Measurements of basal d‐glucose transport through GLUT1 across the intact plasma membrane of isolated segments from single fast‐ and slow‐twitch skeletal muscle fibres of rat
Aim To develop a method for direct measurement of the fluorescent d‐glucose analogue 2‐NBDG transport across the plasma membrane of single skeletal muscle fibres and derive the theoretical framework for determining the kinetic parameters for d‐glucose transport under basal conditions. Methods A nove...
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Published in | Acta Physiologica Vol. 234; no. 4; pp. e13789 - n/a |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
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01.04.2022
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Abstract | Aim
To develop a method for direct measurement of the fluorescent d‐glucose analogue 2‐NBDG transport across the plasma membrane of single skeletal muscle fibres and derive the theoretical framework for determining the kinetic parameters for d‐glucose transport under basal conditions.
Methods
A novel method is described for measuring free 2‐NBDG transport across plasma membrane of single rat muscle fibres at rest. The 2‐NBDG uptake was >90% suppressed by 100 µM cytochalasin B in both fast‐twitch and slow‐twitch fibres, indicating that the 2‐NBDG transport is GLUT‐mediated. Fibres were identified as fast‐twitch or slow‐twitch based on the differential sensitivity of their contractile apparatus to Sr2+.
Results
The time course of 2‐NBDG uptake in the presence of 50 µM 2‐NBDG follows a one‐phase exponential plateau curve and is faster in fast‐twitch (rate constant 0.053 ± 0.0024 s‐1) than in slow‐twitch fibres (rate constant 0.031 ± 0.0021 s‐1). The rate constants were markedly reduced in the presence of 20 mM d‐glucose to 0.0082 ± 0.0004 s‐1 and 0.0056 ± 0.0002 s‐1 in fast‐twitch and slow‐twitch fibres respectively. 2‐NBDG transport was asymmetric, consistent with GLUT1 being the major functional GLUT isoform transporting 2‐NBDG in muscle fibres at rest. The parameters describing the transport kinetics for both 2‐NBDG and d‐glucose (dissociation constants, Michaelis–Menten constants, maximal rates of uptake and outflow) were calculated from the measurements made with 2‐NBDG.
Conclusion
Free 2‐NBDG and d‐glucose transport across the plasma membrane of single rat muscle fibres at rest is fast, conclusively showing that the rate‐limiting step in d‐glucose uptake in skeletal muscle is not necessarily the GLUT‐mediated transport of d‐glucose. |
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AbstractList | Abstract
Aim
To develop a method for direct measurement of the fluorescent
d
‐glucose analogue 2‐NBDG transport across the plasma membrane of single skeletal muscle fibres and derive the theoretical framework for determining the kinetic parameters for
d
‐glucose transport under basal conditions.
Methods
A novel method is described for measuring free 2‐NBDG transport across plasma membrane of single rat muscle fibres at rest. The 2‐NBDG uptake was >90% suppressed by 100 µM cytochalasin B in both fast‐twitch and slow‐twitch fibres, indicating that the 2‐NBDG transport is GLUT‐mediated. Fibres were identified as fast‐twitch or slow‐twitch based on the differential sensitivity of their contractile apparatus to Sr
2+
.
Results
The time course of 2‐NBDG uptake in the presence of 50 µM 2‐NBDG follows a one‐phase exponential plateau curve and is faster in fast‐twitch (rate constant 0.053 ± 0.0024 s
‐1
) than in slow‐twitch fibres (rate constant 0.031 ± 0.0021 s
‐1
). The rate constants were markedly reduced in the presence of 20 mM
d
‐glucose to 0.0082 ± 0.0004 s
‐1
and 0.0056 ± 0.0002 s
‐1
in fast‐twitch and slow‐twitch fibres respectively. 2‐NBDG transport was asymmetric, consistent with GLUT1 being the major functional GLUT isoform transporting 2‐NBDG in muscle fibres at rest. The parameters describing the transport kinetics for both 2‐NBDG and
d
‐glucose (dissociation constants, Michaelis–Menten constants, maximal rates of uptake and outflow) were calculated from the measurements made with 2‐NBDG.
Conclusion
Free 2‐NBDG and
d
‐glucose transport across the plasma membrane of single rat muscle fibres at rest is fast, conclusively showing that the rate‐limiting step in
d
‐glucose uptake in skeletal muscle is not necessarily the GLUT‐mediated transport of
d
‐glucose. AIMTo develop a method for direct measurement of the fluorescent d-glucose analogue 2-NBDG transport across the plasma membrane of single skeletal muscle fibres and derive the theoretical framework for determining the kinetic parameters for d-glucose transport under basal conditions. METHODSA novel method is described for measuring free 2-NBDG transport across plasma membrane of single rat muscle fibres at rest. The 2-NBDG uptake was >90% suppressed by 100 µM cytochalasin B in both fast-twitch and slow-twitch fibres, indicating that the 2-NBDG transport is GLUT-mediated. Fibres were identified as fast-twitch or slow-twitch based on the differential sensitivity of their contractile apparatus to Sr2+ . RESULTSThe time course of 2-NBDG uptake in the presence of 50 µM 2-NBDG follows a one-phase exponential plateau curve and is faster in fast-twitch (rate constant 0.053 ± 0.0024 s-1 ) than in slow-twitch fibres (rate constant 0.031 ± 0.0021 s-1 ). The rate constants were markedly reduced in the presence of 20 mM d-glucose to 0.0082 ± 0.0004 s-1 and 0.0056 ± 0.0002 s-1 in fast-twitch and slow-twitch fibres respectively. 2-NBDG transport was asymmetric, consistent with GLUT1 being the major functional GLUT isoform transporting 2-NBDG in muscle fibres at rest. The parameters describing the transport kinetics for both 2-NBDG and d-glucose (dissociation constants, Michaelis-Menten constants, maximal rates of uptake and outflow) were calculated from the measurements made with 2-NBDG. CONCLUSIONFree 2-NBDG and d-glucose transport across the plasma membrane of single rat muscle fibres at rest is fast, conclusively showing that the rate-limiting step in d-glucose uptake in skeletal muscle is not necessarily the GLUT-mediated transport of d-glucose. To develop a method for direct measurement of the fluorescent d-glucose analogue 2-NBDG transport across the plasma membrane of single skeletal muscle fibres and derive the theoretical framework for determining the kinetic parameters for d-glucose transport under basal conditions. A novel method is described for measuring free 2-NBDG transport across plasma membrane of single rat muscle fibres at rest. The 2-NBDG uptake was >90% suppressed by 100 µM cytochalasin B in both fast-twitch and slow-twitch fibres, indicating that the 2-NBDG transport is GLUT-mediated. Fibres were identified as fast-twitch or slow-twitch based on the differential sensitivity of their contractile apparatus to Sr . The time course of 2-NBDG uptake in the presence of 50 µM 2-NBDG follows a one-phase exponential plateau curve and is faster in fast-twitch (rate constant 0.053 ± 0.0024 s ) than in slow-twitch fibres (rate constant 0.031 ± 0.0021 s ). The rate constants were markedly reduced in the presence of 20 mM d-glucose to 0.0082 ± 0.0004 s and 0.0056 ± 0.0002 s in fast-twitch and slow-twitch fibres respectively. 2-NBDG transport was asymmetric, consistent with GLUT1 being the major functional GLUT isoform transporting 2-NBDG in muscle fibres at rest. The parameters describing the transport kinetics for both 2-NBDG and d-glucose (dissociation constants, Michaelis-Menten constants, maximal rates of uptake and outflow) were calculated from the measurements made with 2-NBDG. Free 2-NBDG and d-glucose transport across the plasma membrane of single rat muscle fibres at rest is fast, conclusively showing that the rate-limiting step in d-glucose uptake in skeletal muscle is not necessarily the GLUT-mediated transport of d-glucose. Aim To develop a method for direct measurement of the fluorescent d‐glucose analogue 2‐NBDG transport across the plasma membrane of single skeletal muscle fibres and derive the theoretical framework for determining the kinetic parameters for d‐glucose transport under basal conditions. Methods A novel method is described for measuring free 2‐NBDG transport across plasma membrane of single rat muscle fibres at rest. The 2‐NBDG uptake was >90% suppressed by 100 µM cytochalasin B in both fast‐twitch and slow‐twitch fibres, indicating that the 2‐NBDG transport is GLUT‐mediated. Fibres were identified as fast‐twitch or slow‐twitch based on the differential sensitivity of their contractile apparatus to Sr2+. Results The time course of 2‐NBDG uptake in the presence of 50 µM 2‐NBDG follows a one‐phase exponential plateau curve and is faster in fast‐twitch (rate constant 0.053 ± 0.0024 s‐1) than in slow‐twitch fibres (rate constant 0.031 ± 0.0021 s‐1). The rate constants were markedly reduced in the presence of 20 mM d‐glucose to 0.0082 ± 0.0004 s‐1 and 0.0056 ± 0.0002 s‐1 in fast‐twitch and slow‐twitch fibres respectively. 2‐NBDG transport was asymmetric, consistent with GLUT1 being the major functional GLUT isoform transporting 2‐NBDG in muscle fibres at rest. The parameters describing the transport kinetics for both 2‐NBDG and d‐glucose (dissociation constants, Michaelis–Menten constants, maximal rates of uptake and outflow) were calculated from the measurements made with 2‐NBDG. Conclusion Free 2‐NBDG and d‐glucose transport across the plasma membrane of single rat muscle fibres at rest is fast, conclusively showing that the rate‐limiting step in d‐glucose uptake in skeletal muscle is not necessarily the GLUT‐mediated transport of d‐glucose. |
Author | Rudayni, Hassan A. Posterino, Giuseppe S. Stephenson, George |
Author_xml | – sequence: 1 givenname: Hassan A. orcidid: 0000-0003-4464-5989 surname: Rudayni fullname: Rudayni, Hassan A. email: harudayni@imamu.edu.sa organization: Imam Mohammad Ibn Saud Islamic University – sequence: 2 givenname: George orcidid: 0000-0002-7095-4817 surname: Stephenson fullname: Stephenson, George organization: La Trobe University – sequence: 3 givenname: Giuseppe S. orcidid: 0000-0003-2539-1469 surname: Posterino fullname: Posterino, Giuseppe S. email: g.posterino@latrobe.edu.au organization: La Trobe University |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/35038771$$D View this record in MEDLINE/PubMed |
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Keywords | fast-twitch muscle fibres GLUT1 d-glucose transport kinetics 2-NBDG transport in single muscle fibres slow-twitch muscle fibres |
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To develop a method for direct measurement of the fluorescent d‐glucose analogue 2‐NBDG transport across the plasma membrane of single skeletal muscle... To develop a method for direct measurement of the fluorescent d-glucose analogue 2-NBDG transport across the plasma membrane of single skeletal muscle fibres... Abstract Aim To develop a method for direct measurement of the fluorescent d ‐glucose analogue 2‐NBDG transport across the plasma membrane of single skeletal... AimTo develop a method for direct measurement of the fluorescent d‐glucose analogue 2‐NBDG transport across the plasma membrane of single skeletal muscle... AIMTo develop a method for direct measurement of the fluorescent d-glucose analogue 2-NBDG transport across the plasma membrane of single skeletal muscle... |
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SubjectTerms | 2‐NBDG transport in single muscle fibres Animals Calcium - metabolism Cell Membrane - metabolism Cytochalasin B d‐glucose transport kinetics fast‐twitch muscle fibres Glucose Glucose - metabolism Glucose transport Glucose Transporter Type 1 - metabolism GLUT1 Muscle contraction Muscle Contraction - physiology Muscle Fibers, Fast-Twitch - metabolism Muscle Fibers, Skeletal - metabolism Muscle Fibers, Slow-Twitch - metabolism Muscle, Skeletal - metabolism Musculoskeletal system Plasma Rats Skeletal muscle slow‐twitch muscle fibres |
Title | Measurements of basal d‐glucose transport through GLUT1 across the intact plasma membrane of isolated segments from single fast‐ and slow‐twitch skeletal muscle fibres of rat |
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