Lysosomal and Nonlysosomal Hydrolases of Skeletal Muscle in Neuromuscular Diseases

Takala, Timo; Myllylä, Vilho V.; Salminen, Antero; Tolonen, U.; Hassinen, Ilmo E.; Vihko, V.

doi:10.1001/archneur.1983.04050080041006

Cited by 17 publications

(6 citation statements)

References 24 publications

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“…Ten individuals (men/women: 8/2) with spinal cord injury [level: C6 to T6; years since injury: 12.5 (2-23) years (mean and range); age: 35 (27)(28)(29)(30)(31)(32)(33)(34)(35)(36)(37)(38)(39)(40)(41)(42)(43)(44)(45) years; mean weight: 78 ± 3.8 (SE) kg] participated in the present study, which was approved by the Municipal Ethical Committee of Copenhagen. Six were tetraplegic and four were paraplegic.…”

Section: Methodsmentioning

confidence: 99%

“…In neurogenic and myogenic muscle diseases, muscular collagen biosynthesis rate and collagen content have been observed to increase 26 simultaneously with activation of lysosomal and nonlysosomal pathways for muscle protein degradation. 42 Futhermore, denervation atrophy of rat skeletal muscle is associated with an increased rate of muscular collagen biosynthesis, 35 whereas during reinnervation collagen synthesis rate may decrease despite accelerated total muscular protein synthesis. 46 Type I and III collagens, which are the major collagen types in skeletal muscle, are found in epimysium, perimysium, and endomysium, 5 whereas type IV, 5 V, 34 and XV 9 collagens are associated with the basement membrane.…”

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confidence: 99%

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Type IV collagen and its degradation in paralyzed human muscle: Effect of functional electrical stimulation

et al. 2000

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Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

Type IV collagen and its degradation in paralyzed human muscle: Effect of functional electrical stimulation

et al. 2000

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“…In diseases with spinal muscular atrophies, including ALS as a neurogenic muscle disease, they have elevated activities of lysosomal proteases and enzymes that accelerate the biosynthesis of muscle collagen [ 20 , 58 ]. Changes in population numbers of inflammatory fibroblasts and phagocytes occur together with increases in enzyme activities, which are accompanied by a proportionally similar increase in muscle collagen content in ALS [ 20 , 59 ]. The collagenase activities of the DPP1 and DPP4 enzymes present a positive correlation with several of the enzymatic activities related to collagen biosynthesis [ 20 ].…”

Section: Resultsmentioning

confidence: 99%

“…Being part of the dipeptidyl dipeptidases family, the activities of dipeptidyl peptidase I, also known as Cathepsin C (DPP1 or CTSC, EC 3.4.14.1), and DPP4 are associated with neuromuscular diseases [ 20 ].…”

Section: Introductionmentioning

confidence: 99%

Systematic Review and Meta-Analyses of Aminopeptidases as Prognostic Biomarkers in Amyotrophic Lateral Sclerosis

Teruel-Peña

Gómez‐Urquiza

Suleiman‐Martos

et al. 2023

IJMS

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Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease characterized by the progressive loss of motor neurons in the spinal cord, brain stem, and cerebral cortex. Biomarkers for ALS are essential for disease detection and to provide information on potential therapeutic targets. Aminopeptidases catalyze the cleavage of amino acids from the amino terminus of protein or substrates such as neuropeptides. Since certain aminopeptidases are known to increase the risk of neurodegeneration, such mechanisms may reveal new targets to determine their association with ALS risk and their interest as a diagnostic biomarker. The authors performed a systematic review and meta-analyses of genome-wide association studies (GWASs) to identify reported aminopeptidases genetic loci associated with the risk of ALS. PubMed, Scopus, CINAHL, ISI Web of Science, ProQuest, LILACS, and Cochrane databases were searched to retrieve eligible studies in English or Spanish, published up to 27 January 2023. A total of 16 studies were included in this systematic review, where a series of aminopeptidases could be related to ALS and could be promising biomarkers (DPP1, DPP2, DPP4, LeuAP, pGluAP, and PSA/NPEPPS). The literature reported the association of single-nucleotide polymorphisms (SNPs: rs10260404 and rs17174381) with the risk of ALS. The genetic variation rs10260404 in the DPP6 gene was identified to be highly associated with ALS susceptibility, but meta-analyses of genotypes in five studies in a matched cohort of different ancestry (1873 cases and 1861 control subjects) showed no ALS risk association. Meta-analyses of eight studies for minor allele frequency (MAF) also found no ALS association for the “C” allele. The systematic review identified aminopeptidases as possible biomarkers. However, the meta-analyses for rs1060404 of DPP6 do not show a risk associated with ALS.

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“…Muscle atrophy and intramuscular accumulation of connective tissue are the characteristic findings in many neuromuscular diseases. These processes may be linked to increased muscle degradation, 19 apoptosis, 17 and acceleration of collagen biosynthesis. 7,12 Fibrosis impairs muscle function and has a role in the clinical manifestations of neuromuscular diseases.…”

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confidence: 99%

Collagen synthesis and degradation in polyneuropathy and myopathies

et al. 2004

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To determine the mechanisms underlying the changes in collagen metabolism responsible for muscle fibrosis in patients with neuromuscular diseases, the synthesis and degradation of collagens was studied in muscles of patients with polyneuropathy and noninflammatory myopathies. The mRNA levels for type I, III, and IV collagens and immunohistochemical staining intensities for collagen propeptides and telopeptides were increased in polyneuropathy, suggesting enhanced synthesis of collagens. In myopathy, the mRNA levels were at the control level. Matrix metalloproteinase (MMP)-2 mRNA level was increased in polyneuropathy, although the quantity of proMMP-2 was not changed. An increase in type IV collagen concentration and proMMP-9 expression was observed in polyneuropathy but not in myopathies. Our results suggest that intramuscular accumulation of type IV collagen occurs in polyneuropathy, possibly leading to thickening of the capillary and muscle fiber basement membranes. This may complicate the transportation of nutrients and cellular excreta between blood and muscle cells.

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Lysosomal and Nonlysosomal Hydrolases of Skeletal Muscle in Neuromuscular Diseases

Cited by 17 publications

References 24 publications

Type IV collagen and its degradation in paralyzed human muscle: Effect of functional electrical stimulation

Type IV collagen and its degradation in paralyzed human muscle: Effect of functional electrical stimulation

Systematic Review and Meta-Analyses of Aminopeptidases as Prognostic Biomarkers in Amyotrophic Lateral Sclerosis

Collagen synthesis and degradation in polyneuropathy and myopathies

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