Basic Science Physiology

Physiology of Muscles

Physiology of Muscles

What You'll Learn

  • Sarcomere anatomy — A-band (dark, myosin), I-band (light, actin only), H-zone (myosin only), Z-line (sarcomere boundary), M-line (center)
  • Excitation-contraction coupling — AP → T-tubule → DHP receptor → RyR → Ca²⁺ release → troponin C binding → cross-bridge cycling
  • Fiber types — Type I (slow, oxidative, red, fatigue-resistant) vs Type II (fast, glycolytic, white, fatigable)
  • Motor unit — Henneman size principle: small motor neurons recruited first
  • Metabolic myopathies — McArdle (myophosphorylase, second wind), Pompe (acid maltase, respiratory failure), CPT II (recurrent rhabdomyolysis)
  • Myopathic vs neuropathic patterns — proximal vs distal weakness, EMG and biopsy distinctions
  • Key dystrophies — DMD/BMD (dystrophin), DM1 vs DM2, FSHD, LGMD
  • Biopsy patterns — ragged red fibers (mito), rimmed vacuoles (IBM), perifascicular atrophy (DM), fiber type grouping (reinnervation)
HighYield Pearls
  • A-band stays constant: During contraction the I-band & H-zone shorten as Z-lines approach — the A-band length is unchanged. Single most-tested sarcomere fact.
  • DHPR ↔ RYR1 mechanical coupling: Skeletal EC coupling does NOT require extracellular Ca²⁺ influx — T-tubule DHPR (voltage sensor) directly opens RYR1 on SR. Cardiac (RYR2) uses Ca-induced Ca release.
  • Rigor mortis = no ATP: Myosin needs ATP to DETACH from actin (not to bind). Loss of ATP after death locks cross-bridges.
  • Henneman size principle: Smallest (Type I, low-threshold) motor units recruited first; largest (Type IIx/b) last as force demand ↑.
  • Malignant hyperthermia: RYR1 (or CACNA1S) gain-of-function + volatile anesthetic / succinylcholine → masseter spasm, hyperthermia, rhabdo, hyperkalemia. Treat with dantrolene + cooling.
  • Type II atrophy = disuse / steroid / endocrine: Steroid myopathy, Cushing, hyperthyroid, paraneoplastic & disuse selectively atrophy Type II fibers (proximal, painless, normal CK).
  • Fiber type grouping = reinnervation: Loss of normal mosaic checkerboard on ATPase stain = chronic neurogenic process (axonal sprouting from surviving motor neurons).
  • Metabolic myopathy red flags: Exercise-induced cramps + myoglobinuria → think McArdle (PYGM, “second wind”), CPT-II (long exercise/fasting, adult rhabdo), or MH-spectrum (RYR1).
  • Neonatal AChR γ → ε switch: Fetal γ-subunit replaced by adult ε-subunit perinatally — relevant to slow-channel/fast-channel congenital myasthenic syndromes.
  • Dystroglycan complex links cytoskeleton to ECM: Dystrophin → β-dystroglycan → α-dystroglycan → laminin. Disruption → DMD/BMD, LGMD, dystroglycanopathies (Walker-Warburg, MEB, FCMD).
🔍 Quick ReferenceStructure / EC coupling · Fiber types / metabolism · Disease / drug
Structure / EC coupling
  • Z-line α-actininanchors thin (actin) filaments — sarcomere boundary
  • M-line myomesinanchors thick (myosin) filaments at sarcomere center
  • A-band unchanged, I/H shrinksliding filament theory (contraction)
  • Troponin C binds Ca²⁺tropomyosin shift → exposes actin myosin-binding sites
  • DHPR (CACNA1S, L-type)T-tubule voltage sensor mechanically gates RYR1
  • RYR1 on SRCa²⁺ release channel for skeletal EC coupling (RYR2 = cardiac)
  • SERCA + phospholambanpumps Ca²⁺ back into SR (relaxation)
  • Myosin ATPasepowers cross-bridge cycle; ATP needed to DETACH (rigor if absent)
Fiber types / metabolism
  • Type I — slow oxidative, redhigh myoglobin/mitochondria, fatigue-resistant, postural, MyHC-I
  • Type IIa — fast oxidative-glycolytic, pinkmoderate fatigue, MyHC-IIa
  • Type IIx/IIb — fast glycolytic, whiteanaerobic, high force, rapid fatigue, sprinting
  • ATPase pH 9.4 darkType II (reversed at pH 4.3 → Type I dark)
  • SDH / NADH-TR darkType I (mitochondria-rich) on oxidative stains
  • Henneman size principlesmall motor units recruited first; rate coding modulates force
  • Creatine phosphate & creatine kinaseimmediate ATP buffer (first ~10 sec)
  • Carnitine palmitoyl shuttleimports long-chain fatty acyl-CoA into mitochondria for β-oxidation
  • Satellite cells (Pax7+)quiescent muscle stem cells under basal lamina; MyoD activation → regeneration
Disease / drug association
  • Malignant hyperthermiaRYR1 / CACNA1S + volatiles / succinylcholine → dantrolene
  • Central core diseaseRYR1 congenital myopathy + MH susceptibility
  • Caffeine-halothane contracture testgold-standard MH susceptibility screen
  • McArdle diseasePYGM (myophosphorylase) deficiency, “second wind” phenomenon, flat lactate on ischemic forearm test
  • CPT-II deficiency (adult)exercise/fasting-induced rhabdomyolysis & myoglobinuria
  • Rhabdomyolysis labsCK ≥ 5× ULN, myoglobinuria, hyperK, hyperphos, HYPOcalcemia, AKI, ↑ uric acid
  • Ragged-red & COX-negative fibersmitochondrial myopathy (oxidative phosphorylation failure)
  • Fiber type grouping + angulated fiberschronic neurogenic reinnervation
  • Selective Type II atrophysteroid / disuse / thyrotoxic / Cushing / paraneoplastic myopathy
  • Dystrophin / dystroglycan / sarcoglycan lossDMD & BMD / dystroglycanopathy / LGMD
  • Neonatal γ → ε AChR subunit switchrelevant to congenital myasthenic syndromes (slow/fast channel)
Muscle Fiber Structure

Sarcomere Anatomy

The sarcomere is the basic contractile unit, bounded by two Z-lines.

Structure Location Composition Board-Relevant Detail
A-band Center of sarcomere Thick (myosin) +/- overlapping thin filaments Does NOT change length during contraction (Anisotropic, dArk). Memory aid: A-band = Always the same length — the single most tested sarcomere fact.
I-band Between A-bands of adjacent sarcomeres Thin filaments only (actin) Shortens during contraction (Isotropic, lIght)
H-zone Center of A-band Myosin only (no actin overlap) Shortens during contraction; disappears at full contraction
Z-line (Z-disc) Sarcomere boundary Alpha-actinin anchors actin Defines sarcomere; Z-to-Z = one sarcomere
M-line Center of H-zone Myomesin; anchors myosin Middle of sarcomere
Board Pearl

During contraction, the A-band stays the same length. The I-band and H-zone shorten as actin slides over myosin (sliding filament theory). This is the most commonly tested sarcomere fact.

Thick vs Thin Filaments

Filament Main Protein Associated Proteins Function
Thick Myosin (heavy chains) Myosin light chains; titin spans Z-line to M-line (third filament system); provides passive elasticity, anchors thick filament, mechanosensing. (Largest known protein.) Cross-bridge formation; ATPase activity in myosin head
Thin Actin (F-actin polymer) Tropomyosin, Troponin complex (T, C, I) Troponin C binds Ca²⁺ → tropomyosin shifts → exposes myosin-binding site

Troponin Subunits

  • Troponin C — binds Calcium (the Ca²⁺ sensor)
  • Troponin T — binds Tropomyosin (attaches complex to thin filament)
  • Troponin I — Inhibits actin-myosin interaction (holds tropomyosin in blocking position)

T-Tubules and Sarcoplasmic Reticulum

  • T-tubules (transverse tubules) — invaginations of the sarcolemma that carry the action potential deep into the muscle fiber
  • Sarcoplasmic reticulum (SR) — intracellular Ca²⁺ store; terminal cisternae flank T-tubules forming the triad
  • Triad = 1 T-tubule + 2 terminal cisternae (located at the A-I band junction in skeletal muscle)
  • DHP receptor (dihydropyridine receptor) — voltage sensor on T-tubule membrane
  • RyR1 (ryanodine receptor) — Ca²⁺ release channel on SR; mechanically coupled to DHP receptor in skeletal muscle
Board Pearl

Malignant hyperthermia results from a mutation in the RyR1 gene (less commonly CACNA1S, DHPR α1 subunit) → uncontrolled Ca²⁺ release from SR → sustained contraction, hyperthermia, rhabdomyolysis. Triggered by volatile anesthetics and succinylcholine. Treat with dantrolene (blocks RyR1).

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