ArticleJournal of muscle research and cell motility1995
Porin-type 1 proteins in sarcoplasmic reticulum and plasmalemma of striated muscle fibres.
Article in Journal of muscle research and cell motility, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 38 citations in OpenAlex.
- Mitochondrial localization of PABPN1 in oculopharyngeal muscular dystrophy.Laboratory investigation; a journal of technical methods and pathology · 2019Article
- Voltage-Dependent Anion Channel 1 As an Emerging Drug Target for Novel Anti-Cancer Therapeutics.Frontiers in oncology · 2017Review
- Voltage-dependent anion channel 1-based peptides interact with Bcl-2 to prevent antiapoptotic activity.The Journal of biological chemistry · 2010Article
- Porin isoform 2 has a different localization in Drosophila melanogaster ovaries than porin 1.Journal of bioenergetics and biomembranes · 2008Article
- The voltage-dependent anion channel in endoplasmic/sarcoplasmic reticulum: characterization, modulation and possible function.The Journal of membrane biology · 2005Review
- A novel signalling pathway originating in mitochondria modulates rat skeletal muscle membrane excitability.The Journal of physiology · 2003Article
- Characterization of channel-forming activity in muscle biopsy from a porin-deficient human patient.Journal of bioenergetics and biomembranes · 2000Article
- Extramitochondrial porin: facts and hypotheses.Journal of bioenergetics and biomembranes · 2000Review
- Intracellular localization and isoform expression of the voltage-dependent anion channel (VDAC) in normal and dystrophic skeletal muscle.Journal of muscle research and cell motility · 2000Article
- Mechanisms underlying phosphate-induced failure of Ca2+ release in single skinned skeletal muscle fibres of the rat.The Journal of physiology · 1998Article
- Voltage-dependent anion channel proteins in synaptosomes of the torpedo electric organ: immunolocalization, purification, and characterization.Journal of bioenergetics and biomembranes · 1998Article
- ATP inhibition and rectification of a Ca2+-activated anion channel in sarcoplasmic reticulum of skeletal muscle.Biophysical journal · 1998Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The location of porin-type 1 proteins in mammalian striated muscle has been assessed using immunogold electron microscopy with an anti-porin 31HL monoclonal antibody as the primary antibody. Gold particles were found on the mitochondrial outer membrane, the sarcoplasmic reticulum and plasmalemma in longitudinal sections of rat and rabbit skeletal muscle and rabbit and sheep cardiac muscle. The relative densities of gold particles in the mitochondrial outer membrane, sarcoplasmic reticulum and plasmalemma were 7:3:1 in white sternomastoid muscle, for example. Skeletal and cardiac sarcoplasmic reticulum vesicles, which had been fractionated by discontinuous sucrose density centrifugation, were subjected to SDS-polyacrylamide gel electrophoresis and Western blotting. The anti-porin 31HL monoclonal antibody detected a band of relative molecular mass (M(r)) 31,000 in all muscle sarcoplasmic reticulum vesicle fractions and also in liver mitochondria. The intensity of immunostaining of the sarcoplasmic reticulum fractions was 2.5-10% that of mitochondrial outer membranes per microgram of membrane protein blotted. Contamination of the sarcoplasmic reticulum fractions by mitochondrial outer membrane was < 0.75% as determined from the specific activity of monoamine oxidase. Thus, only a small part of the porin detected in sarcoplasmic reticulum vesicles can be attributed to mitochondrial contamination. These results show that porin-type1 immunoreactivity is not restricted to mitochondria but found in the sarcoplasmic reticulum and plasmalemma of both mammalian skeletal and cardiac muscle.
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