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Cameron Marzvaan

5/11/17
Engl 363
Dr. Bruce

Working Title: Review of Proposed Mechanisms for Post-Activation Potentiation

Purpose: Team Awesomes purpose is to review recent scientific literature on the

mechanisms of post-activation potentiation.

Introduction: Muscles have a short-term contractile history that allows them to

produce greater force upon subsequent contractions (within ~2-20 minutes), a

phenomenon referred to as post-activation potentiation (PAP). This is thought to

occur mainly through two mechanisms, phosphorylation of regulatory myosin light


[Janices sources]
chains (MLC2) and increased recruitment of higher order motor units
[1,2,3,4]
. During the process of skeletal muscle contraction, an action potential first

propagates through the efferent nervous system, until it reaches the myocyte. Here

the sarcoplasmic reticulum releases calcium ions (Ca 2+), initiating the sliding of

myosin and actin past one another. This changes the shape of the muscle cell, and

thus produces force for movement. The release of Ca 2+ has also been shown to

ultimately phosphorylate MLC2, increasing skeletal muscles sensitivity to Ca 2+. The

result is that subsequent contractions within a short period of time produce greater

force. While Janice will go into depth on this mechanism, the following sources

illuminate the nervous systems role in PAP.

Annotations (APA style):

1. Bozzo, C., Spolaore, B., Toniolo, L., Stevens, L., Bastide, B.,

Cieniewski-Bernard, C., Fontana, A., Mounier, Y., & Reggiani, C.


Cameron Marzvaan
5/11/17
Engl 363
Dr. Bruce

(2005). Nerve influence on myosin light chain phosphorylation in

slow and fast skeletal muscles. FEBS Journal, 272: 57715785

Conclusion: Neural stimulation of skeletal muscle affects control of post-

translational modifications of myosin.

Merit: This paper studied the effects of denervation, chronic low-frequency

stimulation, and chronic administration of a calcineurin inhibitor on fast and slow

muscles. Results illustrated that low levels of MLC2 phosphorylation, and even

expression of slow myosin, were determined by low-frequency neural discharges.

Also, this paper suggested that MLC kinase, expressed by calcineurin-independent

pathways, regulated MLC2 phosphorylation. Thus, this paper can be used to

establish a connection between neural stimulation and MLC2 phosphorylation.

2. Gullich, A., Schmidtbleicher, D. MVC-induced short-term

potentiation of explosive force. (1996). New Studies in Athletics,

11 (4): 67-81

Conclusion: Maximal voluntary contractions performed immediately prior to

explosive exercises of similar biomechanics increases explosive performance in

athletes.

Merit: This paper built upon Luscher et al.s conclusions by measuring changes in H-

wave amplitude of a human muscle before and after stimulation. An H-wave is the

second of two electrical responses in a muscle observed after a submaximal

electrical impulse. This study reported increased H-wave amplitude by PAP, as a


Cameron Marzvaan
5/11/17
Engl 363
Dr. Bruce

result of increased spinal cord motoneuron recruitment. This paper therefore

demonstrates the merit of Luscher et al.s findings, but in humans and in greater

detail.

3. Luscher, H.R., Ruenzel, P., Henneman, E. Composite EPSPs in

motoneurons of different sizes before and during PTP:

implications for transmission failure and its relief in Ia

projections. (1983). Journal of Neurophysiology, 49 (1): 269-89

Conclusion: PAP reduces transmission failures to large motoneurons in cats.

Merit: This paper proposed a mechanism for the increased transmission of

excitation potentials across spinal cord synaptic intersections. An afferent action

potential travels to the spinal cord. This activates an adjacent alpha-motoneuron,

then the signal travels back to the agonist muscle and initiates contraction. This

clear explanation of increased recruitment of higher order motor units can explain

an elevation in fast-twitch fiber force production in conjunction with Bozzo et al.s

findings.

4. Moore R.L., & Stull J.T. (1984). Myosin light chain phosphorylation

in fast and slow skeletal muscles in situ. American Journal of

Physiology, 247 (5 Pt 1): C462-71


Cameron Marzvaan
5/11/17
Engl 363
Dr. Bruce

Conclusion: Increased presence of kinase and decreased phosphatase activity in

fast-twitch muscle fibers, as opposed to slow-twitch fibers, contributes to the

greater extent of MLC2 phosphorylation.

Merit: In addition to confirming a relationship between twitch tension potentiation

and regulatory light chain phosphorylation, this paper showed that stimulating

afferent neural fibers increased action potential transmission across spinal cord

synaptic connections in animals. As such, this paper can be used to strengthen

Bozzo et al.s claims, as well as explain an increase in pre-synaptic potentials of

subsequent contractions.

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