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Published in: Acta Neuropathologica 4/2010

01-04-2010 | Methods Paper

Novel myosin heavy chain immunohistochemical double staining developed for the routine diagnostic separation of I, IIA and IIX fibers

Authors: Olayinka Raheem, Sanna Huovinen, Tiina Suominen, Hannu Haapasalo, Bjarne Udd

Published in: Acta Neuropathologica | Issue 4/2010

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Abstract

The different histochemical ATPase properties of myosins separating the muscle fiber types have been utilized in diagnostic muscle biopsy routine for more than four decades. The ATPase staining method is rather laborious and has several disadvantages, such as weakening of staining over time and non-specific staining of capillaries, making the distinction of extremely atrophic muscle fibers difficult. We have developed a reliable and advanced immunohistochemical myosin double staining method for the identification of fiber types, including highly atrophic fibers in routine diagnostics. With this double staining method, we are able to distinguish among type I (ATPase type 1), IIA (ATPase type 2A), IIX (ATPase type 2B) and remodeled ATPase type 2C fibers expressing both fast and slow myosins using a one slide technique. Immunohistochemical double staining of myosin heavy chain isoforms can be used as an alternative for the conventional ATPase staining method in routine histopathology. The method provides even more detailed information of fast fiber subtypes and highly atrophic fibers on one single slide.
Literature
1.
go back to reference Bancroft JD, Cook HC (1994) Manual of histological techniques and their diagnostic application. Churchill Livingstone, Edinburgh Bancroft JD, Cook HC (1994) Manual of histological techniques and their diagnostic application. Churchill Livingstone, Edinburgh
2.
go back to reference Dye DE, Azzarelli B, Goebel HH, Laing NG (2006) Novel slow-skeletal myosin (MYH7) mutation on the original myosin storage myopathy kindred. Neuromuscul Disord 16:357–360CrossRefPubMed Dye DE, Azzarelli B, Goebel HH, Laing NG (2006) Novel slow-skeletal myosin (MYH7) mutation on the original myosin storage myopathy kindred. Neuromuscul Disord 16:357–360CrossRefPubMed
3.
go back to reference Harper PS (2001) Myotonic dystrophy. WB Sauders, London Harper PS (2001) Myotonic dystrophy. WB Sauders, London
4.
go back to reference Izumo S, Nadal-Ginard B, Mahadavi V (1986) All members of the MHC multigene family respond to thyroid hormone in a highly tissue-specific manner. Science 231:597–600CrossRefPubMed Izumo S, Nadal-Ginard B, Mahadavi V (1986) All members of the MHC multigene family respond to thyroid hormone in a highly tissue-specific manner. Science 231:597–600CrossRefPubMed
5.
go back to reference Laing NG, Laing BA, Meredith C et al (1995) Autosomal dominant distal myopathy: linkage to chromosome 14. Am J Hum Genet 56:422–427PubMed Laing NG, Laing BA, Meredith C et al (1995) Autosomal dominant distal myopathy: linkage to chromosome 14. Am J Hum Genet 56:422–427PubMed
6.
go back to reference Liquori C, Ricker K, Moseley ML et al (2001) Myotonic dystrophy type 2 caused by a CCTG expansion in intron 1 of ZNF9. Science 293:864–867CrossRefPubMed Liquori C, Ricker K, Moseley ML et al (2001) Myotonic dystrophy type 2 caused by a CCTG expansion in intron 1 of ZNF9. Science 293:864–867CrossRefPubMed
7.
go back to reference Mahadevi V, Strehler EE, Periasamy M, Wieczorek DF, Izumo S, Nadal-Ginard B (1986) Sarcomeric myosin heavy chain gene family: organization and pattern of expression. Med Sci Sports Exerc 18:299–308CrossRef Mahadevi V, Strehler EE, Periasamy M, Wieczorek DF, Izumo S, Nadal-Ginard B (1986) Sarcomeric myosin heavy chain gene family: organization and pattern of expression. Med Sci Sports Exerc 18:299–308CrossRef
8.
go back to reference Martinsson T, Oldfors A, Darin N et al (2000) Autosomal dominant myopathy: missense mutation (Glu-706 → Lys) in the myosin heavy chain IIa gene. Proc Natl Acad Sci USA 97:14614–14619CrossRefPubMed Martinsson T, Oldfors A, Darin N et al (2000) Autosomal dominant myopathy: missense mutation (Glu-706 → Lys) in the myosin heavy chain IIa gene. Proc Natl Acad Sci USA 97:14614–14619CrossRefPubMed
9.
go back to reference Meredith C, Hermann R, Parry C et al (2004) Mutations in the slow muscle fiber myosin heavy chain gene (MYH7) cause Laing early-onset distal myopathy (MPD1). Am J Hum Genet 75:703–708CrossRefPubMed Meredith C, Hermann R, Parry C et al (2004) Mutations in the slow muscle fiber myosin heavy chain gene (MYH7) cause Laing early-onset distal myopathy (MPD1). Am J Hum Genet 75:703–708CrossRefPubMed
10.
go back to reference Oldfors A, Darin N, Martinsson T (2002) Autosomal dominant myosin heavy chain IIa myopathy. In: karpati G (ed) Structural and molecular basis of skeletal muscle diseases. ISN Neuropath Press, Basel, pp 85–87 Oldfors A, Darin N, Martinsson T (2002) Autosomal dominant myosin heavy chain IIa myopathy. In: karpati G (ed) Structural and molecular basis of skeletal muscle diseases. ISN Neuropath Press, Basel, pp 85–87
11.
go back to reference Oldfors A, Tajsharghi H, Thornell LE (2005) Mutation of the slow myosin heavy chain rod domain underlies hyaline body myopathy. Neurology 64:580–581PubMed Oldfors A, Tajsharghi H, Thornell LE (2005) Mutation of the slow myosin heavy chain rod domain underlies hyaline body myopathy. Neurology 64:580–581PubMed
12.
go back to reference Pette D, Vrbová G (1992) Adaptation of mammalian skeletal muscle fibers to chronic electrical stimulation. Rev Physiol Biochem Pharmacol 120:115–202CrossRefPubMed Pette D, Vrbová G (1992) Adaptation of mammalian skeletal muscle fibers to chronic electrical stimulation. Rev Physiol Biochem Pharmacol 120:115–202CrossRefPubMed
13.
go back to reference Rayment I, Holden HM, Whittaker M et al (1993) Structure of the actin complex and its implications for muscle contraction. Science 261:58–65CrossRefPubMed Rayment I, Holden HM, Whittaker M et al (1993) Structure of the actin complex and its implications for muscle contraction. Science 261:58–65CrossRefPubMed
14.
go back to reference Ruppel KM, Spundich JA (1996) Structure–function analysis of the motor domain of myosin. Annu Rev Cell Dev Biol 12:543–573CrossRefPubMed Ruppel KM, Spundich JA (1996) Structure–function analysis of the motor domain of myosin. Annu Rev Cell Dev Biol 12:543–573CrossRefPubMed
15.
go back to reference Tajsharghi H, Oldfors A, Macleod DP, Swash M (1997) Homozygous mutation in MYH7 in myosin storage myopathy and cardiomyopathy. Neurology 68:962CrossRef Tajsharghi H, Oldfors A, Macleod DP, Swash M (1997) Homozygous mutation in MYH7 in myosin storage myopathy and cardiomyopathy. Neurology 68:962CrossRef
16.
go back to reference Tajsharghi H, Thornell LE, Lindberg C, Lindvall B, Hendriksson KG, Oldfors A (2003) Myosin storage myopathy associated with a heterozygous missense mutation in MYH7. Ann Neurol 54:494–500CrossRefPubMed Tajsharghi H, Thornell LE, Lindberg C, Lindvall B, Hendriksson KG, Oldfors A (2003) Myosin storage myopathy associated with a heterozygous missense mutation in MYH7. Ann Neurol 54:494–500CrossRefPubMed
17.
go back to reference Udd B, Meola G, Krahe R et al (2006) 140th ENMC international workshop: myotonic dystrophy DM2/PROMM and other myotonic dystrophies with guidelines on management. Neuromuscul Disord 16:403–413CrossRefPubMed Udd B, Meola G, Krahe R et al (2006) 140th ENMC international workshop: myotonic dystrophy DM2/PROMM and other myotonic dystrophies with guidelines on management. Neuromuscul Disord 16:403–413CrossRefPubMed
18.
go back to reference Udd B, Meola G, Krahe R et al (2003) Report of the 115th ENMC workshop: DM2/PROMM and other myotonic dystrophies. 3rd Workshop, 14–16 February 2003, Naarden, The Netherlands. Neuromuscul Disord 13:589–596CrossRefPubMed Udd B, Meola G, Krahe R et al (2003) Report of the 115th ENMC workshop: DM2/PROMM and other myotonic dystrophies. 3rd Workshop, 14–16 February 2003, Naarden, The Netherlands. Neuromuscul Disord 13:589–596CrossRefPubMed
19.
go back to reference Udd B, Krahe R, Wallgren-Petterson C, Falkc B, Kalimo H (1997) Proximal myotonic dystrophy—a family with autosomal dominant muscular dystrophy, cataracts, hearing loss and hypogonadism: heterogeneity of proximal myotonic syndromes? Neuromuscl Disord 7:217–218CrossRef Udd B, Krahe R, Wallgren-Petterson C, Falkc B, Kalimo H (1997) Proximal myotonic dystrophy—a family with autosomal dominant muscular dystrophy, cataracts, hearing loss and hypogonadism: heterogeneity of proximal myotonic syndromes? Neuromuscl Disord 7:217–218CrossRef
20.
go back to reference Vihola A, Bassez G, Meola G et al (2003) Histopathological differences of myotonic dystrophy type 1 (DM1) and PROMM/DM2. Neurology 60:1854–1857PubMed Vihola A, Bassez G, Meola G et al (2003) Histopathological differences of myotonic dystrophy type 1 (DM1) and PROMM/DM2. Neurology 60:1854–1857PubMed
21.
go back to reference Weiss A, McDonough D, Wertman B et al (1999) Organization of human and mouse skeletal myosin heavy chain gene clusters is highly conserved. Proc Natl Acad Sci USA 96:2958–2963CrossRefPubMed Weiss A, McDonough D, Wertman B et al (1999) Organization of human and mouse skeletal myosin heavy chain gene clusters is highly conserved. Proc Natl Acad Sci USA 96:2958–2963CrossRefPubMed
Metadata
Title
Novel myosin heavy chain immunohistochemical double staining developed for the routine diagnostic separation of I, IIA and IIX fibers
Authors
Olayinka Raheem
Sanna Huovinen
Tiina Suominen
Hannu Haapasalo
Bjarne Udd
Publication date
01-04-2010
Publisher
Springer-Verlag
Published in
Acta Neuropathologica / Issue 4/2010
Print ISSN: 0001-6322
Electronic ISSN: 1432-0533
DOI
https://doi.org/10.1007/s00401-010-0643-8

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