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Tissue determinants of nuclear magnetic resonance relaxation times. Effect of water and collagen content in muscle and tendon. 1989

T D Scholz, and S R Fleagle, and T L Burns, and D J Skorton
Cardiovascular Center and University of Iowa, Iowa City.

Previous studies have suggested a possible relationship between tissue collagen content and nuclear magnetic resonance (NMR) relaxation times. To further investigate this relationship, we studied skeletal muscle, tendon, and the muscle/tendon transition area of normal gastrocnemius muscle from 10 dogs, and determined tissue water and collagen (hydroxyproline) content and NMR T1 and T2 relaxation times at 20 MHz. Water and hydroxyproline contents and T1 and T2 were significantly different among the three tissues. Both spin-lattice and spin-spin relaxation times were linearly related to tissue water content. A significant curvilinear inverse relationship between T1 and hydroxyproline (r2 = 0.93) and a significant inverse curvilinear relationship between T2 and hydroxyproline (r2 = 0.92) were found. Statistically controlling for hydroxy-proline concentration eliminated differences in T1 and T2 among the muscle, muscle/tendon transition, and tendon groups. Thus, NMR relaxation times of skeletal muscle and tendon appear to be influenced by both tissue water and collagen content.

UI MeSH Term Description Entries
D009132 Muscles Contractile tissue that produces movement in animals. Muscle Tissue,Muscle,Muscle Tissues,Tissue, Muscle,Tissues, Muscle
D009682 Magnetic Resonance Spectroscopy Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING). In Vivo NMR Spectroscopy,MR Spectroscopy,Magnetic Resonance,NMR Spectroscopy,NMR Spectroscopy, In Vivo,Nuclear Magnetic Resonance,Spectroscopy, Magnetic Resonance,Spectroscopy, NMR,Spectroscopy, Nuclear Magnetic Resonance,Magnetic Resonance Spectroscopies,Magnetic Resonance, Nuclear,NMR Spectroscopies,Resonance Spectroscopy, Magnetic,Resonance, Magnetic,Resonance, Nuclear Magnetic,Spectroscopies, NMR,Spectroscopy, MR
D001834 Body Water Fluids composed mainly of water found within the body. Water, Body
D003094 Collagen A polypeptide substance comprising about one third of the total protein in mammalian organisms. It is the main constituent of SKIN; CONNECTIVE TISSUE; and the organic substance of bones (BONE AND BONES) and teeth (TOOTH). Avicon,Avitene,Collagen Felt,Collagen Fleece,Collagenfleece,Collastat,Dermodress,Microfibril Collagen Hemostat,Pangen,Zyderm,alpha-Collagen,Collagen Hemostat, Microfibril,alpha Collagen
D004285 Dogs The domestic dog, Canis familiaris, comprising about 400 breeds, of the carnivore family CANIDAE. They are worldwide in distribution and live in association with people. (Walker's Mammals of the World, 5th ed, p1065) Canis familiaris,Dog
D006909 Hydroxyproline A hydroxylated form of the imino acid proline. A deficiency in ASCORBIC ACID can result in impaired hydroxyproline formation. Oxyproline,4-Hydroxyproline,cis-4-Hydroxyproline,4 Hydroxyproline,cis 4 Hydroxyproline
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D013710 Tendons Fibrous bands or cords of CONNECTIVE TISSUE at the ends of SKELETAL MUSCLE FIBERS that serve to attach the MUSCLES to bones and other structures. Endotenon,Epotenon,Tendons, Para-Articular,Tendons, Paraarticular,Endotenons,Epotenons,Para-Articular Tendon,Para-Articular Tendons,Paraarticular Tendon,Paraarticular Tendons,Tendon,Tendon, Para-Articular,Tendon, Paraarticular,Tendons, Para Articular

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