FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2094833610> ?p ?o ?g. }

• W2094833610 endingPage "23" @default.
• W2094833610 startingPage "13" @default.
• W2094833610 abstract "Sarcoplasmic reticulum (SR) serves a central role in calcium uptake and release, thereby regulating muscle relaxation and contraction, respectively. Recently, we have isolated fractions referable to longitudinal tubules (R2) and terminal cisternae (R4), the two major types of sarcoplasmic reticulum (A. Saito et al. (1984) J. Cell Biol. 99, 875-885). The terminal cisternae contain two types of membranes, the calcium pump membrane and the junctional face membrane. The terminal cisternae are filled with electron-opaque contents which serve as a Ca2+ reservoir. The longitudinal tubules consist mainly of the calcium pump membrane. In this study, we describe a new longitudinal tubule fraction (F2) and characterize it together with the R2 and R4 SR fractions. The calcium pump membrane of the longitudinal tubules is a highly specialized membrane consisting of about 90% calcium pump protein as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Extensive changes in morphology can be observed in the SR fractions referable to osmotic differences during the fixation conditions using either glutaraldehyde-tannic acid or osmium tetroxide fixatives. The changes include swelling or shrinkage and aggregation of the compartmental contents when the fixative contains calcium ions. The two types of SR have different osmotic permeability to the same medium, as indicated by differential swelling or shrinkage. Both longitudinal tubule and terminal cisternae vesicles of SR appear larger and are spherical vesicles when the glutaraldehyde-tannic acid fixative is isotonic as compared with the standard fixation method. We have previously reported that the ruthenium red-sensitive calcium release channels are localized to the terminal cisternae. The terminal cisternae as isolated are leaky to Ca2+ since these channels are in the open state (S. Fleischer et al. (1985) Proc. Natl. Acad. Sci USA 82, 7256-7259). Thus, the Ca2+, Mg2+-dependent ATPase (Ca2+ ATPase) rate is only slightly enhanced in the presence of a Ca2+ ionophore, which dissipates the Ca2+ gradient across the SR membrane. We now find that preincubation with ruthenium red restores the tight coupling of the Ca2+ ATPase activity to Ca2+ transport. That is to say, ATPase activity is reduced and the addition of ionophore stimulates the Ca2+ ATPase activity 4- to 7-fold. The Ca2+ ATPase activity in longitudinal tubules is already tightly coupled. It is minimal after a Ca2+ gradient has been generated, but can be stimulated 9- to 20-fold when the Ca2+ gradient is dissipated with ionophore. This finding suggests that the Ca2+ ATPase activity in SR is tightly coupled to Ca2+ transport in situ." @default.
• W2094833610 created "2016-06-24" @default.
• W2094833610 creator A5016750178 @default.
• W2094833610 creator A5028391222 @default.
• W2094833610 creator A5067197555 @default.
• W2094833610 date "1987-10-01" @default.
• W2094833610 modified "2023-09-25" @default.
• W2094833610 title "Preparation and characterization of longitudinal tubules of sarcoplasmic reticulum from fast skeletal muscle" @default.
• W2094833610 cites W125040153 @default.
• W2094833610 cites W1543140440 @default.
• W2094833610 cites W1563253655 @default.
• W2094833610 cites W1565088140 @default.
• W2094833610 cites W1604248953 @default.
• W2094833610 cites W1633786871 @default.
• W2094833610 cites W1775749144 @default.
• W2094833610 cites W1890043375 @default.
• W2094833610 cites W1952906612 @default.
• W2094833610 cites W2002885745 @default.
• W2094833610 cites W2004073919 @default.
• W2094833610 cites W2017342563 @default.
• W2094833610 cites W2019843818 @default.
• W2094833610 cites W2059647854 @default.
• W2094833610 cites W2060527098 @default.
• W2094833610 cites W2064775579 @default.
• W2094833610 cites W2074849129 @default.
• W2094833610 cites W2093433788 @default.
• W2094833610 cites W2100837269 @default.
• W2094833610 cites W2175093448 @default.
• W2094833610 cites W2278844900 @default.
• W2094833610 cites W2405138165 @default.
• W2094833610 doi "https://doi.org/10.1016/0003-9861(87)90317-1" @default.
• W2094833610 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2444161" @default.
• W2094833610 hasPublicationYear "1987" @default.
• W2094833610 type Work @default.
• W2094833610 sameAs 2094833610 @default.
• W2094833610 citedByCount "25" @default.
• W2094833610 countsByYear W20948336102012 @default.
• W2094833610 crossrefType "journal-article" @default.
• W2094833610 hasAuthorship W2094833610A5016750178 @default.
• W2094833610 hasAuthorship W2094833610A5028391222 @default.
• W2094833610 hasAuthorship W2094833610A5067197555 @default.
• W2094833610 hasConcept C120665830 @default.
• W2094833610 hasConcept C121332964 @default.
• W2094833610 hasConcept C12554922 @default.
• W2094833610 hasConcept C130316041 @default.
• W2094833610 hasConcept C139966638 @default.
• W2094833610 hasConcept C158617107 @default.
• W2094833610 hasConcept C178790620 @default.
• W2094833610 hasConcept C185592680 @default.
• W2094833610 hasConcept C190062978 @default.
• W2094833610 hasConcept C2777529624 @default.
• W2094833610 hasConcept C2779424567 @default.
• W2094833610 hasConcept C2780848204 @default.
• W2094833610 hasConcept C2781393965 @default.
• W2094833610 hasConcept C41625074 @default.
• W2094833610 hasConcept C43617362 @default.
• W2094833610 hasConcept C519063684 @default.
• W2094833610 hasConcept C55493867 @default.
• W2094833610 hasConcept C86803240 @default.
• W2094833610 hasConcept C93877712 @default.
• W2094833610 hasConceptScore W2094833610C120665830 @default.
• W2094833610 hasConceptScore W2094833610C121332964 @default.
• W2094833610 hasConceptScore W2094833610C12554922 @default.
• W2094833610 hasConceptScore W2094833610C130316041 @default.
• W2094833610 hasConceptScore W2094833610C139966638 @default.
• W2094833610 hasConceptScore W2094833610C158617107 @default.
• W2094833610 hasConceptScore W2094833610C178790620 @default.
• W2094833610 hasConceptScore W2094833610C185592680 @default.
• W2094833610 hasConceptScore W2094833610C190062978 @default.
• W2094833610 hasConceptScore W2094833610C2777529624 @default.
• W2094833610 hasConceptScore W2094833610C2779424567 @default.
• W2094833610 hasConceptScore W2094833610C2780848204 @default.
• W2094833610 hasConceptScore W2094833610C2781393965 @default.
• W2094833610 hasConceptScore W2094833610C41625074 @default.
• W2094833610 hasConceptScore W2094833610C43617362 @default.
• W2094833610 hasConceptScore W2094833610C519063684 @default.
• W2094833610 hasConceptScore W2094833610C55493867 @default.
• W2094833610 hasConceptScore W2094833610C86803240 @default.
• W2094833610 hasConceptScore W2094833610C93877712 @default.
• W2094833610 hasIssue "1" @default.
• W2094833610 hasLocation W20948336101 @default.
• W2094833610 hasLocation W20948336102 @default.
• W2094833610 hasOpenAccess W2094833610 @default.
• W2094833610 hasPrimaryLocation W20948336101 @default.
• W2094833610 hasRelatedWork W2055072170 @default.
• W2094833610 hasRelatedWork W2063510804 @default.
• W2094833610 hasRelatedWork W2065843407 @default.
• W2094833610 hasRelatedWork W2081095779 @default.
• W2094833610 hasRelatedWork W2083105222 @default.
• W2094833610 hasRelatedWork W2101435875 @default.
• W2094833610 hasRelatedWork W2359370715 @default.
• W2094833610 hasRelatedWork W2436809931 @default.
• W2094833610 hasRelatedWork W3036974360 @default.
• W2094833610 hasRelatedWork W1968909559 @default.
• W2094833610 hasVolume "258" @default.
• W2094833610 isParatext "false" @default.
• W2094833610 isRetracted "false" @default.
• W2094833610 magId "2094833610" @default.

• next