Collagen, cross-linking, and advanced glycation end products in aging human skeletal muscle

• Published in: Journal of applied physiology (1985) Vol. 103; no. 6; pp. 2068 - 2076
• Main Authors: Haus, Jacob M, Carrithers, John A, Trappe, Scott W, Trappe, Todd A
• Format: Journal Article
• Language: English
• Published: Bethesda, MD Am Physiological Soc 01-12-2007; American Physiological Society
• Subjects: Actins - metabolism; Activities of Daily Living; Adult; Age Factors; Aged; Aged, 80 and over; Aging; Aging - metabolism; Aging - pathology; Amino Acids - metabolism; Arginine - analogs & derivatives; Arginine - metabolism; Biological and medical sciences; Biopsy; Collagen - metabolism; Female; Fundamental and applied biological sciences. Psychology; Glycation End Products, Advanced - metabolism; Humans; Lysine - analogs & derivatives; Lysine - metabolism; Male; Muscle Contraction; Muscle Strength; Muscular Diseases - metabolism; Muscular Diseases - pathology; Muscular Diseases - physiopathology; Musculoskeletal system; Myofibrils - metabolism; Myosins - metabolism; Proteins; Quadriceps Muscle - metabolism; Quadriceps Muscle - pathology; Quadriceps Muscle - physiopathology; Human; Senescence; Hydroxyproline; Reaction product; Ageing; Glycoprotein; Striated muscle; Glycation; Vertebrata; Mammalia; hydroxylysylpyridinoline; Actin; Collagen; Myosin; pentosidine; sarcopenia
• ISSN: 8750-7587; 1522-1601
• DOI: 10.1152/japplphysiol.00670.2007

Human Performance Laboratory, Ball State University, Muncie, Indiana
Submitted 23 June 2007
; accepted in final form 20 September 2007
We examined intramuscular endomysial collagen, cross-linking, and advanced glycation end products, as well as the general and contractile protein concentration of 20 young (25 ± 3 yr) and 22 old (78 ± 6 yr, range: 70–93 yr) sedentary men and women to better understand the underlying basis of changes in skeletal muscle mass and function that occur with aging. The old individuals had an impaired ability (increased time) ( P < 0.05) to climb stairs (80%), rise from a chair (56%), and walk (44%), as well as lower ( P < 0.05) quadriceps muscle volume (–29%), muscle strength (–35%), muscle power (–48%), and strength (–17%) and power (–33%) normalized to muscle size. Vastus lateralis muscle biopsies revealed that intramuscular endomysial collagen (young: 9.6 ± 1.1, old: 10.2 ± 1.2 µg/mg muscle wet wt) and collagen cross-linking (hydroxylysylpyridinoline) (young: 395 ± 65, old: 351 ± 45 mmol hydroxylysylpyridinoline/mol collagen) were unchanged ( P > 0.05) with aging. The advanced glycation end product, pentosidine, was increased ( P < 0.05) by 200% (young: 5.2 ± 1.3, old: 15.9 ± 4.5 mmol pentosidine/mol collagen) with aging. While myofibrillar protein concentration was lower (–5%, P < 0.05), the concentration of the main contractile proteins myosin and actin were unchanged ( P > 0.05) with aging. These data suggest that the synthesis and degradation of proteins responsible for the generation (myosin and actin) and transfer (collagen and pyridinoline cross-links) of muscle force are tightly regulated in aging muscle. Glycation-related cross-linking of intramuscular connective tissue may contribute to altered muscle force transmission and muscle function with healthy aging.
hydroxyproline; hydroxylysylpyridinoline; pentosidine; myosin; actin; sarcopenia
Address for reprint requests and other correspondence: T. Trappe, Human Performance Laboratory, Ball State Univ., Muncie, IN 47306 (e-mail: ttrappe{at}bsu.edu )