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Heikki J. Helminen - One of the best experts on this subject based on the ideXlab platform.
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Quantitative Analysis of Collagen Network Structure and Fibril Dimensions in Cartilage Repair with Autologous Chondrocyte Transplantation
Cells tissues organs, 2010Co-Authors: Teemu K. Långsjö, Mika M Hyttinen, Heikki J. Helminen, Anna Vasara, Mikko J. Lammi, Antti Kaukinen, Ilkka KivirantaAbstract:Objective: The aim of this study was to undertake a stereological analysis to quantify the dimensions of the Collagen Network in the repair tissue of porcine joints after they had b
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Physical exercise improves properties of bone and its Collagen Network in growing and maturing mice.
Calcified tissue international, 2009Co-Authors: Hanna Isaksson, Jari Arokoski, Viivi Tolvanen, Mikko A.j. Finnilä, Jarkko T. Iivarinen, Juha Tuukkanen, Kari Seppänen, Pieter A.j. Brama, Jukka S. Jurvelin, Heikki J. HelminenAbstract:This study characterized bone structure, composition, and mechanical properties in growing male mice. The development of the Collagen Network during maturation was monitored, and the effect of voluntary physical exercise was investigated. We hypothesized that increased bone loading from exercise would increase the amount and improve the properties of the Collagen Network during growth and maturation. Half of the mice (total n = 168) had access to running wheels, while half were kept sedentary. Weight and running activity were recorded, and groups of mice were killed at 1, 2, 4, and 6 months of age. The Collagen Network was assessed by biochemical evaluation of Collagen content and cross-links and by tensile testing of decalcified bone. Mineralized femur was analyzed with pQCT and three-point-bending and femoral neck–strength tests. After 6 months, the exercising mice had 10% lower body weight than the sedentary group. There was no difference in the amount of Collagen or Collagen cross-links, while tensile testing had higher breaking force and stiffness of the Collagen Network in runners after 4 months but not after 6 months. The bone mineral density and cross-sectional area were higher in the running group after 6 months. Runners also showed higher breaking force and stiffness of the diaphysis and the femoral neck at 2 and 6 months. The significant modulation of mechanical properties of the Collagen Network without any change in Collagen content indicates that physical exercise improves properties of the Collagen Network in maturing bone. The improvement after exercise of the properties of mineralized bone appears to be more pronounced and long-lasting compared to the early improved properties of the Collagen Network.
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Changes in spatial Collagen content and Collagen Network architecture in porcine articular cartilage during growth and maturation
Osteoarthritis and cartilage, 2008Co-Authors: Jarno Rieppo, Mika M Hyttinen, Jukka S. Jurvelin, Erja Halmesmäki, Henri Ruotsalainen, Anna Vasara, Ilkka Kiviranta, Heikki J. HelminenAbstract:Summary Objectives The present study was designed to reveal changes in the Collagen Network architecture and Collagen content in cartilage during growth and maturation of pigs. Methods Femoral groove articular cartilage specimens were collected from 4-, 11- and 21-month-old domestic pigs ( n =12 in each group). The animal care conditions were kept constant throughout the study. Polarized light microscopy was used to determine the Collagen fibril Network birefringence, fibril orientation and parallelism. Infrared spectroscopy was used to monitor changes in the spatial Collagen content in cartilage tissue. Results During growth, gradual alterations were recorded in the Collagen Network properties. At 4 months of age, a major part of the Collagen fibrils was oriented parallel to the cartilage surface throughout the tissue. However, the fibril orientation changed considerably as skeletal maturation progressed. At 21 months of age, the fibrils of the deep zone cartilage ran predominantly at right angles to the cartilage surface. The Collagen content increased and its depthwise distribution changed during growth and maturation. A significant increase of the Collagen Network birefringence was observed in the deep tissue at the age of 21 months. Conclusions The present study revealed dynamic changes of the Collagen Network during growth and maturation of the pigs. The structure of the Collagen Network of young pigs gradually approached a Network with the classical Benninghoff architecture. The probable explanation for the alterations is growth of the bone epiphysis with simultaneous adaptation of the cartilage to increased joint loading. The maturation of articular cartilage advances gradually with age and offers, in principle, the possibility to influence the quality of the tissue, especially by habitual joint loading. These observations in porcine cartilage may be of significance with respect to the maturation of human articular cartilage.
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Practical considerations in the use of polarized light microscopy in the analysis of the Collagen Network in articular cartilage
Microscopy research and technique, 2008Co-Authors: Jarno Rieppo, Heikki J. Helminen, Jukka S. Jurvelin, Ilkka Kiviranta, Jarmo Hallikainen, Mika M HyttinenAbstract:Polarized light microscopy is a traditional method for visualizing the Collagen Network architecture of articular cartilage. Articular cartilage repair and tissue engineering studies have raised new demands for techniques capable of quantitative characterization of the scar and repair tissues, including properties of the Collagen Network. Modern polarized light microscopy can be used to measure Collagen fibril orientation, parallelism, and birefringence. New commercial instruments are computer controlled and the measurements are easy to perform. However, often the interpretation of results causes difficulties, even errors, because the theoretical aspects of the technique are demanding. The aim of this study was to describe the instrumentation and properties of a modern polarized light microscope, to point out some sources of error in the interpretation of the results, and to recall the theoretical background of the polarized light microscopy. Microsc. Res. Tech., 2008. © 2007 Wiley-Liss, Inc.
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Inactivation of one allele of the type II Collagen gene alters the Collagen Network in murine articular cartilage and makes cartilage softer
Annals of the rheumatic diseases, 2001Co-Authors: Mika M Hyttinen, T Lapvetelainen, Jukka S. Jurvelin, Juha Toyras, Lindblom J, Darwin J. Prockop, Machiko Arita, Heikki J. HelminenAbstract:OBJECTIVE To evaluate the influence of inactivation of one allele (“heterozygous knockout” or “heterozygous inactivation”) of the type II proCollagen gene (Col2a1) on the biomechanical properties and structure of the articular cartilage and subchondral bone in 15 month old mice. METHODS Indentation stiffness of the humerus head articular cartilage was measured by a microindentation method. Cartilage and subchondral bone were prepared for digital densitometry of proteoglycans (PGs), polarised light microscopy (PLM) of Collagen, and osteoarthrosis (OA) grading. RESULTS Heterozygous inactivation of the Col2a1 gene softened articular cartilage (p=0.002) as measured by indentation stiffness ((mean (SEM) 0.50 (0.07) MPa v 0.94 (0.13) MPa in controls). Fibrillar Collagen Network exhibited lower birefringence in the intermediate (p=0.04) and deep zones (p=0.01) of cartilage by PLM, indicating either decreased Collagen content or a lower degree of fibril parallelism in the knockout mice. The total and zonal thicknesses of articular cartilage were unchanged. Zonal PG contents did not differ significantly. In knockout mice, the prevalence of superficial fibrillation—that is, a sign of OA, was higher than in controls (73% v 21%, p=0.002). The Collagen induced birefringence of the superficial zone was not reduced. The subchondral bone volume fraction was lower in knockout mice than in controls, 31% v 43% (p=0.01), and optical retardation values in PLM of bone Collagen were slightly but significantly lower (p=0.01). CONCLUSION Heterozygous inactivation of the Col2a1 gene made articular cartilage softer, altered the Collagenous Network, reduced subchondral bone volume, and altered its microstructure. Changes in the cartilage Collagen Network probably contributed to increased susceptibility to OA.
Gerard Deleris - One of the best experts on this subject based on the ideXlab platform.
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analysis of type i and iv Collagens by ft ir spectroscopy and imaging for a molecular investigation of skeletal muscle connective tissue
Analytical and Bioanalytical Chemistry, 2006Co-Authors: Cyril Petibois, Katia Wehbe, Jeanpaul Delage, Gilles Gouspillou, Gerard DelerisAbstract:Many muscular diseases result from abnormal organization of connective tissue and/or Collagen Network formation. Only a few molecular imaging techniques are able to analyze this Collagen Network by differentiating Collagen types. In this study, FT-IR spectroscopy was used to analyze type I and IV Collagens, the most important compounds of which are perimysium and endomysium, respectively. Secondary structure of Collagen types was determined by curve-fitting the 1,700–1,480 cm−1 spectral interval. Type I Collagen could be differentiated from type IV by its higher amounts of triple helix and α-helix, but lower amounts of β-sheets (P < 0.01). FT-IR imaging was then used to determine structural features of perimysium and endomysium Collagen Network in bovine Flexor carpi radialis muscle. Secondary structure of proteins contained in perimysium and endomysium was found to be very close to type I and IV Collagens, respectively. FT-IR spectroscopy and imaging are thus analytical tools that might be used for investigating biodistribution and assembly of Collagen types in connective tissues.
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Analysis of type I and IV Collagens by FT-IR spectroscopy and imaging for a molecular investigation of skeletal muscle connective tissue.
Analytical and bioanalytical chemistry, 2006Co-Authors: Cyril Petibois, Katia Wehbe, Jeanpaul Delage, Gilles Gouspillou, Gerard DelerisAbstract:Many muscular diseases result from abnormal organization of connective tissue and/or Collagen Network formation. Only a few molecular imaging techniques are able to analyze this Collagen Network by differentiating Collagen types. In this study, FT-IR spectroscopy was used to analyze type I and IV Collagens, the most important compounds of which are perimysium and endomysium, respectively. Secondary structure of Collagen types was determined by curve-fitting the 1,700-1,480 cm(-1) spectral interval. Type I Collagen could be differentiated from type IV by its higher amounts of triple helix and alpha-helix, but lower amounts of beta-sheets (P < 0.01). FT-IR imaging was then used to determine structural features of perimysium and endomysium Collagen Network in bovine Flexor carpi radialis muscle. Secondary structure of proteins contained in perimysium and endomysium was found to be very close to type I and IV Collagens, respectively. FT-IR spectroscopy and imaging are thus analytical tools that might be used for investigating biodistribution and assembly of Collagen types in connective tissues.
Mika M Hyttinen - One of the best experts on this subject based on the ideXlab platform.
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Quantitative Analysis of Collagen Network Structure and Fibril Dimensions in Cartilage Repair with Autologous Chondrocyte Transplantation
Cells tissues organs, 2010Co-Authors: Teemu K. Långsjö, Mika M Hyttinen, Heikki J. Helminen, Anna Vasara, Mikko J. Lammi, Antti Kaukinen, Ilkka KivirantaAbstract:Objective: The aim of this study was to undertake a stereological analysis to quantify the dimensions of the Collagen Network in the repair tissue of porcine joints after they had b
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Changes in spatial Collagen content and Collagen Network architecture in porcine articular cartilage during growth and maturation
Osteoarthritis and cartilage, 2008Co-Authors: Jarno Rieppo, Mika M Hyttinen, Jukka S. Jurvelin, Erja Halmesmäki, Henri Ruotsalainen, Anna Vasara, Ilkka Kiviranta, Heikki J. HelminenAbstract:Summary Objectives The present study was designed to reveal changes in the Collagen Network architecture and Collagen content in cartilage during growth and maturation of pigs. Methods Femoral groove articular cartilage specimens were collected from 4-, 11- and 21-month-old domestic pigs ( n =12 in each group). The animal care conditions were kept constant throughout the study. Polarized light microscopy was used to determine the Collagen fibril Network birefringence, fibril orientation and parallelism. Infrared spectroscopy was used to monitor changes in the spatial Collagen content in cartilage tissue. Results During growth, gradual alterations were recorded in the Collagen Network properties. At 4 months of age, a major part of the Collagen fibrils was oriented parallel to the cartilage surface throughout the tissue. However, the fibril orientation changed considerably as skeletal maturation progressed. At 21 months of age, the fibrils of the deep zone cartilage ran predominantly at right angles to the cartilage surface. The Collagen content increased and its depthwise distribution changed during growth and maturation. A significant increase of the Collagen Network birefringence was observed in the deep tissue at the age of 21 months. Conclusions The present study revealed dynamic changes of the Collagen Network during growth and maturation of the pigs. The structure of the Collagen Network of young pigs gradually approached a Network with the classical Benninghoff architecture. The probable explanation for the alterations is growth of the bone epiphysis with simultaneous adaptation of the cartilage to increased joint loading. The maturation of articular cartilage advances gradually with age and offers, in principle, the possibility to influence the quality of the tissue, especially by habitual joint loading. These observations in porcine cartilage may be of significance with respect to the maturation of human articular cartilage.
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Practical considerations in the use of polarized light microscopy in the analysis of the Collagen Network in articular cartilage
Microscopy research and technique, 2008Co-Authors: Jarno Rieppo, Heikki J. Helminen, Jukka S. Jurvelin, Ilkka Kiviranta, Jarmo Hallikainen, Mika M HyttinenAbstract:Polarized light microscopy is a traditional method for visualizing the Collagen Network architecture of articular cartilage. Articular cartilage repair and tissue engineering studies have raised new demands for techniques capable of quantitative characterization of the scar and repair tissues, including properties of the Collagen Network. Modern polarized light microscopy can be used to measure Collagen fibril orientation, parallelism, and birefringence. New commercial instruments are computer controlled and the measurements are easy to perform. However, often the interpretation of results causes difficulties, even errors, because the theoretical aspects of the technique are demanding. The aim of this study was to describe the instrumentation and properties of a modern polarized light microscope, to point out some sources of error in the interpretation of the results, and to recall the theoretical background of the polarized light microscopy. Microsc. Res. Tech., 2008. © 2007 Wiley-Liss, Inc.
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Inactivation of one allele of the type II Collagen gene alters the Collagen Network in murine articular cartilage and makes cartilage softer
Annals of the rheumatic diseases, 2001Co-Authors: Mika M Hyttinen, T Lapvetelainen, Jukka S. Jurvelin, Juha Toyras, Lindblom J, Darwin J. Prockop, Machiko Arita, Heikki J. HelminenAbstract:OBJECTIVE To evaluate the influence of inactivation of one allele (“heterozygous knockout” or “heterozygous inactivation”) of the type II proCollagen gene (Col2a1) on the biomechanical properties and structure of the articular cartilage and subchondral bone in 15 month old mice. METHODS Indentation stiffness of the humerus head articular cartilage was measured by a microindentation method. Cartilage and subchondral bone were prepared for digital densitometry of proteoglycans (PGs), polarised light microscopy (PLM) of Collagen, and osteoarthrosis (OA) grading. RESULTS Heterozygous inactivation of the Col2a1 gene softened articular cartilage (p=0.002) as measured by indentation stiffness ((mean (SEM) 0.50 (0.07) MPa v 0.94 (0.13) MPa in controls). Fibrillar Collagen Network exhibited lower birefringence in the intermediate (p=0.04) and deep zones (p=0.01) of cartilage by PLM, indicating either decreased Collagen content or a lower degree of fibril parallelism in the knockout mice. The total and zonal thicknesses of articular cartilage were unchanged. Zonal PG contents did not differ significantly. In knockout mice, the prevalence of superficial fibrillation—that is, a sign of OA, was higher than in controls (73% v 21%, p=0.002). The Collagen induced birefringence of the superficial zone was not reduced. The subchondral bone volume fraction was lower in knockout mice than in controls, 31% v 43% (p=0.01), and optical retardation values in PLM of bone Collagen were slightly but significantly lower (p=0.01). CONCLUSION Heterozygous inactivation of the Col2a1 gene made articular cartilage softer, altered the Collagenous Network, reduced subchondral bone volume, and altered its microstructure. Changes in the cartilage Collagen Network probably contributed to increased susceptibility to OA.
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Regular joint loading in youth assists in the establishment and strengthening of the Collagen Network of articular cartilage and contributes to the prevention of osteoarthrosis later in life: a hypothesis.
Journal of bone and mineral metabolism, 2000Co-Authors: Heikki J. Helminen, Jari Arokoski, T Lapvetelainen, Mika M Hyttinen, Jukka S. Jurvelin, Ilkka Kiviranta, Mikko J. Lammi, Markku TammiAbstract:Regular joint loading in youth assists in the establishment and strengthening of the Collagen Network of articular cartilage and contributes to the prevention of osteoarthrosis later in life. A hypothesis.
Jukka S. Jurvelin - One of the best experts on this subject based on the ideXlab platform.
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Alterations in structure and properties of Collagen Network of osteoarthritic and repaired cartilage modify knee joint stresses
Biomechanics and modeling in mechanobiology, 2010Co-Authors: Mika E. Mononen, Jukka S. Jurvelin, Petro Julkunen, Ilkka Kiviranta, Juha Toyras, Rami K KorhonenAbstract:Organization of the Collagen Network is known to be different in healthy, osteoarthritic and repaired cartilage. The aim of the study was to investigate how the structure and properties of Collagen Network of cartilage modulate stresses in a knee joint with osteoarthritis or cartilage repair. Magnetic resonance imaging (MRI) at 1.5 T was conducted for a knee joint of a male subject. Articular cartilage and menisci in the knee joint were segmented, and a finite element mesh was constructed based on the two-dimensional section in sagittal projection. Then, the knee joint stresses were simulated under impact loads by implementing the structure and properties of healthy, osteoarthritic and repaired cartilage in the models. During the progression of osteoarthritis, characterized especially by the progressive increase in the Collagen fibrillation from the superficial to the deeper layers, the stresses were reduced in the superficial zone of cartilage, while they were increased in and under menisci. Increased fibril Network stiffness of repair tissue with randomly organized Collagen fibril Network reduced the peak stresses in the adjacent tissue and strains at the repair-adjacent cartilage interface. High Collagen fibril strains were indicative of stress concentration areas in osteoarthritic and repaired cartilage. The Collagen Network orientation and stiffness controlled the stress distributions in healthy, osteoarthritic and repaired cartilage. The evaluation of articular cartilage function using clinical MRI and biomechanical modeling could enable noninvasive estimation of osteoarthritis progression and monitoring of cartilage repair. This study presents a step toward those goals.
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Physical exercise improves properties of bone and its Collagen Network in growing and maturing mice.
Calcified tissue international, 2009Co-Authors: Hanna Isaksson, Jari Arokoski, Viivi Tolvanen, Mikko A.j. Finnilä, Jarkko T. Iivarinen, Juha Tuukkanen, Kari Seppänen, Pieter A.j. Brama, Jukka S. Jurvelin, Heikki J. HelminenAbstract:This study characterized bone structure, composition, and mechanical properties in growing male mice. The development of the Collagen Network during maturation was monitored, and the effect of voluntary physical exercise was investigated. We hypothesized that increased bone loading from exercise would increase the amount and improve the properties of the Collagen Network during growth and maturation. Half of the mice (total n = 168) had access to running wheels, while half were kept sedentary. Weight and running activity were recorded, and groups of mice were killed at 1, 2, 4, and 6 months of age. The Collagen Network was assessed by biochemical evaluation of Collagen content and cross-links and by tensile testing of decalcified bone. Mineralized femur was analyzed with pQCT and three-point-bending and femoral neck–strength tests. After 6 months, the exercising mice had 10% lower body weight than the sedentary group. There was no difference in the amount of Collagen or Collagen cross-links, while tensile testing had higher breaking force and stiffness of the Collagen Network in runners after 4 months but not after 6 months. The bone mineral density and cross-sectional area were higher in the running group after 6 months. Runners also showed higher breaking force and stiffness of the diaphysis and the femoral neck at 2 and 6 months. The significant modulation of mechanical properties of the Collagen Network without any change in Collagen content indicates that physical exercise improves properties of the Collagen Network in maturing bone. The improvement after exercise of the properties of mineralized bone appears to be more pronounced and long-lasting compared to the early improved properties of the Collagen Network.
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Changes in spatial Collagen content and Collagen Network architecture in porcine articular cartilage during growth and maturation
Osteoarthritis and cartilage, 2008Co-Authors: Jarno Rieppo, Mika M Hyttinen, Jukka S. Jurvelin, Erja Halmesmäki, Henri Ruotsalainen, Anna Vasara, Ilkka Kiviranta, Heikki J. HelminenAbstract:Summary Objectives The present study was designed to reveal changes in the Collagen Network architecture and Collagen content in cartilage during growth and maturation of pigs. Methods Femoral groove articular cartilage specimens were collected from 4-, 11- and 21-month-old domestic pigs ( n =12 in each group). The animal care conditions were kept constant throughout the study. Polarized light microscopy was used to determine the Collagen fibril Network birefringence, fibril orientation and parallelism. Infrared spectroscopy was used to monitor changes in the spatial Collagen content in cartilage tissue. Results During growth, gradual alterations were recorded in the Collagen Network properties. At 4 months of age, a major part of the Collagen fibrils was oriented parallel to the cartilage surface throughout the tissue. However, the fibril orientation changed considerably as skeletal maturation progressed. At 21 months of age, the fibrils of the deep zone cartilage ran predominantly at right angles to the cartilage surface. The Collagen content increased and its depthwise distribution changed during growth and maturation. A significant increase of the Collagen Network birefringence was observed in the deep tissue at the age of 21 months. Conclusions The present study revealed dynamic changes of the Collagen Network during growth and maturation of the pigs. The structure of the Collagen Network of young pigs gradually approached a Network with the classical Benninghoff architecture. The probable explanation for the alterations is growth of the bone epiphysis with simultaneous adaptation of the cartilage to increased joint loading. The maturation of articular cartilage advances gradually with age and offers, in principle, the possibility to influence the quality of the tissue, especially by habitual joint loading. These observations in porcine cartilage may be of significance with respect to the maturation of human articular cartilage.
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Practical considerations in the use of polarized light microscopy in the analysis of the Collagen Network in articular cartilage
Microscopy research and technique, 2008Co-Authors: Jarno Rieppo, Heikki J. Helminen, Jukka S. Jurvelin, Ilkka Kiviranta, Jarmo Hallikainen, Mika M HyttinenAbstract:Polarized light microscopy is a traditional method for visualizing the Collagen Network architecture of articular cartilage. Articular cartilage repair and tissue engineering studies have raised new demands for techniques capable of quantitative characterization of the scar and repair tissues, including properties of the Collagen Network. Modern polarized light microscopy can be used to measure Collagen fibril orientation, parallelism, and birefringence. New commercial instruments are computer controlled and the measurements are easy to perform. However, often the interpretation of results causes difficulties, even errors, because the theoretical aspects of the technique are demanding. The aim of this study was to describe the instrumentation and properties of a modern polarized light microscope, to point out some sources of error in the interpretation of the results, and to recall the theoretical background of the polarized light microscopy. Microsc. Res. Tech., 2008. © 2007 Wiley-Liss, Inc.
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t2 relaxation time mapping reveals age and species related diversity of Collagen Network architecture in articular cartilage
Osteoarthritis and Cartilage, 2006Co-Authors: Mikko J Nissi, Jukka S. Jurvelin, Jarno Rieppo, Juha Toyras, Mikko S Laasanen, I Kiviranta, Miika T NieminenAbstract:Summary Objective The magnetic resonance imaging (MRI) parameter T 2 relaxation time has been shown to be sensitive to the Collagen Network architecture of articular cartilage. The aim of the study was to investigate the agreement of T 2 relaxation time mapping and polarized light microscopy (PLM) for the determination of histological properties (i.e., zone and fibril organization) of articular cartilage. Methods T 2 relaxation time was determined at 9.4T field strength in healthy adult human, juvenile bovine and juvenile porcine patellar cartilage, and related to Collagen anisotropy and fibril angle as measured by quantitative PLM. Results Both T 2 and PLM revealed a mutually consistent but varying number of Collagen-associated laminae (3, 3–5 or 3–7 laminae in human, porcine and bovine cartilage, respectively). Up to 44% of the depth-wise variation in T 2 was accounted for by the changing anisotropy of Collagen fibrils, confirming that T 2 contrast of articular cartilage is strongly affected by the Collagen fibril anisotropy. A good correspondence was observed between the thickness of T 2 -laminae and Collagenous zones as determined from PLM anisotropy measurements ( r =0.91, r =0.95 and r =0.91 for human, bovine and porcine specimens, respectively). Conclusions According to the present results, T 2 mapping is capable of detecting histological differences in cartilage Collagen architecture among species, likely to be strongly related to the differences in maturation of the tissue. This diversity in the MRI appearance of healthy articular cartilage should also be recognized when using juvenile animal tissue as a model for mature human cartilage in experimental studies.
Cyril Petibois - One of the best experts on this subject based on the ideXlab platform.
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analysis of type i and iv Collagens by ft ir spectroscopy and imaging for a molecular investigation of skeletal muscle connective tissue
Analytical and Bioanalytical Chemistry, 2006Co-Authors: Cyril Petibois, Katia Wehbe, Jeanpaul Delage, Gilles Gouspillou, Gerard DelerisAbstract:Many muscular diseases result from abnormal organization of connective tissue and/or Collagen Network formation. Only a few molecular imaging techniques are able to analyze this Collagen Network by differentiating Collagen types. In this study, FT-IR spectroscopy was used to analyze type I and IV Collagens, the most important compounds of which are perimysium and endomysium, respectively. Secondary structure of Collagen types was determined by curve-fitting the 1,700–1,480 cm−1 spectral interval. Type I Collagen could be differentiated from type IV by its higher amounts of triple helix and α-helix, but lower amounts of β-sheets (P < 0.01). FT-IR imaging was then used to determine structural features of perimysium and endomysium Collagen Network in bovine Flexor carpi radialis muscle. Secondary structure of proteins contained in perimysium and endomysium was found to be very close to type I and IV Collagens, respectively. FT-IR spectroscopy and imaging are thus analytical tools that might be used for investigating biodistribution and assembly of Collagen types in connective tissues.
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Analysis of type I and IV Collagens by FT-IR spectroscopy and imaging for a molecular investigation of skeletal muscle connective tissue.
Analytical and bioanalytical chemistry, 2006Co-Authors: Cyril Petibois, Katia Wehbe, Jeanpaul Delage, Gilles Gouspillou, Gerard DelerisAbstract:Many muscular diseases result from abnormal organization of connective tissue and/or Collagen Network formation. Only a few molecular imaging techniques are able to analyze this Collagen Network by differentiating Collagen types. In this study, FT-IR spectroscopy was used to analyze type I and IV Collagens, the most important compounds of which are perimysium and endomysium, respectively. Secondary structure of Collagen types was determined by curve-fitting the 1,700-1,480 cm(-1) spectral interval. Type I Collagen could be differentiated from type IV by its higher amounts of triple helix and alpha-helix, but lower amounts of beta-sheets (P < 0.01). FT-IR imaging was then used to determine structural features of perimysium and endomysium Collagen Network in bovine Flexor carpi radialis muscle. Secondary structure of proteins contained in perimysium and endomysium was found to be very close to type I and IV Collagens, respectively. FT-IR spectroscopy and imaging are thus analytical tools that might be used for investigating biodistribution and assembly of Collagen types in connective tissues.