ArticleThe Biochemical journal1998
Rabbit cardiac and skeletal myocytes differ in constitutive and inducible expression of the glucose-regulated protein GRP94.
Article in The Biochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 22 citations in OpenAlex.
- Overexpressing microRNA-150 attenuates hypoxia-induced human cardiomyocyte cell apoptosis by targeting glucose-regulated protein-94.Molecular medicine reports · 2018Article
- Role of the unfolded protein response, GRP78 and GRP94 in organ homeostasis.Journal of cellular physiology · 2015Review
- Curcumin counteracts loss of force and atrophy of hindlimb unloaded rat soleus by hampering neuronal nitric oxide synthase untethering from sarcolemma.The Journal of physiology · 2014Article
- The stress protein/chaperone Grp94 counteracts muscle disuse atrophy by stabilizing subsarcolemmal neuronal nitric oxide synthase.Antioxidants & redox signaling · 2014Article
- Article
- Deletion of muscle GRP94 impairs both muscle and body growth by inhibiting local IGF production.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2012Article
- Genetics of sick sinus syndrome.Cardiac electrophysiology clinics · 2010Article
- Glucose regulated protein 94 is required for muscle differentiation through its control of the autocrine production of insulin-like growth factors.Biochimica et biophysica acta · 2010Article
- Myofiber stress-response in myositis: parallel investigations on patients and experimental animal models of muscle regeneration and systemic inflammation.Arthritis research & therapy · 2010Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The glucose-regulated protein GRP94 is a stress-inducible glycoprotein that is known to be constitutively and ubiquitously expressed in the endoplasmic reticulum of mammalian cells. From a rabbit heart cDNA library we isolated four overlapping clones coding for the rabbit homologue of GRP94 mRNA. Northern blot analysis shows that a 3200 nt mRNA species corresponding to GRP94 mRNA is detectable in several tissues and it is 5-fold more abundant in the heart than in the skeletal muscle. Hybridization analysis in situ shows that GRP94 mRNA accumulates in cardiac myocytes, whereas in skeletal muscles it is not detectable in myofibres. A monoclonal antibody raised by using a 35 kDa recombinant GRP94 polypeptide as immunogen detects a single reactive polypeptide of 94 kDa in a Western blot of liver and heart homogenates and does not react with skeletal muscle homogenates. Conversely, GRP94 mRNA and protein are detectable in both cardiac and skeletal muscle myocytes of fetal and neonatal rabbits. After 24 h of endotoxin administration to adult rabbits, GRP94 mRNA accumulation increases 3-fold in both heart and skeletal muscle and it is followed by a comparable increase in protein accumulation. However, hybridization and immunohistochemistry in situ do not reveal any change in the expression of GRP94 mRNA and protein in skeletal muscle myocytes after endotoxin treatment. Thus skeletal muscle fibres display a unique regulation of the GRP94 gene, which is up-regulated during perinatal development, whereas in the adult animal it is apparently silent and not responsive to endotoxin treatment.
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