Different pattern of HSP47 expression in skeletal muscle of patients with neuromuscular diseases

Higuchi, Itsuro; Hashiguchi, Akihiro; Matsuura, Eiji; Higashi, Keiko; Shiraishi, Tadafumi; Hirata, Noriko; Arimura, Kimiyoshi; Osame, Mitsuhiro

doi:10.1016/j.nmd.2006.11.008

Cited by 10 publications

(8 citation statements)

References 30 publications

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“…The overexpressed Hsp47 has been observed in the muscle membrane only in the case of active inflammatory myopathy. In particular, Hsp47 is strongly expressed in the membrane of regenerating fibres, implying that it may be involved in the repair or regeneration of muscle fibres in addition to the fibrotic change in the connective tissue [316].…”

Section: A Subpopulation Of Hsps Can Interact With and Translocate Thmentioning

confidence: 99%

Membranes: a meeting point for lipids, proteins and therapies

Escribá¹,

González-Ros²,

Goñi³

et al. 2008

J Cellular Molecular Medi

356

287

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Membranes constitute a meeting point for lipids and proteins. Not only do they define the entity of cells and cytosolic organelles but they also display a wide variety of important functions previously ascribed to the activity of proteins alone. Indeed, lipids have commonly been considered a mere support for the transient or permanent association of membrane proteins, while acting as a selective cell/organelle barrier. However, mounting evidence demonstrates that lipids themselves regulate the location and activity of many membrane proteins, as well as defining membrane microdomains that serve as spatio-temporal platforms for interacting signalling proteins. Membrane lipids are crucial in the fission and fusion of lipid bilayers and they also act as sensors to control environmental or physiological conditions. Lipids and lipid structures participate directly as messengers or regulators of signal transduction. Moreover, their alteration has been associated with the development of numerous diseases. Proteins can interact with membranes through lipid co-/post-translational modifications, and electrostatic and hydrophobic interactions, van der Waals forces and hydrogen bonding are all involved in the associations among membrane proteins and lipids. The present study reviews these interactions from the molecular and biomedical point of view, and the effects of their modulation on the physiological activity of cells, the aetiology of human diseases and the design of clinical drugs. In fact, the influence of lipids on protein function is reflected in the possibility to use these molecular species as targets for therapies against cancer, obesity, neurodegenerative disorders, cardiovascular pathologies and other diseases, using a new approach called membrane-lipid therapy.

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Section: A Subpopulation Of Hsps Can Interact With and Translocate Thmentioning

confidence: 99%

Membranes: a meeting point for lipids, proteins and therapies

Escribá¹,

González-Ros²,

Goñi³

et al. 2008

J Cellular Molecular Medi

356

287

View full text Add to dashboard Cite

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“…Up‐regulation of HSP47, which is known as a collagen‐specific HSP, suggests that potential fibrosis during skeletal muscle regeneration (Higuchi et al. ). However, it is still not known whether heat shock transcription factor 1 (HSF1)‐deficiency influences the expression level of HSP47 during skeletal muscle regeneration.…”

Section: Introductionmentioning

confidence: 99%

“…It has been reported that muscle necrosis accompanies the up-regulations of HSPs, such as HSP70 and HSP90 (Bornman et al 1998;Santoro 2000) in mdx mice, which are the murine model for Duchenne muscular dystrophy. Up-regulation of HSP47, which is known as a collagen-specific HSP, suggests that potential fibrosis during skeletal muscle regeneration (Higuchi et al 2007). However, it is still not known whether heat shock transcription factor 1 (HSF1)-deficiency influences the expression level of HSP47 during skeletal muscle regeneration.…”

Section: Introductionmentioning

confidence: 99%

Regeneration of injured skeletal muscle in heat shock transcription factor 1-null mice

et al. 2013

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The purpose of this study was to investigate a role of heat shock transcription factor 1 (HSF1)-mediated stress response during regeneration of injured soleus muscle by using HSF1-null mice. Cardiotoxin (CTX) was injected into the left muscle of male HSF1-null and wild-type mice under anesthesia with intraperitoneal injection of pentobarbital sodium. Injection of physiological saline was also performed into the right muscle. Soleus muscles were dissected bilaterally 2 and 4 weeks after the injection. The relative weight and fiber cross-sectional area in CTX-injected muscles of HSF1-null, not of wild-type, mice were less than controls with injection of physiological saline 4 weeks after the injury, indicating a slower regeneration. Injury-related increase of Pax7-positive muscle satellite cells in HSF1-null mice was inhibited versus wild-type mice. HSF1-deficiency generally caused decreases in the basal expression levels of heat shock proteins (HSPs). But the mRNA expression levels of HSP25 and HSP90α in HSF1-null mice were enhanced in response to CTX-injection, compared with wild-type mice. Significant up-regulations of proinflammatory cytokines, such as interleukin (IL) -6, IL-1β, and tumor necrosis factor mRNAs, with greater magnitude than in wild-type mice were observed in HSF1-deficient mouse muscle. HSF1 and/or HSF1-mediated stress response may play a key role in the regenerating process of injured skeletal muscle. HSF1 deficiency may depress the regenerating process of injured skeletal muscle via the partial depression of increase in Pax7-positive satellite cells. HSF1-deficiency-associated partial depression of skeletal muscle regeneration might also be attributed to up-regulation of proinflammatory cytokines.

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“…Prior to its recognition as a resident ER chaperone protein that specifically controls collagen helix formation, HSP47 (also called colligin-2) was characterized as a cell surface protein that binds extracellular collagen (34). HSP47 was enriched in sarcolemma of muscle biopsies from Duchenne, Becker, and dysferlin-deficient muscular dystrophy patients compared with healthy controls and may function in repair or regeneration of muscle fibers (35). In Fig.…”

Section: Discussionmentioning

confidence: 92%

A Plasma Membrane Wound Proteome

Mellgren

2010

Journal of Biological Chemistry

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Cells in mechanically active tissues undergo constant plasma membrane damage that must be repaired to allow survival. To identify wound-associated proteins, a cell-impermeant, thiolreactive biotinylation reagent was used to label and subsequently isolate intracellular proteins that become exposed on the surface of cultured cells after plasma membrane damage induced by scraping from substratum or crushing with glass beads. Scrape-damaged cells survived injury and were capable of forming viable colonies. Proteins that were exposed to the cell surface were degraded or internalized a few seconds to several minutes after damage, except for vimentin, which was detectable on the cell surface for at least an hour after injury. Seven major biotinylated protein bands were identified on SDS-PAGE gels. Mass spectrometric studies identified cytoskeletal proteins (caldesmon-1 and vimentin), endoplasmic reticulum proteins (ERp57, ERp5, and HSP47), and nuclear proteins (lamin C, heterogeneous nuclear ribonucleoprotein F, and nucleophosmin-1) as major proteins exposed after injury. Although caldesmon was a major wound-associated protein in calpain small subunit knock-out fibroblasts, it was rapidly degraded in wildtype cells, probably by calpains. Lamin C exposure after wounding was most likely the consequence of nuclear envelope damage. These studies document major intracellular proteins associated with the cell surface of reversibly damaged somatic cells. The studies also show that externalization of some proteins reported to have physiologic or pathologic roles on the cell surface can occur in cells undergoing plasma membrane damage and subsequent repair.Cells in tissues of multicellular organisms are often subjected to mechanical stresses that result in PM 2 damage (1-4). It is therefore not surprising that mechanisms have evolved to rapidly repair breaches in the PM that would otherwise rapidly lead to cell death. The currently accepted model posits calcium-dependent homotypic fusion of intracellular vesicles to provide a large membrane "patch" that rapidly (within seconds) seals the opening in the PM, maintaining cell viability. The nature of the intracellular membrane component(s) required for repair is a matter of speculation (5, 6). Few other details of the PM repair process are known, although some proteins, including membrane fusion proteins (5), myosin motor proteins (5), dysferlin (7), annexin A1 (8), calpains (9), and MG53 (10), have been shown to participate in repair in various model systems. To my knowledge, a systematic search for a "plasma membrane repairome," i.e. proteins required for repair of mechanically damaged membrane, has only been carried out in marine oocytes. Several high molecular weight yolk granule proteins were found to comprise a complex that facilitated vesicle patch formation (11).The entire chronologic sequence of repair and subsequent remodeling of the wound site is another area that requires further exploration, because an expeditious, full resolution of PM damage must be essential in tis...

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Different pattern of HSP47 expression in skeletal muscle of patients with neuromuscular diseases

Cited by 10 publications

References 30 publications

Membranes: a meeting point for lipids, proteins and therapies

Membranes: a meeting point for lipids, proteins and therapies

Regeneration of injured skeletal muscle in heat shock transcription factor 1-null mice

A Plasma Membrane Wound Proteome

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