Force Relaxation, Labile Heat and Parvalbumin Content of Skeletal Muscle Fibres of Xenopus Laevis

Overview

Journal J Physiol

Specialty Physiology

Date 1993 Apr 1

PMID 8246178

Citations 15

Authors

J Lannergren

G Elzinga

G J Stienen

Affiliations

Soon will be listed here.

Abstract

1. Measurements were made of stable (hb) and labile (ha) maintenance heat rate, slowing of relaxation as a function of tetanus duration, and parvalbumin (PA) content in intact single muscle fibres of types 1 and 2 from Xenopus laevis. The majority of experiments were performed at 20 degrees C. In addition, total and myofibrillar ATPase activity was measured in skinned Xenopus fibres, also of types 1 and 2; these studies were performed at 4 degrees C. 2. In agreement with a previous study hb was significantly higher in type 1 (175 +/- 13 mW (g wet wt)-1; n = 8) than in type 2 fibres (88 +/- 9 mW (g wet wt)-1; n = 7). The value of ha was 236 +/- 22 and 117 +/- 16 mW (g wet wt)-1, respectively (mean +/- S.E.M.). ha decayed with a time constant of 0.27 +/- 0.02 (n = 8) and 0.33 +/- 0.02 s (n = 7). 3. The early relaxation rate of tetanic force, extrapolated to the onset of stimulation (yo + yb; where yo is 'extra' rate of relaxation and yb steady rate) was 85.6 +/- 4.2 s-1 for type 1 fibres (n = 8) and 62.7 +/- 7.3 s-1 for type 2 fibres (n = 7). Relaxation rate at the end of a 1.8 s tetanus (yb) was 29.4 +/- 1.6 and 33.3 +/- 1.5 s-1, respectively; thus, there was more slowing with tetanus duration in type 1 fibres. The time constant for slowing of relaxation with tetanus duration was similar to that for decay of ha. 4. Parvalbumin concentration, [PA], was 0.45 +/- 0.04 mM in type 1 (n = 7) and 0.22 +/- 0.04 mM (n = 7) in type 2 fibres. 5. For individual fibres positive correlations were found between the 'extra' rate of relaxation (yo), labile heat (ha) and [PA]. Significantly more labile heat was liberated than can be accounted for by the enthalpy change of Ca2+ binding to PA. 6. For five fibres (type 1) studied both at 20 and 10 degrees C, the magnitude of slowing of relaxation, expressed as yo/(yo + yb), was 0.58 +/- 0.03 at 20 degrees C and 0.65 +/- 0.03 at 10 degrees C. 7. Both slowing of relaxation and labile heat were depressed in the second of two closely spaced tetani in type 1 fibres. Repriming of both effects followed similar, biphasic time courses and required more than 10 min for completion at 20 degrees C.(ABSTRACT TRUNCATED AT 400 WORDS)

Citing Articles

Relationship between gene expression networks and muscle contractile physiology differences in Anolis lizards.

Smith L, Anderson C, Withangage M, Koch A, Roberts T, Liebl A J Comp Physiol B. 2022; 192(3-4):489-499.

PMID: 35596083 DOI: 10.1007/s00360-022-01441-w.

Energetics of muscle contraction: further trials.

Yamada K J Physiol Sci. 2016; 67(1):19-43.

PMID: 27412384 PMC: 10717381. DOI: 10.1007/s12576-016-0470-3.

Cytosolic calcium transients are a determinant of contraction-induced HSP72 transcription in single skeletal muscle fibers.

Stary C, Hogan M J Appl Physiol (1985). 2016; 120(10):1260-6.

PMID: 26869714 PMC: 4867320. DOI: 10.1152/japplphysiol.01060.2015.

Transcriptomic analysis supports similar functional roles for the two thymuses of the tammar wallaby.

Wong E, Papenfuss A, Heger A, Hsu A, Ponting C, Miller R BMC Genomics. 2011; 12:420.

PMID: 21854594 PMC: 3173455. DOI: 10.1186/1471-2164-12-420.

Gene expression throughout a vertebrate's embryogenesis.

Bozinovic G, Sit T, Hinton D, Oleksiak M BMC Genomics. 2011; 12:132.

PMID: 21356103 PMC: 3062618. DOI: 10.1186/1471-2164-12-132.

References

Rall J, Woledge R . Influence of temperature on mechanics and energetics of muscle contraction. Am J Physiol. 1990; 259(2 Pt 2):R197-203. DOI: 10.1152/ajpregu.1990.259.2.R197. View

Stienen G, Roosemalen M, Wilson M, Elzinga G . Depression of force by phosphate in skinned skeletal muscle fibers of the frog. Am J Physiol. 1990; 259(2 Pt 1):C349-57. DOI: 10.1152/ajpcell.1990.259.2.C349. View

Hou T, Johnson J, Rall J . Parvalbumin content and Ca2+ and Mg2+ dissociation rates correlated with changes in relaxation rate of frog muscle fibres. J Physiol. 1991; 441:285-304. PMC: 1180199. DOI: 10.1113/jphysiol.1991.sp018752. View

Klein M, Kovacs L, Simon B, Schneider M . Decline of myoplasmic Ca2+, recovery of calcium release and sarcoplasmic Ca2+ pump properties in frog skeletal muscle. J Physiol. 1991; 441:639-71. PMC: 1180218. DOI: 10.1113/jphysiol.1991.sp018771. View

Berquin A, Lebacq J . Parvalbumin, labile heat and slowing of relaxation in mouse soleus and extensor digitorum longus muscles. J Physiol. 1992; 445:601-16. PMC: 1180000. DOI: 10.1113/jphysiol.1992.sp018942. View

ABBOTT B . The heat production associated with the maintenance of a prolonged contraction and the extra heat produced during large shortening. J Physiol. 1951; 112(3-4):438-45. PMC: 1393031. DOI: 10.1113/jphysiol.1951.sp004541. View

Homsher E, MOMMAERTS W, RICCHIUTI N, Wallner A . Activation heat, activation metabolism and tension-related heat in frog semitendinosus muscles. J Physiol. 1972; 220(3):601-25. PMC: 1331672. DOI: 10.1113/jphysiol.1972.sp009725. View

MULIERI L, Luhr G, Trefry J, ALPERT N . Metal-film thermopiles for use with rabbit right ventricular papillary muscles. Am J Physiol. 1977; 233(5):C146-56. DOI: 10.1152/ajpcell.1977.233.5.C146. View

Homsher E, Kean C . Skeletal muscle energetics and metabolism. Annu Rev Physiol. 1978; 40:93-131. DOI: 10.1146/annurev.ph.40.030178.000521. View

10.

BLINKS J, Rudel R, Taylor S . Calcium transients in isolated amphibian skeletal muscle fibres: detection with aequorin. J Physiol. 1978; 277:291-323. PMC: 1282390. DOI: 10.1113/jphysiol.1978.sp012273. View

11.

Curtin N, Woledge R . Chemical change and energy production during contraction of frog muscle: how are their time courses related?. J Physiol. 1979; 288:353-66. PMC: 1281430. View

12.

Glyn H, Sleep J . Dependence of adenosine triphosphatase activity of rabbit psoas muscle fibres and myofibrils on substrate concentration. J Physiol. 1985; 365:259-76. PMC: 1193000. DOI: 10.1113/jphysiol.1985.sp015770. View

13.

Peckham M, Woledge R . Labile heat and changes in rate of relaxation of frog muscles. J Physiol. 1986; 374:123-35. PMC: 1182711. DOI: 10.1113/jphysiol.1986.sp016070. View

14.

Curtin N, HOWARTH J, Rall J, Wilson M, Woledge R . Absolute values of myothermic measurements on single muscle fibres from frog. J Muscle Res Cell Motil. 1986; 7(4):327-32. DOI: 10.1007/BF01753653. View

15.

Tanokura M, Yamada K . Heat capacity and entropy changes of the two major isotypes of bullfrog (Rana catesbeiana) parvalbumins induced by calcium binding. Biochemistry. 1987; 26(24):7668-74. DOI: 10.1021/bi00398a020. View

16.

Homsher E, Lacktis J, Yamada T, Zohman G . Repriming and reversal of the isometric unexplained enthalpy in frog skeletal muscle. J Physiol. 1987; 393:157-70. PMC: 1192387. DOI: 10.1113/jphysiol.1987.sp016817. View

17.

Elzinga G, Lannergren J, Stienen G . Stable maintenance heat rate and contractile properties of different single muscle fibres from Xenopus laevis at 20 degrees C. J Physiol. 1987; 393:399-412. PMC: 1192399. DOI: 10.1113/jphysiol.1987.sp016829. View

18.

Kitano T . Effect of carbon dioxide on heat production of frog skeletal muscles. J Physiol. 1988; 397:643-55. PMC: 1192147. DOI: 10.1113/jphysiol.1988.sp017023. View

19.

Simonides W, van Hardeveld C . Identification and quantification in single muscle fibers of four isoforms of parvalbumin in the iliofibularis muscle of Xenopus laevis. Biochim Biophys Acta. 1989; 998(2):137-44. DOI: 10.1016/0167-4838(89)90265-3. View

20.

Kurebayashi N, Ogawa Y . Discrimination of Ca(2+)-ATPase activity of the sarcoplasmic reticulum from actomyosin-type ATPase activity of myofibrils in skinned mammalian skeletal muscle fibres: distinct effects of cyclopiazonic acid on the two ATPase activities. J Muscle Res Cell Motil. 1991; 12(4):355-65. DOI: 10.1007/BF01738590. View