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Nemaline Myopathy: Evidence of Dipeptidyl Peptidase I Deficiency

Nemaline Myopathy: Evidence of Dipeptidyl Peptidase I Deficiency Abstract • Fluorescent protease histochemical analysis of muscle biopsy specimens from two patients with nemaline myopathy revealed the apparent absence of one proteolytic enzyme, dipeptidyl peptidase I. Although the function of peptidases in normal muscle is obscure, this abnormality suggests that proteases may participate in posttranslational modification of proteins that are to be assembled into Z lines or, alternatively, in the disassembly and degradation of Z-line material. References 1. Hers HG, van Hoof F (eds): Lysosomes and Storage Disease . New York, Academic Press Inc, 1973. 2. Alper CA, Colten HR, Gear JSS, et al: Homozygous human C3 deficiency . J Clin Invest 1976;57:222-229.Crossref 3. Lapiere CM, Lenaers A, Kohn LD: Procollagen peptidase: An enzyme excising the coordination peptides of procollagen . Proc Natl Acad Sci USA 1971;68:3054-3058.Crossref 4. Beynon RJ, Bond JS: Deficiency of a kidney metalloproteinase activity in inbred mouse strains . Science 1983;219:1351-1353.Crossref 5. Stauber WT, Riggs JE, Schochet SS: Fluorescent protease histochemistry in neuromuscular disease . Neurology 1984;34( (suppl 1) ):194. 6. Stauber WT, Ong SH: Fluorescence demonstration of cathepsin B in skeletal, cardiac, and vascular smooth muscle . J Histochem Cytochem 1981;29:866-869.Crossref 7. Stauber WT, Ong SH: Fluorescence demonstration of cathepsin H-like protease in cardiac, skeletal and vascular smooth muscles . Histochem J 1982;14:585-591.Crossref 8. Stauber WT, Ong SH: Fluorescence demonstration of dipeptidyl peptidase I (cathepsin C) in skeletal, cardiac, and vascular smooth muscles . J Histochem Cytochem 1981;30:162-164.Crossref 9. Stauber WT, Ong SH: Fluorescence demonstration of dipeptidyl peptidase II in skeletal, cardiac, and vascular smooth muscles . J Histochem Cytochem 1981;29:672-677.Crossref 10. Fardeau M: Ultrastructural lesions in progressive muscular dystrophies , in Walton JN, Canal N, Scarlato G (eds): Muscle Diseases . Amsterdam, Excerpta Medica, 1970, pp 98-108. 11. Stauber WT, Hedge AM, Trout JJ, et al: Inhibition of lysosomal function in red and white skeletal muscles by chloroquine . Exp Neurol 1981;71:295-306.Crossref 12. DeMartino GN, Goldberg AL: Thyroid hormones control lysosomal enzymes activities in liver and skeletal muscle . Proc Natl Acad Sci USA 1978;75:1369-1373.Crossref 13. Jennekens FGI, Roord JJ, Veldman H, et al: Congenital nemaline myopathy: I. Defective organization of αactinin is restricted to muscle . Muscle Nerve 1983;6:61-68.Crossref 14. Pontremoli S, Melloni E, Damiani G, et al: Binding of monoclonal antibody to cathepsin M located on the external surface of rabbit lysosomes . Arch Biochem Biophys 1984;233:267-271.Crossref http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Neurology American Medical Association

Nemaline Myopathy: Evidence of Dipeptidyl Peptidase I Deficiency

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Publisher
American Medical Association
Copyright
Copyright © 1986 American Medical Association. All Rights Reserved.
ISSN
0003-9942
eISSN
1538-3687
DOI
10.1001/archneur.1986.00520010035017
Publisher site
See Article on Publisher Site

Abstract

Abstract • Fluorescent protease histochemical analysis of muscle biopsy specimens from two patients with nemaline myopathy revealed the apparent absence of one proteolytic enzyme, dipeptidyl peptidase I. Although the function of peptidases in normal muscle is obscure, this abnormality suggests that proteases may participate in posttranslational modification of proteins that are to be assembled into Z lines or, alternatively, in the disassembly and degradation of Z-line material. References 1. Hers HG, van Hoof F (eds): Lysosomes and Storage Disease . New York, Academic Press Inc, 1973. 2. Alper CA, Colten HR, Gear JSS, et al: Homozygous human C3 deficiency . J Clin Invest 1976;57:222-229.Crossref 3. Lapiere CM, Lenaers A, Kohn LD: Procollagen peptidase: An enzyme excising the coordination peptides of procollagen . Proc Natl Acad Sci USA 1971;68:3054-3058.Crossref 4. Beynon RJ, Bond JS: Deficiency of a kidney metalloproteinase activity in inbred mouse strains . Science 1983;219:1351-1353.Crossref 5. Stauber WT, Riggs JE, Schochet SS: Fluorescent protease histochemistry in neuromuscular disease . Neurology 1984;34( (suppl 1) ):194. 6. Stauber WT, Ong SH: Fluorescence demonstration of cathepsin B in skeletal, cardiac, and vascular smooth muscle . J Histochem Cytochem 1981;29:866-869.Crossref 7. Stauber WT, Ong SH: Fluorescence demonstration of cathepsin H-like protease in cardiac, skeletal and vascular smooth muscles . Histochem J 1982;14:585-591.Crossref 8. Stauber WT, Ong SH: Fluorescence demonstration of dipeptidyl peptidase I (cathepsin C) in skeletal, cardiac, and vascular smooth muscles . J Histochem Cytochem 1981;30:162-164.Crossref 9. Stauber WT, Ong SH: Fluorescence demonstration of dipeptidyl peptidase II in skeletal, cardiac, and vascular smooth muscles . J Histochem Cytochem 1981;29:672-677.Crossref 10. Fardeau M: Ultrastructural lesions in progressive muscular dystrophies , in Walton JN, Canal N, Scarlato G (eds): Muscle Diseases . Amsterdam, Excerpta Medica, 1970, pp 98-108. 11. Stauber WT, Hedge AM, Trout JJ, et al: Inhibition of lysosomal function in red and white skeletal muscles by chloroquine . Exp Neurol 1981;71:295-306.Crossref 12. DeMartino GN, Goldberg AL: Thyroid hormones control lysosomal enzymes activities in liver and skeletal muscle . Proc Natl Acad Sci USA 1978;75:1369-1373.Crossref 13. Jennekens FGI, Roord JJ, Veldman H, et al: Congenital nemaline myopathy: I. Defective organization of αactinin is restricted to muscle . Muscle Nerve 1983;6:61-68.Crossref 14. Pontremoli S, Melloni E, Damiani G, et al: Binding of monoclonal antibody to cathepsin M located on the external surface of rabbit lysosomes . Arch Biochem Biophys 1984;233:267-271.Crossref

Journal

Archives of NeurologyAmerican Medical Association

Published: Jan 1, 1986

References