmrcgCJm-VNxruuEjvYzmH_PQ67gEBIrWzL1vh7I_vpZdkbIAUQ0XyIaIuIqqCE8IJQTp5lZ9AwvmCs-vb897mE0-xlCA-E1KTm_EV2CkJQRrk4y6abaVA2X-2c7bxr9xHzO-fHnevddn-Z38aQX2FntEaPNhoVjbOXubJdfm023llso0lyZ7Xzw8_bPM2rX4L883q9zO9M6110o9t6Ne4MhlfZiVZ9wNfH_Tz7ev3xy-pmsb7_dLtarhdtyWlcYAmkIaBYxbVSSJpaQ0eYFsB5xRluSloL3XQaGFFCKVKjqkoQwBoOFXJ2nr0_9B29-z5hiHIwocW-VxbdFGTd1JCcLB8FoaGiBjaD7_4BH9zkbfqEpAQ45SURCbo4QFvVozTJm-hVO3eUSxC8qhkVTaKK_1BpdDiYNlmrTar_JYCDILkZgkctR28G5fcSiJwDIVMg0lJyDoScA5E0b4_vnTYDdn8UxwQkgB-Auays7Q1u0McntP4BehTEIQ</recordid><startdate>20081001</startdate><enddate>20081001</enddate><creator>Martínez, Elisa Costa</creator><creator>Hernández, Jose Carlos Rodríguez</creator><creator>Machado, Margarida</creator><creator>Mano, João F.</creator><creator>Ribelles, Jose Luis Gómez</creator><creator>Pradas, Manuel Monleón</creator><creator>Sánchez, Manuel Salmerón</creator><general>Mary Ann Liebert, Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QP</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20081001</creationdate><title>Human Chondrocyte Morphology, Its Dedifferentiation, and Fibronectin Conformation on Different PLLA Microtopographies</title><author>Martínez, Elisa Costa ; 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Part A</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Martínez, Elisa Costa</au><au>Hernández, Jose Carlos Rodríguez</au><au>Machado, Margarida</au><au>Mano, João F.</au><au>Ribelles, Jose Luis Gómez</au><au>Pradas, Manuel Monleón</au><au>Sánchez, Manuel Salmerón</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Human Chondrocyte Morphology, Its Dedifferentiation, and Fibronectin Conformation on Different PLLA Microtopographies</atitle><jtitle>Tissue engineering. Part A</jtitle><addtitle>Tissue Eng Part A</addtitle><date>2008-10-01</date><risdate>2008</risdate><volume>14</volume><issue>10</issue><spage>1751</spage><epage>1762</epage><pages>1751-1762</pages><issn>1937-3341</issn><eissn>1937-335X</eissn><abstract>Surfaces of poly(L-lactic acid) (PLLA) of well-defined microtopography were prepared by making use of the semicrystalline character of PLLA. Different thermal treatments before isothermal crystallization (which include nucleation steps) permit to obtain a controlled number of simultaneously growing spherulites, which, in the end, modulate the topography at the microscale. Four qualitatively different surfaces were prepared. The dynamics of primary human chondrocyte adhesion and cytoskeleton organization was investigated on the different surfaces. Chondrocyte morphology is shown to be influenced by the microtopography of the system as obtained by scanning electron microscopy and atomic force microscopy (AFM). The cytoplasmatic distribution of a focal adhesion protein, tensin, is followed as a function of time. Since the effect of surface topography on cell morphology is a consequence of the process of interaction between the extracellular matrix (ECM) proteins, adsorbed on the surface of the material, and related cell adhesion molecules, the conformation of one ECM protein, fibronectin, adsorbed on the different substrates was investigated by means of AFM.</abstract><cop>United States</cop><pub>Mary Ann Liebert, Inc</pub><pmid>18823278</pmid><doi>10.1089/ten.tea.2007.0270</doi><tpages>12</tpages></addata></record> |
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subjects | Actins - metabolism Biocompatible Materials - chemistry Cartilage cells Cell Differentiation Chondrocytes - cytology Chondrocytes - metabolism Chondrocytes - ultrastructure Fibronectins - chemistry Health aspects Humans Lactic Acid - chemistry Methods Microfilament Proteins - metabolism Microscopy Microscopy, Atomic Force Microscopy, Electron, Scanning Polymers - chemistry Protein Conformation Tensins Tissue engineering Tissue Engineering - methods Topographical drawing |
title | Human Chondrocyte Morphology, Its Dedifferentiation, and Fibronectin Conformation on Different PLLA Microtopographies |
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