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Published on: September 22, 2009
Development transitions of thin filament proteins in rat extraocular muscles
Carole L Moncman1, Miguel E Andrade, Andrea A McCool
1Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY 40536, United States. cmonc2@uky.edu
Insights
Between postnatal day 10 and 15, rat extraocular muscles undergo critical myosin transitions, with changes in alpha-actinin 3 and nebulin expression indicating maturation coinciding with eyelid opening.
Area of Science:
- Muscle Physiology
- Developmental Biology
- Biochemistry
Background:
- Extraocular muscles are unique striated muscles with distinct developmental patterns.
- Postnatal development involves significant myosin isoform transitions in these muscles.
Purpose of the Study:
- To investigate the postnatal expression and distribution of alpha-actinin, tropomyosin, and nebulin isoforms in rat extraocular muscles.
- To correlate these changes with known myosin isoform transitions during development.
Main Methods:
- Gel electrophoresis and western blotting were used to monitor protein expression.
- Analysis focused on postnatal days P10 to P15, a critical developmental window.
Main Results:
- Alpha-actinin 3 expression begins around postnatal day 15.
- Nebulin shows a lower molecular mass at P5-10, increasing by P15.
- These changes in alpha-actinin 3 and nebulin coincide with myosin isoform shifts.
Conclusions:
- The period between postnatal day 10 and 15 is a critical window for extraocular muscle maturation.
- These molecular changes correlate with functional development, including eyelid opening.
Abstract:
Extraocular muscles are a unique subset of striated muscles. During postnatal development, the extraocular muscles undergo a number of myosin isoform transitions that occur between postnatal day P10 (P10) and P15. These include: (1) loss of embryonic myosin from the global layer resulting in the expression restricted to the orbital layer; (2) the onset of expression of extraocular myosin and the putative tonic myosin (myh 7b/14); and (3) the redistribution of nonmuscle myosin IIB from a subsarcolemmal position to a sarcomeric distribution in the slow fibers of the global layer. For this study, we examined the postnatal appearance and distribution of α-actinin, tropomyosin, and nebulin isoforms during postnatal development of the rat extraocular muscles. Although sarcomeric α-actinin is detectable from birth, α-actinin 3 appears around P15. Both tropomyosin-1 and -2 are present from birth in the same distribution as in the adult animal. The expression of nebulin was monitored by gel electrophoresis and western blots. At P5-10, nebulin exhibits a lower molecular mass than observed P15 and later during postnatal development. The changes in α-actinin 3 and nebulin expression between P10 and P15 coincide with transitions in myosin isoforms as detailed above. These data point to P10-P15 as the critical period for the maturation of the extraocular muscles, coinciding with eyelid opening.
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