Polymorphism of contractile proteins

Gros, François; Buckingham, Margaret

doi:10.1002/bip.360260016

Cited by 7 publications

(3 citation statements)

References 34 publications

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“…Studies with the peptide phalloidin, which binds specifically to actin and strengthens the interaction between actin monomers (Estes et al, 1981), have been reported to alter the Ca2+ sensitivity of the thin filament (e.g., Bukatina et al, 1995), suggesting that an actin-mediated mechanism is feasible. However, the two fiber types used here contain the same actin isoform (Gros and Buckingham, 1989). Therefore, an actin-mediated pathway would require that the actomyosin interaction produce conformational changes in actin that are specific to the myosin isoform and the nucleotide bound to myosin.…”

Section: Effect Of Nucleotide On Ca2+-activated Tension and Stiffnessmentioning

confidence: 99%

Nucleotide-Dependent Contractile Properties of Ca2+-Activated Fast and Slow Skeletal Muscle Fibers

Wahr

Cantor

Metzger

1997

Biophysical Journal

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The relation between single skinned skeletal fiber contractile mechanics and the myosin mechanoenzyme was examined by perturbing the actomyosin interaction with the ATP analog CTP in fibers from both rabbit psoas and rat soleus. Tension, instantaneous stiffness, and the rate of tension redevelopment (ktr), under software-based sarcomere length control, were examined at 15 degrees C for a range of Ca2+ concentrations in both fiber types. CTP produced 94% of the maximum ATP-generated tension in psoas fibers and 77% in soleus fibers. In psoas, CTP also increased stiffness to 106% of the ATP stiffness, whereas in soleus stiffness decreased to 92%. Thus, part of the greater difference between maximum ATP- and CTP-generated tension in soleus fibers appears to be due to a decrease in strongly bound cross-bridge number. Interestingly, although the nucleotide exchange produced substantial increases in the steepness (nH) of the tension- and stiffness-pCa relationships in soleus fibers, only minor changes were seen in psoas fibers. At maximum Ca2+ and nominal P(i) levels, ktr in psoas fibers increased from 11.7 s-1 with ATP to 16.6 s-1 with CTP and in soleus fibers from 4.9 to 8.4 s-1. Increased P(i) levels decreased the maximum Ca(2+)-activated tension in both fiber types and increased the ktr of psoas fibers, but the ktr of soleus fibers was not significantly altered. Thus, although the nucleotide exchange generally produced similar changes in the mechanics, there were significant muscle lineage differences in the tension- and stiffness-pCa relations and in the effects of P(i) on ktr, such that differences in contractile mechanics were lessened in the presence of CTP.

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Section: Effect Of Nucleotide On Ca2+-activated Tension and Stiffnessmentioning

confidence: 99%

Nucleotide-Dependent Contractile Properties of Ca2+-Activated Fast and Slow Skeletal Muscle Fibers

Wahr

Cantor

Metzger

1997

Biophysical Journal

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“…The requirement for the expression of a growth-related isoform in fish, or indeed for the expression of embryonic/neonatal MyoHC isoforms during early muscle development, is unresolved. According to the so-called 'functional' hypothesis (Gros and Buckingham, 1987), the differential expression of various MyoHC isoforms throughout development and in the different fibre types of the adult are consequences of various functional demands on the molecule dictating the evolution of a multigene family by selective pressure. Such functional demands may possibly reside in the S1 region of the molecule, where differences in primary structure could affect its actin binding properties and ATPase activity.…”

Section: Discussionmentioning

confidence: 99%

Small-Diameter White Myotomal Muscle Fibres Associated With Growth Hyperplasia in the Carp (Cyprinus Carpio) ExPress a Distinct Myosin Heavy Chain Gene

Ennion

Gauvry

Butterworth

et al. 1995

Journal of Experimental Biology

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A carp myosin heavy chain gene isoform was isolated from a genomic clone, restriction mapped and partially sequenced to reveal the location of various exons. The clone contains a complete gene of approximately 12.0 kb which is half the size of the corresponding mammalian and avian myosin heavy chain genes. The mRNA transcript of this gene, however, is the same size as mammalian and avian striated muscle myosin heavy chain genes (about 6000 nucleotides), illustrating that the difference in size at the genomic level is due to shorter introns. A 169 bp NsiI restriction fragment containing only the 3' untranslated region of this gene was subcloned and used as an isoform-specific probe to study the expression of this particular isoform. Hybridisation analysis could only detect expression of this myosin heavy chain gene in the white muscle of adult carp that had been subjected to an increased environmental temperature. No expression of this gene was detected in carp under 1 year of age. In situ hybridisation demonstrated that expression of this gene is limited to small-diameter white muscle fibres of adult carp, which are thought to be responsible for muscle growth by fibre hyperplasia.

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“…The wide range of myosin' s forms may be the result of polymorphisms (Gros & Buckingham, 1987). Polymorphisms can lead into discussions on "types" and varieties within a group and, if time permits, on balancing selection, epigenetics, and phenotypic variants.…”

Section: Connecting Concepts: Proteins Predator Strategies and Functmentioning

confidence: 99%

How to Build a Super Predator

Babaian¹,

Kumar²

2021

The American Biology Teacher

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We present a drawing discovery lab that crosscuts multiple disciplines in biology and links concepts in genetics and evolutionary thinking to enhance understanding of the genotype-to-phenotype transformation. These combined concepts are also linked to ecological frameworks in nature through the model of biological plasticity. Students and teachers explore drawing skills to flesh out the future of a predator while engaging with the computational software MEGA, which introduces students and teachers to nucleotide changes, mutations, variation, phylogenetics, and molecular evolution.

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Polymorphism of contractile proteins

Cited by 7 publications

References 34 publications

Nucleotide-Dependent Contractile Properties of Ca2+-Activated Fast and Slow Skeletal Muscle Fibers

Nucleotide-Dependent Contractile Properties of Ca2+-Activated Fast and Slow Skeletal Muscle Fibers

Small-Diameter White Myotomal Muscle Fibres Associated With Growth Hyperplasia in the Carp (Cyprinus Carpio) ExPress a Distinct Myosin Heavy Chain Gene

How to Build a Super Predator

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