A hypothesis note that reframes post-exertional malaise (PEM) as a shear-activated failure state
emerging from baseline membrane control-surface instability, impaired resolution (ER stress / phosphatase efficacy), and mistimed nitric-oxide signaling.
Post-exertional malaise (PEM) is the defining clinical feature of myalgic encephalomyelitis /
chronic fatigue syndrome (ME/CFS), yet its triggering mechanism remains poorly explained by models
focused solely on exertion load, inflammation, or mitochondrial insufficiency.
PEM is notable not for the magnitude of stress required to provoke it, but for the fact that
ordinary physiological demands—such as standing, walking, or cognitive effort—can be sufficient
to initiate delayed, multi-system dysfunction.
This document reframes post-exertional malaise (PEM) as a shear-activated failure state.
Rather than viewing PEM as a consequence of exertion, inflammation, or mitochondrial weakness alone,
the core claim is that baseline membrane and endothelial instability renders otherwise-normal shear forces injurious.
Everyday physiological demands (standing, walking, heat, cognitive load) then become sufficient to trigger a delayed multi-system collapse.
Key framing: PEM is not “caused by exertion itself.” Exertion is a stress test. The injury is the system’s
inability to absorb and resolve flow stress when membrane control and signal termination are fragile.
Figure A — Overview: shear-activated failure state (5-box flow)
Figure A. Conceptual overview: baseline resolution failure (membrane + ER) destabilizes the control surface,
SMPDL3B failure mode determines phenotype dynamics, and normal shear exposures drive downstream execution strain and clinical PEM.
Section 1 — The baseline abnormalities (the vulnerable state)
At baseline, ME/CFS is modeled here as instability of the phospholipid “control surface” of immune and endothelial cells.
Phospholipids are not passive building blocks — they determine where receptors sit, how long signals persist,
and whether a cell can turn off cleanly after activation.
Impaired organization of lipid rafts
Reduced receptor clustering and internalization
Prolonged receptor residency at the membrane
Loss of coordinated signal termination
Interpretation: signals may start normally, but fail to shut off cleanly.
Figure B — The membrane “control surface”: why signals fail to shut off cleanly
Figure B. Conceptual “control surface” schematic. Stable lipid-raft organization supports receptor clustering and timely internalization,
allowing signals to terminate cleanly. In membrane-unstable states, raft fragmentation increases receptor residency time and impairs coordinated termination,
enabling persistent signaling without requiring high cytokine output.
1.2 SMPDL3B-related loss of membrane control capacity
SMPDL3B sits at a critical point in phospholipid biology and raft stability. In this framework it is treated as a
membrane stability / signal-gain governor that influences multiple receptor platforms (TLR/IFN, insulin signaling, endothelial shear platforms).
Dampens innate immune signal gain (reduces over-responsiveness)
Shedding phenotype
Defensive PI-PLC activation
Episodic loss of anchoring
Oscillatory instability (flares)
Deficient phenotype
Chronically fragile rafts
Low recovery bandwidth
Persistent signal residency
Figure C — SMPDL3B as a membrane stability / signal-gain governor (two failure modes)
Figure C. SMPDL3B is treated as a membrane stability and signal-gain governor.
Loss of SMPDL3B control can express as (left) episodic defensive shedding with oscillatory instability,
or (right) chronic deficiency with fragile rafts and persistent signal residency.
1.3 ER stress & impaired resolution machinery (signal-duration failure)
ER stress compounds membrane instability by slowing the “reset machinery”:
receptor recycling, protein folding/turnover, and the post-activation return to baseline architecture.
In this model, the outcome is signal-duration failure rather than cytokine excess.
Endothelial cells normally convert shear stress into adaptive vasodilation via raft-anchored eNOS signaling.
In membrane-unstable states, eNOS becomes mislocalized and its regulators stop lining up in time:
Cav-1 braking and Ca²⁺ activation desynchronize.
Crucial point: NO is not necessarily absent — it is mistimed and misplaced.
That means baseline microvascular control is fragile: small flow changes are no longer buffered smoothly.
Figure D. Mechanistic “zoom” of shear buffering. In healthy endothelium, lipid-raft/caveolae organization anchors eNOS in the
shear-sensing neighborhood so Cav-1 braking and Ca²⁺ activation align, producing a localized NO pulse that smooths flow. In membrane-instability states,
raft/caveolae disorganization leads to eNOS mislocalization, desynchronized regulation, and mistimed/patchy NO signaling—allowing shear to become focal,
spiky, and mechanically/oxidatively stressful downstream. :contentReference[oaicite:1]{index=1}
1.5 Glycocalyx & heparan sulfate: the shear–timing interface
The endothelial glycocalyx—particularly heparan sulfate (HS) proteoglycans—functions as a
dynamic shear-sensing and signal-timing interface rather than a passive structural coating.
HS participates directly in converting mechanical shear into spatially and temporally precise
endothelial signaling.
In this framework, HS dysfunction in ME/CFS is modeled as a secondary consequence of membrane
control-surface instability rather than a primary structural loss. SMPDL3B-related lipid-raft
disorganization disrupts caveolae geometry and receptor microdomains, increasing mechanical strain
on HS proteoglycans and altering their surface residency and sulfation patterning.
Patchy or poorly patterned HS impairs spatial averaging of shear forces, causing local over- or
under-sensing. This directly contributes to mislocalized and mistimed eNOS activation,
as caveolin-1 braking and Ca²⁺ activation no longer align within stable microdomains.
Key clarification: nitric oxide is not necessarily deficient in ME/CFS.
Rather, NO signaling becomes mistimed and spatially incoherent, converting
otherwise-normal shear into focal mechanical and oxidative stress.
Interpretation: glycocalyx disruption reflects a reversible control-layer failure driven by membrane
instability and impaired signal termination, not fixed endothelial damage.
Heparan sulfate (HS) as the shear–timing interface linking SMPDL3B instability to eNOS mis-timing
Figure — HS as the shear–timing interface.
In ME/CFS, SMPDL3B-related membrane instability disrupts HS residency and patterning,
degrading spatial averaging of shear and producing mislocalized, mistimed eNOS activation.
The result is heterogeneous microvascular flow and delayed shear injury rather than global NO deficiency.
Section 2 — Shear stress as the activator (the stress test)
2.1 What shear stress normally is
Shear stress is the frictional force of blood flow across the endothelial surface.
In healthy physiology, shear is sensed by the glycocalyx and raft-anchored mechanosensors,
triggering precisely timed NO release. In that state, shear is information, not damage.
2.2 What changes in ME/CFS (activator meets vulnerability)
When baseline membrane organization, ER resolution, and NO timing are unstable:
Shear sensing becomes inaccurate
Vasodilation timing becomes “off”
Capillary flow becomes heterogeneous
This converts normal demands into focal mechanical strain — local velocity spikes, narrowed flow segments,
and higher-impact deformation events. Shear becomes the activator that exposes baseline vulnerability.
Figure E — Shear stress as the activator: “information” (buffered) vs “strain” (focal spikes)
Figure E. Shear stress is the frictional force of blood flow across the endothelium. In healthy physiology it is sensed by the glycocalyx
and raft-anchored mechanosensors, producing precisely timed NO release and smooth capillary transit. When membrane/ER resolution and NO timing are unstable,
shear sensing becomes inaccurate and flow becomes heterogeneous, producing focal velocity spikes and narrowed segments that act as a mechanical “stress test”
exposing baseline vulnerability. :contentReference[oaicite:1]{index=1}
Red blood cells (RBCs) are designed to deform, but only within limits. They also cannot repair membranes.
Under pathological shear, RBCs can undergo excessive deformation and membrane stress, producing:
Membrane lipid peroxidation
Microvesicle shedding
Subclinical hemoglobin leakage
This can coexist with “normal” baseline labs while still producing post-load worsening and delayed symptom peaks.
3.2 Microclots as secondary amplifiers (not the initiator)
Endothelial instability plus abnormal flow can promote a “stickier” microvascular environment and abnormal fibrin behavior.
Microclots preferentially form in low-flow microregions, persist longer than normal, and further increase local shear.
Interpretation: microclots can strongly amplify PEM dynamics, but in this document they are treated as secondary amplifiers, not the initiating lesion.
Figure G — Microclots amplify shear heterogeneity (secondary amplifier)
Figure G. Microclots are treated here as secondary amplifiers: fibrin-rich “islands” form in low-flow microregions,
narrowing channels and forcing the same flow through smaller gaps. This produces local velocity spikes and higher focal shear, which can increase RBC deformation
and worsen downstream post-load dynamics.
Haptoglobin (Hp) acts as a buffering layer that clears free hemoglobin released into plasma during RBC stress.
Hp phenotypes do not “cause” ME/CFS, but can influence crash severity and recovery time under identical stressors
by changing how well the system absorbs heme/hemoglobin-related oxidative load.
Figure H — Hp phenotypes as “shock absorbers” for red blood cell stress
Same shear / RBC stress event, different buffering capacity: Hp 1-1 (strong), Hp 2-1 (moderate/variable), Hp 2-2 (weaker).
Hp does not cause ME/CFS; it shifts how hard crashes hit once free hemoglobin enters plasma.
Concept: identical shear-driven RBC stress can yield different symptom impact depending on hemoglobin buffering efficiency.
Section 4 — Clean synthesis (the core claim)
Baseline state: membrane/raft instability + ER-resolution weakness → signals linger and endothelial control is fragile.
Activator: normal shear stress from standing or exertion becomes injurious because buffering (NO timing) is unreliable.
One-panel summary of the document’s claim: PEM reflects shear-activated failure when membrane control and signal termination are fragile.
Hp phenotype does not initiate disease — it shifts how hard the same event lands.
Figure I. Baseline membrane/raft instability plus ER-resolution weakness makes endothelial flow control fragile.
Normal shear then becomes a stress test that produces RBC stress and microvascular injury; microclots amplify shear heterogeneity.
Buffering layers (e.g., Hp phenotype) shift crash threshold and recovery time.
One-sentence takeaway
One-sentence takeaway:
PEM is not caused by exertion itself, but by the failure of membrane-mediated flow control to absorb shear stress during recovery.
The following documents define the conceptual and methodological framework used to interpret
genetic signals and physiological mechanisms in this paper. They establish layer boundaries, phenotype discipline,
and phase dependence within the GLA system.
These materials are provided for transparency and interpretive context.
They are not cited as evidentiary sources and should be read as evolving systems-biology models.