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Journal of Cachexia, Sarcopenia and Muscle
Published in: Journal of Cachexia, Sarcopenia and Muscle 1/2013

01-03-2013 | Review

Serological muscle loss biomarkers: an overview of current concepts and future possibilities

Authors: Anders Nedergaard, Morten A. Karsdal, Shu Sun, Kim Henriksen

Published in: Journal of Cachexia, Sarcopenia and Muscle | Issue 1/2013

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Abstract

Background

The skeletal muscle mass is the largest organ in the healthy body, comprising 30–40 % of the body weight of an adult man. It confers protection from trauma, locomotion, ventilation, and it represents a “sink” in glucose metabolism and a reservoir of amino acids to other tissues such as the brain and blood cells. Naturally, loss of muscle has dire consequences for health as well as functionality. Muscle loss is a natural consequence of especially aging, inactivity, and their associated metabolic dysfunction, but it is strongly accelerated in critical illness such as organ failure, sepsis, or cancer. Whether this muscle loss is considered a primary or secondary condition, it is known that muscle loss is a symptom that predicts morbidity and mortality and one that is known to impact quality of life and independence. Therefore, monitoring of muscle mass is relevant in a number of pathologies as well as in clinical trials as measures of efficacy as well as safety.

Methods and results

Existing biomarkers of muscle mass or muscle loss have shown to be either too unreliable or too impractical in relation to the perceived clinical benefit to reach regular clinical research or use. We suggest serological neoepitope biomarkers as a possible technology to address some of these problems. Blood biomarkers of this kind have previously been shown to respond with high sensitivity and shorter time to minimum significant change than available biomarkers of muscle mass. We provide brief reviews of existing muscle mass or function biomarker technologies, muscle protein biology, and existing neoepitope biomarkers and proceed to present tentative recommendations on how to select and detect neoepitope biomarkers.

Conclusion

We suggest that serological peptide biomarkers whose tissue and pathology specificity are derived from post-translational modification of proteins in tissues of interest, presenting so-called neoepitopes, represents an exciting candidate technology to fill out an empty niche in biomarker technology.
Literature
1.
Evans W. Skeletal muscle loss: cachexia, sarcopenia, and inactivity. Am J Clin Nutr. 2010;91:1123S–7S.PubMedCrossRef
2.
Fearon K, Evans WJ, Anker SD. Myopenia—a new universal term for muscle wasting. J Cachexia Sarcopenia Muscle. 2011;2:1–3.PubMedCrossRef
3.
Narici MV, Maffulli N. Sarcopenia: characteristics, mechanisms and functional significance. Br Med Bull. 2010;95:139–59.PubMedCrossRef
4.
Evans W. Functional and metabolic consequences of sarcopenia. J Nutr. 1997;127:998S–1003S.PubMed
5.
Miller BF, Olesen JL, Hansen M, et al. Coordinated collagen and muscle protein synthesis in human patella tendon and quadriceps muscle after exercise. J Physiol (Lond). 2005;567:1021–33.CrossRef
6.
White JP, Baynes JW, Welle SL, et al. The regulation of skeletal muscle protein turnover during the progression of cancer cachexia in the Apc(Min/+) mouse. PLoS One. 2011;6:e24650.PubMedCrossRef
7.
Rennie MJ, Selby A, Atherton P, et al. Facts, noise and wishful thinking: muscle protein turnover in aging and human disuse atrophy. ScandJ MedSciSports. 2010;20:5–9.
8.
Rennie MJ, Edwards RH, Emery PW, et al. Depressed protein synthesis is the dominant characteristic of muscle wasting and cachexia. ClinPhysiol. 1983;3:387–98.
9.
Emery PW, Edwards RH, Rennie MJ, et al. Protein synthesis in muscle measured in vivo in cachectic patients with cancer. Br MedJ (ClinResEd). 1984;289:584–6.CrossRef
10.
Morrison WL, Gibson JN, Rennie MJ. Skeletal muscle and whole body protein turnover in cardiac cachexia: influence of branched-chain amino acid administration. Eur J Clin Invest. 1988;18:648–54.PubMedCrossRef
11.
Rutten EPA, Franssen FME, Engelen MPKJ, et al. Greater whole-body myofibrillar protein breakdown in cachectic patients with chronic obstructive pulmonary disease. Am J Clin Nutr. 2006;83:829–34.PubMed
12.
Bonde M, Garnero P, Fledelius C, et al. Measurement of bone degradation products in serum using antibodies reactive with an isomerized form of an 8 amino acid sequence of the C-telopeptide of type I collagen. J Bone Miner Res. 1997;12:1028–34.PubMedCrossRef
13.
Weber M-A, Kinscherf R, Krakowski-Roosen H, et al. Myoglobin plasma level related to muscle mass and fiber composition: a clinical marker of muscle wasting? J Mol Med. 2007;85:887–96.PubMedCrossRef
14.
Tonomura Y, Mori Y, Torii M, et al. Evaluation of the usefulness of biomarkers for cardiac and skeletal myotoxicity in rats. Toxicology. 2009;266:48–54.PubMedCrossRef
15.
Bay-Jensen AC, Leeming DJ, Kleyer A, et al. Ankylosing spondylitis is characterized by an increased turnover of several different metalloproteinase-derived collagen species: a cross-sectional study. Rheumatol Int. doi:10.​1007/​s00296-011-2237-8. Published Online First: 16 November 2011.
16.
Bay-Jensen A-C, Liu Q, Byrjalsen I, et al. Enzyme-linked immunosorbent assay (ELISAs) for metalloproteinase derived type II collagen neoepitope, CIIM–increased serum CIIM in subjects with severe radiographic osteoarthritis. Clin Biochem. 2011;44:423–9.PubMedCrossRef
17.
Henrotin Y, Deberg M, Dubuc J-E, et al. Type II collagen peptides for measuring cartilage degradation. Biorheology. 2004;41:543–7.PubMed
18.
Rissman RA, Poon WW, Blurton-Jones M, et al. Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology. J ClinInvest. 2004;114:121–30.
19.
Mehndiratta P, Mehta S, Manjila SV, et al. Isolated necrotizing myopathy associated with ANTI-PL12 antibody. Muscle Nerve. 2012;46:282–6.PubMedCrossRef
20.
Nakajima A, Yoshino K, Soejima M, et al. High frequencies and co-existing of myositis-specific autoantibodies in patients with idiopathic inflammatory myopathies overlapped to rheumatoid arthritis. Rheumatol Int. 2012;32:2057–61.PubMedCrossRef
21.
Karsdal MA, Henriksen K, Leeming DJ, et al. Novel combinations of post-translational modification (PTM) neo-epitopes provide tissue-specific biochemical markers—are they the cause or the consequence of the disease? Clin Biochem. 2010;43:793–804.PubMedCrossRef
22.
Heymsfield SB, Arteaga C, McManus C, et al. Measurement of muscle mass in humans: validity of the 24-hour urinary creatinine method. Am J Clin Nutr. 1983;37:478–94.PubMed
23.
Wang ZM, Gallagher D, Nelson ME, et al. Total-body skeletal muscle mass: evaluation of 24-h urinary creatinine excretion by computerized axial tomography. Am J Clin Nutr. 1996;63:863–9.PubMed
24.
Hansen M, Trappe T, Crameri RM, et al. Myofibrillar proteolysis in response to voluntary or electrically stimulated muscle contractions in humans. ScandJ MedSciSports. 2009;19:75–82.
25.
Millward DJ. PCB. 3-Methylhistidine turnover in the whole body, and the contribution of skeletal muscle and intestine to urinary 3-methylhistidine excretion in the adult rat. Biochem J. 1983;214:607.PubMed
26.
Bauer DC, Hunter DJ, Abramson SB, et al. Classification of osteoarthritis biomarkers: a proposed approach. Osteoarthr Cartil. 2006;14:723–7.PubMedCrossRef
27.
28.
Hettwer S, Dahinden P, Kucsera S, et al. Elevated levels of a C-terminal agrin fragment identifies a new subset of sarcopenia patients. Exp Gerontol. doi:10.​1016/​j.​exger.​2012.​03.​002. Published Online First: 11 March 2012.
29.
Huang J, Forsberg NE. Role of calpain in skeletal-muscle protein degradation. Proc Natl Acad Sci USA. 1998;95:12100–5.PubMedCrossRef
30.
Du J, Hu Z, Mitch WE. Molecular mechanisms activating muscle protein degradation in chronic kidney disease and other catabolic conditions. Eur J Clin Invest. 2005;35:157–63.PubMedCrossRef
31.
Lee SW, Dai G, Hu Z, et al. Regulation of muscle protein degradation: coordinated control of apoptotic and ubiquitin–proteasome systems by phosphatidylinositol 3 kinase. J Am Soc Nephrol. 2004;15:1537–45.PubMedCrossRef
32.
Zhao J, Brault JJ, Schild A, et al. FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. Cell Metabolism. 2007;6:472–83.PubMedCrossRef
33.
Clark KA, McElhinny AS, Beckerle MC, et al. Striated muscle cytoarchitecture: an intricate web of form and function. Annu Rev Cell Dev Biol. 2002;18:637–706.PubMedCrossRef
34.
Gosker HR, Engelen MPKJ, van Mameren H, et al. Muscle fiber type IIX atrophy is involved in the loss of fat-free mass in chronic obstructive pulmonary disease. Am J Clin Nutr. 2002;76:113–9.PubMed
35.
Bloch RJ, Gonzalez-Serratos H. Lateral force transmission across costameres in skeletal muscle. Exerc Sport Sci Rev. 2003;31:73–8.PubMedCrossRef
36.
Anastasi G, Amato A, Tarone G, et al. Distribution and localization of vinculin–talin–integrin system and dystrophin–glycoprotein complex in human skeletal muscle. Immunohistochemical study using confocal laser scanning microscopy. Cells TissuesOrgans. 2003;175:151–64.CrossRef
37.
Acharyya S, Butchbach MER, Sahenk Z, et al. Dystrophin glycoprotein complex dysfunction: a regulatory link between muscular dystrophy and cancer cachexia. Cancer Cell. 2005;8:421–32.PubMedCrossRef
38.
Oak SA, Zhou YW, Jarrett HW. Skeletal muscle signaling pathway through the dystrophin glycoprotein complex and Rac1. J Biol Chem. 2003;278:39287–95.PubMedCrossRef
39.
Rando TA. The dystrophin–glycoprotein complex, cellular signaling, and the regulation of cell survival in the muscular dystrophies. Muscle Nerve. 2001;24:1575–94.PubMedCrossRef
40.
Bönnemann CG. The collagen VI-related myopathies: muscle meets its matrix. Nat Rev Neurol. 2011;7:379–90.PubMedCrossRef
41.
Pegoraro E, Mancias P, Swerdlow SH, et al. Congenital muscular dystrophy with primary laminin alpha2 (merosin) deficiency presenting as inflammatory myopathy. Ann Neurol. 1996;40:782–91.PubMedCrossRef
42.
Taillandier D, Combaret L, Pouch M-N, et al. The role of ubiquitin-proteasome-dependent proteolysis in the remodelling of skeletal muscle. Proc Nutr Soc. 2004;63:357–61.PubMedCrossRef
43.
Costelli P, Tullio RD, Baccino FM, et al. Activation of Ca(2+)-dependent proteolysis in skeletal muscle and heart in cancer cachexia. Br J Cancer. 2001;84:946–50.PubMedCrossRef
44.
Bechet D, Tassa A, Taillandier D, et al. Lysosomal proteolysis in skeletal muscle. Int J Biochem Cell Biol. 2005;37:2098–114.PubMedCrossRef
45.
Kramerova I, Kudryashova E, Venkatraman G, et al. Calpain 3 participates in sarcomere remodeling by acting upstream of the ubiquitin–proteasome pathway. Hum Mol Genet. 2005;14:2125–34.PubMedCrossRef
46.
Williams AB, Decourten-Myers GM, Fischer JE, et al. Sepsis stimulates release of myofilaments in skeletal muscle by a calcium-dependent mechanism. FASEB J. 1999;13:1435–43.PubMed
47.
Tidball JG, Spencer MJ. Expression of a calpastatin transgene slows muscle wasting and obviates changes in myosin isoform expression during murine muscle disuse. J Physiol (Lond). 2002;545:819–28.CrossRef
48.
Belcastro AN, Shewchuk LD, Raj DA. Exercise-induced muscle injury: a calpain hypothesis. Mol Cell Biochem. 1998;179:135–45.PubMedCrossRef
49.
Zhao J, Brault JJ, Schild A, et al. FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. Cell Metab. 2007;6:472–83.PubMedCrossRef
50.
Capel F, Prod’homme M, Bechet D, et al. Lysosomal and proteasome-dependent proteolysis are differentially regulated by insulin and/or amino acids following feeding in young, mature and old rats. J Nutr Biochem. 2009;20:570–6.PubMedCrossRef
51.
Belizario JE, Lorite MJ, Tisdale MJ. Cleavage of caspases-1, -3, -6, -8 and -9 substrates by proteases in skeletal muscles from mice undergoing cancer cachexia. Br J Cancer. 2001;84:1135–40.PubMedCrossRef
52.
Dargelos E, Poussard S, Brulé C, et al. Calcium-dependent proteolytic system and muscle dysfunctions: a possible role of calpains in sarcopenia. Biochimie. 2008;90:359–68.PubMedCrossRef
53.
Deval C, Mordier S, Obled C, et al. Identification of cathepsin L as a differentially expressed message associated with skeletal muscle wasting. Biochem J. 2001;360:143–50.PubMedCrossRef
54.
Taillandier D, Aurousseau E, Meynial-Denis D, et al. Coordinate activation of lysosomal, Ca 2+-activated and ATP-ubiquitin-dependent proteinases in the unweighted rat soleus muscle. Biochem J. 1996;316:65–72.PubMed
55.
Tsujinaka T, Ebisui C, Fujita J, et al. Muscle undergoes atrophy in association with increase of lysosomal cathepsin activity in interleukin-6 transgenic mouse. Biochem Biophys Res Commun. 1995;207:168–74.PubMedCrossRef
56.
Lecker SH, Jagoe RT, Gilbert A, et al. Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression. FASEB J. 2004;18:39–51.PubMedCrossRef
57.
Yamazaki Y, Kamei Y, Sugita S, et al. The cathepsin L gene is a direct target of FOXO1 in skeletal muscle. Biochem J. 2010;427:171–8.PubMedCrossRef
58.
Jagoe RT, Redfern CP, Roberts RG, et al. Skeletal muscle mRNA levels for cathepsin B, but not components of the ubiquitin–proteasome pathway, are increased in patients with lung cancer referred for thoracotomy. ClinSci(Lond). 2002;102:353–61.CrossRef
59.
Bosutti A, Toigo G, Ciocchi B, et al. Regulation of muscle cathepsin B proteolytic activity in protein-depleted patients with chronic diseases. Clinical nutrition (Edinburgh, Scotland). 2002;21:373–8.CrossRef
60.
Temparis S, Asensi M, Taillandier D, et al. Increased ATP-ubiquitin-dependent proteolysis in skeletal muscles of tumor-bearing rats. Cancer Res. 1994;54:5568–73.PubMed
61.
Matsukura U, Okitani A, Nishimuro T, et al. Mode of degradation of myofibrillar proteins by an endogenous protease, cathepsin L. Biochim Biophys Acta. 1981;662:41–7.PubMedCrossRef
62.
Schwartz W, Bird JW. Degradation of myofibrillar proteins by cathepsins B and D. Biochem J. 1977;167:811–20.PubMed
63.
Giannelli G, De Marzo A, Marinosci F, et al. Matrix metalloproteinase imbalance in muscle disuse atrophy. Histol Histopathol. 2005;20:99–106.PubMed
64.
Carmeli E, Moas M, Reznick AZ, et al. Matrix metalloproteinases and skeletal muscle: a brief review. Muscle Nerve. 2004;29:191–7.PubMedCrossRef
65.
Reznick AZ, Menashe O, Bar-Shai M, et al. Expression of matrix metalloproteinases, inhibitor, and acid phosphatase in muscles of immobilized hindlimbs of rats. Muscle Nerve. 2003;27:51–9.PubMedCrossRef
66.
Li H, Mittal A, Makonchuk DY, et al. Matrix metalloproteinase-9 inhibition ameliorates pathogenesis and improves skeletal muscle regeneration in muscular dystrophy. Hum Mol Genet. 2009;18:2584–98.PubMedCrossRef
67.
Kumar A, Bhatnagar S, Kumar A. Matrix metalloproteinase inhibitor batimastat alleviates pathology and improves skeletal muscle function in dystrophin-deficient mdx mice. Am J Pathol. 2010;177:248–60.PubMedCrossRef
68.
Flink IL, Morkin E. Sequence of the 20-kilodalton heavy chain peptide from the carboxyl-terminus of bovine cardiac myosin subfragment-1. J ClinInvest. 1984;74:639–46.CrossRef
69.
Hanan T, Shaklai N. The role of H2O2-generated myoglobin radical in crosslinking of myosin. Free Radic Res. 1995;22:215–27.PubMedCrossRef
70.
Evangelista AM, Rao VS, Filo AR, et al. Direct regulation of striated muscle myosins by nitric oxide and endogenous nitrosothiols. PLoS One. 2010;5:e11209.PubMedCrossRef
71.
Murakami H, Guillet C, Tardif N, et al. Cumulative 3-nitrotyrosine in specific muscle proteins is associated with muscle loss during aging. Exp Gerontol. 2012;47:129–35.PubMedCrossRef
72.
Barreiro E, Hussain SNA. Protein carbonylation in skeletal muscles: impact on function. Antioxid Redox Signal. 2010;12:417–29.PubMedCrossRef
73.
Magherini F, Abruzzo PM, Puglia M, et al. Proteomic analysis and protein carbonylation profile in trained and untrained rat muscles. J Proteomics. 2012;75:978–92.PubMedCrossRef
74.
Shanely RA, Zergeroglu MA, Lennon SL, et al. Mechanical ventilation-induced diaphragmatic atrophy is associated with oxidative injury and increased proteolytic activity. Am J Respir Crit Care Med. 2002;166:1369–74.PubMedCrossRef
75.
Zergeroglu MA, McKenzie MJ, Shanely RA, et al. Mechanical ventilation-induced oxidative stress in the diaphragm. J Appl Physiol. 2003;95:1116–24.PubMed
76.
Betters JL, Criswell DS, Shanely RA, et al. Trolox attenuates mechanical ventilation-induced diaphragmatic dysfunction and proteolysis. Am J Respir Crit Care Med. 2004;170:1179–84.PubMedCrossRef
77.
McClung JM, Kavazis AN, Whidden MA, et al. Antioxidant administration attenuates mechanical ventilation-induced rat diaphragm muscle atrophy independent of protein kinase B (PKB Akt) signalling. J Physiol (Lond). 2007;585:203–15.CrossRef
78.
McClung JM, Whidden MA, Kavazis AN, et al. Redox regulation of diaphragm proteolysis during mechanical ventilation. Am J Physiol Regul Integr Comp Physiol. 2008;294:R1608–17.PubMedCrossRef
79.
Whidden MA, McClung JM, Falk DJ, et al. Xanthine oxidase contributes to mechanical ventilation-induced diaphragmatic oxidative stress and contractile dysfunction. J Appl Physiol. 2009;106:385–94.PubMedCrossRef
80.
Haehling S, Morley JE, Coats AJS, et al. Ethical guidelines for authorship and publishing in the Journal of Cachexia, Sarcopenia and Muscle. J Cachexia Sarcopenia Muscle. 2010;1:7–8.CrossRef
81.
Ottenheijm CAC, Heunks LMA, Dekhuijzen RPN. Diaphragm adaptations in patients with COPD. Respir Res. 2008;9:12.PubMedCrossRef
82.
Voermans NC, Bönnemann CG, Huijing PA, et al. Clinical and molecular overlap between myopathies and inherited connective tissue diseases. Neuromuscul Disord. 2008;18:843–56.PubMedCrossRef
83.
Ruiz JR, Sui X, Lobelo F, et al. Association between muscular strength and mortality in men: prospective cohort study. BMJ. 2008;337:a439.PubMedCrossRef
84.
Gale C, Martyn C, Cooper C. Grip strength, body composition, and mortality. International Journal of Epidemiology. 2007;36(1):228–35.PubMedCrossRef
85.
Sui X, Laditka JN, Hardin JW, et al. Estimated functional capacity predicts mortality in older adults. J Am Geriatr Soc. 2007;55:1940–7.PubMedCrossRef
86.
Wind H, Gouttebarge V, Kuijer PPFM, et al. Assessment of functional capacity of the musculoskeletal system in the context of work, daily living, and sport: a systematic review. J Occup Rehabil. 2005;15:253–72.PubMedCrossRef
87.
Cesari M, Leeuwenburgh C, Lauretani F, et al. Frailty syndrome and skeletal muscle: results from the Invecchiare in Chianti study. Am J Clin Nutr. 2006;83:1142–8.PubMed
88.
Goodpaster BH, Kelley DE, Thaete FL, et al. Skeletal muscle attenuation determined by computed tomography is associated with skeletal muscle lipid content. J Appl Physiol. 2000;89:104–10.PubMed
89.
Pahor M, Manini T, Cesari M. Sarcopenia: clinical evaluation, biological markers and other evaluation tools. The Journal of Nutrition Health and Aging. 2009;13(8):724–8.CrossRef
90.
Brozek J, Grande F, Anderson JT, et al. Densitometric analysis of body composition: revision of some quantitative assumptions. Ann N Y Acad Sci. 1963;110:113–40.PubMedCrossRef
91.
St-Onge M-P, Wang Z, Horlick M, et al. Dual-energy X-ray absorptiometry lean soft tissue hydration: independent contributions of intra- and extracellular water. Am J Physiol Endocrinol Metab. 2004;287:E842–7.PubMedCrossRef
92.
Kim J, Wang Z, Heymsfield SB, et al. Total-body skeletal muscle mass: estimation by a new dual-energy X-ray absorptiometry method. Am J Clin Nutr. 2002;76:378–83.PubMed
93.
Proctor DN, O’Brien PC, Atkinson EJ, et al. Comparison of techniques to estimate total body skeletal muscle mass in people of different age groups. Am J Physiol. 1999;277:E489–95.PubMed
94.
Kyle UG, Bosaeus I, De Lorenzo AD, et al. Bioelectrical impedance analysis—part I: review of principles and methods. Clinical nutrition (Edinburgh, Scotland). 2004;23:1226–43.CrossRef
95.
Reeves ND, Maganaris CN, Narici MV. Ultrasonographic assessment of human skeletal muscle size. Eur J Appl Physiol. 2004;91:116–8.PubMedCrossRef
96.
Fuller N, Hardingham C, Graves M, et al. Predicting composition of leg sections with anthropometry and bioelectrical impedance analysis, using magnetic resonance imaging as reference. Clinical Science. 1999;96(6):647–57.PubMedCrossRef
97.
Rolland Y, Lauwers-Cances VR, Cournot M, et al. Sarcopenia, calf circumference, and physical function of elderly women: a cross-sectional study. J Am Geriatr Soc. 2003;51:1120–4.PubMedCrossRef
98.
Heymsfield S, McManus C, Smith J. Anthropometric measurement of muscle mass: revised equations for calculating bone-free arm muscle area. Am J Clin Nutr. 1982;36(4):680–90.PubMed
99.
Calles-Escandon J, Cunningham JJ, Snyder P, et al. Influence of exercise on urea, creatinine, and 3-methylhistidine excretion in normal human subjects. Am J Physiol. 1984;246:E334–8.PubMed
100.
Rennie MJ, Phillips S, Smith K. Reliability of results and interpretation of measures of 3-methylhistidine in muscle interstitium as marker of muscle proteolysis. J Appl Physiol. 2008;105:1380–1. authorreply1382–3.PubMedCrossRef
101.
Millward DJ, Bates PC, Grimble GK, et al. Quantitative importance of non-skeletal-muscle sources of N tau-methylhistidine in urine. Biochem J. 1980;190:225–8.PubMed
102.
Tesch PA, von Walden F, Gustafsson T, et al. Skeletal muscle proteolysis in response to short-term unloading in humans. J Appl Physiol. 2008;105:902–6.PubMedCrossRef
103.
Smith IJ, Dodd SL. Calpain activation causes a proteasome-dependent increase in protein degradation and inhibits the Akt signalling pathway in rat diaphragm muscle. Exp Physiol. 2007;92:561–73.PubMedCrossRef
104.
Enns DL, Raastad T, Ugelstad I, et al. Calpain/calpastatin activities and substrate depletion patterns during hindlimb unweighting and reweighting in skeletal muscle. Eur J Appl Physiol. 2007;100:445–55.PubMedCrossRef
105.
106.
Smith IJ, Lecker SH, Hasselgren P-O. Calpain activity and muscle wasting in sepsis. Am J Physiol Endocrinol Metab. 2008;295:E762–71.PubMedCrossRef
107.
Murphy RM, Goodman CA, McKenna MJ, et al. Calpain-3 is autolyzed and hence activated in human skeletal muscle 24 h following a single bout of eccentric exercise. J Appl Physiol. 2007;103:926–31.PubMedCrossRef
108.
Guyon JR, Kudryashova E, Potts A, et al. Calpain 3 cleaves filamin C and regulates its ability to interact with gamma- and delta-sarcoglycans. Muscle Nerve. 2003;28:472–83.PubMedCrossRef
109.
Du J, Wang X, Miereles C, et al. Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions. J ClinInvest. 2004;113:115–23.
110.
Byun Y, Chen F, Chang R, et al. Caspase cleavage of vimentin disrupts intermediate filaments and promotes apoptosis. Cell Death Differ. 2001;8:443–50.PubMedCrossRef
111.
Chen F, Chang R, Trivedi M, et al. Caspase proteolysis of desmin produces a dominant-negative inhibitor of intermediate filaments and promotes apoptosis. J Biol Chem. 2003;278:6848–53.PubMedCrossRef
112.
Pereira AMM, Strasberg-Rieber M, Rieber M. Invasion-associated MMP-2 and MMP-9 are up-regulated intracellularly in concert with apoptosis linked to melanoma cell detachment. Clin Exp Metastasis. 2005;22:285–95.PubMedCrossRef
113.
Mort JS, Recklies AD, Poole AR. Extracellular presence of the lysosomal proteinase cathepsin B in rheumatoid synovium and its activity at neutral pH. Arthritis Rheum. 1984;27:509–15.PubMedCrossRef
114.
Premzl A, Zavasnik-Bergant V, Turk V, et al. Intracellular and extracellular cathepsin B facilitate invasion of MCF-10A neoT cells through reconstituted extracellular matrix in vitro. Exp Cell Res. 2003;283:206–14.PubMedCrossRef
115.
Poole AR, Hembry RM, Dingle JT. Cathepsin D in cartilage: the immunohistochemical demonstration of extracellular enzyme in normal and pathological conditions. J Cell Sci. 1974;14:139–61.PubMed
116.
Poole AR, Hembry RM, Dingle JT, et al. Proceedings: extracellular release of cathepsin D from cells in human normal and rheumatoid. Ann Rheum Dis. 1974;33:405–6.PubMedCrossRef
117.
Johnson P, Lobley GE, Perry SV. Distribution and biological role of 3-methyl-histidine in actin and myosin. Biochem J. 1969;114:34P.PubMed
118.
Fedorova M, Kuleva N, Hoffmann R. Identification, quantification, and functional aspects of skeletal muscle protein-carbonylation in vivo during acute oxidative stress. J Proteome Res. 2010;9:2516–26.PubMedCrossRef
Metadata
Title
Serological muscle loss biomarkers: an overview of current concepts and future possibilities
Authors
Anders Nedergaard
Morten A. Karsdal
Shu Sun
Kim Henriksen
Publication date
01-03-2013
Publisher
Springer-Verlag
Published in
Journal of Cachexia, Sarcopenia and Muscle / Issue 1/2013
Print ISSN: 2190-5991
Electronic ISSN: 2190-6009
DOI
https://doi.org/10.1007/s13539-012-0086-2

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10-04-2024 Myocardial Infarction News

» View more highlights on the ACC 2024 congress hub page

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