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

Koskinen, Satu; Kjær, Michael; Mohr, Thomas; Sørensen, Fin Biering; Suuronen, Tiina; Takala, Timo

doi:10.1002/(sici)1097-4598(200004)23:4<580::aid-mus18>3.0.co;2-4

Cited by 47 publications

(36 citation statements)

References 47 publications

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“…Accordingly, Koskinen et al 38 reported that NMES can elevate the gelatinolytic activity of proYMMP-2, suggesting an increase in type IV collagen turnover in individuals with spinal cord injury, which indicates an adaptive remodeling process of intramuscular collagen in response to electrical training of skeletal muscle. Accordingly, Koskinen et al 38 reported that NMES can elevate the gelatinolytic activity of proYMMP-2, suggesting an increase in type IV collagen turnover in individuals with spinal cord injury, which indicates an adaptive remodeling process of intramuscular collagen in response to electrical training of skeletal muscle.…”

Section: Discussionmentioning

confidence: 99%

Neuromuscular Electrical Stimulation Induces Beneficial Adaptations in the Extracellular Matrix of Quadriceps Muscle After Anterior Cruciate Ligament Transection of Rats

Durigan

Peviani²,

Delfino³

et al. 2014

American Journal of Physical Medicine &Amp; Rehabilitation

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Section: Discussionmentioning

confidence: 99%

Neuromuscular Electrical Stimulation Induces Beneficial Adaptations in the Extracellular Matrix of Quadriceps Muscle After Anterior Cruciate Ligament Transection of Rats

Durigan

Peviani²,

Delfino³

et al. 2014

American Journal of Physical Medicine &Amp; Rehabilitation

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“…The mean number of TUNEL-positive nuclei per 40ϫ objective field was counted from four sections on different planes in each sample. Pro matrix metalloproteinase 2 (MMP-2) activity was measured by zymography as described (16), using 50 g of protein and 7.5% gels. ␤-Glucuronidase activity was measured in a cardiac muscle homogenate as mentioned earlier (15).…”

Section: Methodsmentioning

confidence: 99%

Lack of type XV collagen causes a skeletal myopathy and cardiovascular defects in mice

Eklund

Piuhola

Komulainen

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

168

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Type XV collagen occurs widely in the basement membrane zones of tissues, but its function is unknown. To understand the biological role of this protein, a null mutation in the Col15a1 gene was introduced into the germ line of mice. Despite the complete lack of type XV collagen, the mutant mice developed and reproduced normally, and they were indistinguishable from their wild-type littermates. However, Col15a1-deficient mice showed progressive histological changes characteristic for muscular diseases after 3 months of age, and they were more vulnerable than controls to exercise-induced muscle injury. Despite the antiangiogenic role of type XV collagen-derived endostatin, the development of the vasculature appeared normal in the null mice. Nevertheless, ultrastructural analyses revealed collapsed capillaries and endothelial cell degeneration in the heart and skeletal muscle. Furthermore, perfused hearts showed a diminished inotropic response, and exercise resulted in cardiac injury, changes that mimic early or mild heart disease. Thus, type XV collagen appears to function as a structural component needed to stabilize skeletal muscle cells and microvessels.T ype XV collagen belongs to the heterogeneous group of non-fibril-forming collagens and is thought to be a homotrimer consisting of three ␣1(XV) collagen chains (1). It is characterized by a central highly interrupted triple helical domain and large N-and C-terminal noncollagenous domains (2-4), and it has been shown to be a chondroitin sulfate proteoglycan (5). Type XV collagen mRNAs are expressed in many tissues, but the highest mRNA levels in the mouse can be detected in the heart and skeletal muscle (4). The protein is shown by immunostaining to have a widespread tissue distribution and has been localized mainly to the basement membrane zones, although it can also be found in the fibrillar collagen matrix of some tissues (6, 7). Its function is not known, however.In terms of primary structure, type XV collagen is highly homologous with type XVIII collagen, and together they form a distinct subgroup among the collagens (1, 3). They have thrombospondin-1 sequence homology in the N terminus, seven homologous collagenous domains, and highly homologous Cterminal noncollagenous domains. Type XVIII collagen is the precursor of endostatin, which has been shown to have a potent antiangiogenic effect (8), and the highest degree of homology between collagen types XV and XVIII involves the C-terminal endostatin sequence. The corresponding fragment in type XV collagen has also been shown to have antiangiogenic activity (9, 10).To understand the biological function and significance of type XV collagen, we generated a mouse strain lacking in ␣1(XV) collagen chains by site-specific Cre-loxP-mediated deletion in embryonic stem (ES) cells (11). The data suggest a structural role for type XV collagen in providing mechanical stability between cells and the extracellular matrix in skeletal muscle fibers and microvessels. Col15a1 deficiency leads to functional rather than struct...

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“…Although several MMPs exist in skeletal muscle, so far the expression of only MMP-2 (gelatinase A) and MMP-9 (gelatinase B) has been studied in detail in skeletal muscle in physiological and pathophysiological conditions (Allen et al, 1999; Choi and Dalakas, 2000; Kieseier et al, 2001; Koskinen et al, 2000; Koskinen et al, 2001). Increased expression of MMPs has also been implicated in the pathogenesis of inflammatory myopathies (Choi and Dalakas, 2000; Kieseier et al, 2001; Pearson and Young, 1993; Schoser et al, 2002).…”

Section: Matrix Metalloproteinasesmentioning

confidence: 99%

Wasting mechanisms in muscular dystrophy

Shin

Tajrishi

Ogura

et al. 2013

The International Journal of Biochemistry & Cell Biology

122

143

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Muscular dystrophy is a group of more than 30 different clinical genetic disorders that are characterized by progressive skeletal muscle wasting and degeneration. Primary deficiency of specific extracellular matrix, sarcoplasmic, cytoskeletal, or nuclear membrane protein results in several secondary changes such as sarcolemmal instability, calcium influx, fiber necrosis, oxidative stress, inflammatory response, breakdown of extracellular matrix, and eventually fibrosis which leads to loss of ambulance and cardiac and respiratory failure. A number of molecular processes have now been identified which hasten disease progression in human patients and animal models of muscular dystrophy. Accumulating evidence further suggests that aberrant activation of several signaling pathways aggravate pathological cascades in dystrophic muscle. Although replacement of defective gene with wild-type is paramount to cure, management of secondary pathological changes has enormous potential to improving the quality of life and extending lifespan of muscular dystrophy patients. In this article, we have reviewed major cellular and molecular mechanisms leading to muscle wasting in muscular dystrophy.

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

Cited by 47 publications

References 47 publications

Neuromuscular Electrical Stimulation Induces Beneficial Adaptations in the Extracellular Matrix of Quadriceps Muscle After Anterior Cruciate Ligament Transection of Rats

Neuromuscular Electrical Stimulation Induces Beneficial Adaptations in the Extracellular Matrix of Quadriceps Muscle After Anterior Cruciate Ligament Transection of Rats

Lack of type XV collagen causes a skeletal myopathy and cardiovascular defects in mice

Wasting mechanisms in muscular dystrophy

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