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TFF-3 MODULATES RE-

SPONSIVENESS TO BRON-

CHODILATORS IN AIR-

WAYS 

Mira Yin 

 

✵ ABSTRACT 
Rhinovirus (RV) is the major cause of exacer-

bations, or worsening of symptoms, in asthmatic chil-
dren and adults. This often reduces the efficacy of 
therapeutic interventions such as bronchodilators — a 
type of medication used to promote airflow and alle-
viate asthma symptoms. The exact mechanisms 
through which RV exposure decreases responsive-
ness to bronchodilators remain unclear. Previous data 
demonstrates that airway cells release a specific sig-
nature of inflammatory mediators following RV expo-
sure. Other research has shown that Trefoil Factor 3 
(TFF-3), one of the mediators identified by our screen, 
regulates cell motility in other cell types. We show that 
RV exposure attenuates relaxation in both the airway 
and human airway smooth muscle (HASM). Given our 
data, we aim to examine whether or not TFF-3 attenu-
ates the relaxation of HASM and airways. 

Primary non-diseased human airway smooth 
muscle (HASM) was used to examine the conse-
quences of TFF-3 in modulating HASM and airway re-
laxation. Following RV-C15 exposure, it was found 
that the airway and HASM relaxation was attenuated. 
TFF-3 exposure also attenuated both airway and 
HASM relaxation. Additionally, TFF-3 exposure par-
tially weakened iso-induced reversal of carbachol-in-
duced phosphorylation of the myosin light chain. 
Within the cADDis Live Cell Assays, which provide 
real-time kinetic measurements of cyclic Adenosine 
Monophosphate (cAMP) production, TFF-3 attenu-
ated formoterol-induced cAMP production. Research-
ing how bronchodilation pathways change following 
RV infection can lead to the development of effective 
treatments and pharmaceutical solutions to alleviate 

worsening asthma symptoms during a viral exacerba-
tion of the disease. 

 

1 INTRODUCTION 
Rhinovirus, or RV, is the major cause of ex-

acerbations in asthmatic children and adults and can 
lead to reduced efficacy of therapies for symptomatic 
relief. Previous research has found that RV produces 
unique effects on asthmatics in comparison to other 
viral infections, causing increased symptom severity 
and stronger effects on treatment response (Reddel et 
al. 2011). Another study revealed that bronchodilator 
treatments have reduced efficacy in both adult and 
pediatric patients once exposed to RV (James & Col-
lins 2012). Although the mechanisms of RV induced 
asthmatic exacerbations are well-studied, research 
has yet to uncover exactly how RV may affect treat-
ment efficacy.  

 

 
Figure 1: Proposed Trefoil Factor-3 Cell Signaling 
Pathway  
The proposed pathway for when TFF-3 is released 
into the body post-infection with rhinovirus, activat-
ing  cell receptors as a response. 

 
We identified one of the mediators released 

following RV infection of airway epithelial cells as Tre-
foil Factor 3 (TFF-3). TFF-3 exhibits various properties, 
including forming dimers which interact with other pro-
teins and aid in signaling within the body (Weste et al. 
2022). Research has demonstrated that TFF-3 plays a 
role in the wound healing response and has estab-
lished functions in mucosal cells in the gastrointestinal 



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tract, specifically aiding in their repair and regenera-
tion post-damage (Braga et al. 2020) through en-
hanced cell migration and anti-apoptotic effects (Fan 
et al. 2023). Given that TFF-3 engages in reparative re-
sponses, it likely plays a similar role within the airways 
following RV exposure. Our findings suggest that TFF-
3 is present in a post-RV stimulation of primary human 
airway epithelial cells and intact in human lung slices. 
Figure 1 depicts a proposed signaling pathway by 
which TFF-3 can modulate airway function. As shown, 
the Human Airway Epithelial Cell (HAEC) releases lig-
and TFF-3 post-exposure to RV, which activates Prote-
ase-Activated Receptor-2 (PAR2) and/or C-X-C Motif 
Chemokine Receptor 4 (CXCR4) cell receptors on the 
human airway smooth muscle (HASM). Previous studies 
have established a connection between PAR2 and both 
inflammation and inflammatory diseases (Kennedy et 
al. 2020), while CXCR4 is related to tissue regeneration 
and cell proliferation. This in turn leads to the inhibition 
of alpha s, which is linked to the G protein and adenylyl 
cyclase (AC), decreasing cAMP production and airway 
relaxation. (Bianchi & Mezzapelle 2020). 

 

2 MATERIALS AND METHODS 

 
Figure 2: Human Airway Smooth Muscle Analysis 
Methods (Left) Cells cultured on both sides of the 
transwell insert until confluency reached (Top Right) 
Western Blotting (Bottom Right) cAMP assay work-
flow. 

 
This study utilized primary HASM cells to con-

duct the various procedures seen in Figure 2. We ob-
tained human lung tissue samples from the National 
Disease Research Interchange (NDRI) and from the In-
ternational Institute for the Advancement of Medicine 
(IIAM). Primary HASM cell lines originated from the 

trachea of both healthy, non-asthmatic donors with no 
history of chronic diseases or smoking, and from dis-
eased, aborted-transplant human lung donors. Cells 
were cultured in F-12 medium supplemented with 10% 
Fetal Bovine Serum (FBS) to encourage growth, along 
with 100 U/mL penicillin, 0.1 mg/ml streptomycin, and 
0.1% Primocin from Invitrogen to prevent contamina-
tion. To split the cell lines, we washed the cells with 
phosphate buffered saline (PBS) and aspirated the solu-
tion. Then, we added the enzyme 0.05% 1X Trypsin-
EDTA (Gibco) to detach and release the cells from the 
bottom of the plates or flasks. Later in the procedure, we 
added in feeding media to prevent the trypsin from lys-
ing the cells and causing complete damage.  

The experiment utilized the HASM cells in 
subculture during passages 1–5, as these cells retain 
the expression of native contractile protein. HAEC was 
derived from the same tracheas as the HASM cells. 
Cells were on transwell inserts from Corning and were 
fed on both the upper and lower side of the insert with 
Pneumacult Ex Basal Media from StemCell Technolo-
gies until they reached the appropriate level of con-
fluency. The cells then underwent air-liquid interface 
(ALI) differentiation for 21 days prior to stimulation 
and were fed with Pneumacult ALI Media. We fed and 
maintained cell lines by routinely replacing media in 
order to prevent the cells from drying out.  

  

 
Figure 3: Western Blotting Media Treatments 

 
HASM underwent treatment to test the effects of 

TFF-3 on protein modifications that are surrogates for 
bronchodilation/relaxation. The cells grew to conflu-
ence until the desired percentage of cells covered the 
surface of the plate, then were serum starved with stock 
media 24-74 hours before treatment. This Western blot 



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utilized four different cell donor lines, with cells receiv-
ing a treatment of 0.15μM and 1.5μM of TFF-3 48 hours 
before short-time point treatments. After the 48-hour 
period, specific wells then received a treatment of either 
carbachol (carbamoyl choline - Cch) solution at 20μM 
for 10 minutes, a bronchodilator known as isoprenaline 
hydrochloride/isoproterenol (Iso) at 1μM for 5 minutes, 
or both (Figure 3). Sigma Aldrich (St. Louis, MO) sup-
plied Carbachol (Cch), Iso, and perchloric acid. RNA 
transfection produced Rhinovirus C15, followed by a 
RNase A treatment of clarified lysates and ultracentrifu-
gation through a 30% sucrose cushion to purify the vi-
rus. Cell Signaling Technologies supplied Radio-Im-
munoprecipitation Assay (RIPA) buffer, utilized to lyse 
the cells. A quick addition of stop buffer (perchloric 
acid) then halted intracellular signaling, followed by ly-
sate collection for Western blotting. 

After collection, lysate either underwent soni-
cation or freezing to break the cell membranes and 
release the contents, followed by a heating process at 
70°C for 10 minutes to denature the samples. The 
samples then underwent centrifugation at 14000 rpm 
for 5 minutes. Using a micropipette, we added 3uL of 
the latter, 15uL of the samples, and 5uL of the sample 
buffer into 15 4-12% Bis-Tris polyacrylamide gel wells. 
After running the gels, iBlot facilitated the transfer of 
samples onto the membrane for staining with anti-
bodies against phosphorylated myosin light chain 
(pMLC) and total myosin light chain (MLC) to compare 
the fold change of expression between the two. Anti-
bodies for detection of pMLC came from Cell Signal-
ing Technologies. EMD Millipore supplied the MLC 
antibodies. We then used ImageStudio to visualize 
membranes and analyze band intensities. 

 

 
Figure 4:  Generation and Measurement of Human 
Precision Cut Lung Slices  
(Top) Method shown in images depicting how 
hPCLS are generated from human lung samples.  
(Bottom) hPCLS are then measured to measure con-
traction (when Cch stimulated) and relaxation (when 
Iso stimulated). 

 
Human precision cut lung slices (hPCLS) 

shown in the top section of Figure 4 originated from 
the lungs of diseased or non-diseased patients and re-
ceived an injection of 2% low melting agarose into the 
bronchi and branched airways to inflate them. After 
the agarose set in ice, we sectioned the lung lobes 
and isolated the airways into 8mm diameter cores us-
ing the coring tool and sliced at a thickness of 350μm 
using the Precisionary Instruments VF300 Vibratome. 
The best intact airways provided samples for PCLS as-
says and separate measurements for contraction and 
relaxation as shown in the bottom of Figure 4. Any 
other airway slices contributed to supernatant experi-
ments.  

Muscle relaxation was tracked by measuring 
cAMP production. To measure the total cellular cAMP 
production in cell lysates, we plated sub-confluent 
HASM cells and allowed them to grow to ~80% conflu-
ence using cAMP assays purchased from the Applied Bi-
osystems cAMP-Screen Immunoassay System, adhering 
to the manufacturer provided instructions. After aspirat-
ing the media, we replaced it with conditioned media 
from a control buffer or with RV-C15 stimulated 



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epithelial cells for 48 hours prior to stimulation with iso-
proterenol. The cells underwent lysis and were incu-
bated for 30 minutes at 37°C. We then added Conju-
gate Dilution Buffer, cAMP-AP Conjugate, anti-cAMP 
antibody, and the samples to a pre-coated assay plate 
to incubate for 1 hour on a plate shaker. After a 30 mi-
nute incubation period with CSPD®/Sapphire-II RTU 
Substrate, a luminometer measured light emission from 
the plates. We derived data from standard curves and 
reported cAMP levels following standard dilutions. 

When performed with the cell lines, the cAD-
Dis Live Cell Assays detected Gs protein activation, 
which when stimulated produces cAMP. This allowed 
for the determination of TFF-3’s effect on this signal. 
This assay was able to measure cAMP production in 
real time, showcasing the response kinetics with 
greater dimming and indicating a higher cAMP con-
centration in the cells.  

On Day 0, cells underwent preparation for 
transduction and seeding. We decanted T75 contain-
ing confluent HASMCs by removing the media within 
the flask, and then we washed the cells with 1X PBS 
(Gibco). We then trypsinized the cells to release them 
from the bottom of the flask and isolated them for 
plating in F12 feeding medium supplemented with 
10% FBS and Primocin (Gibco). We counted the cells 
in suspension using a hemocytometer and 0.4% Try-
pan Blue (Gibco). Cell density varied per experimental 
target. Cells were plated in a 96 well black-walled tis-
sue culture treated assay plate (Corning COSTAR). 
The cells grew and proliferated for two days until 
transduction.  

To perform the transduction, we supple-
mented the media with a combination of the cADDis 
Green Down cAMP Sensor Assay (Montana Molecular) 
and Trichostatin A (Sigma). The cells incubated for an-
other two days until imaging. We took images once 
per second using an inverted fluorescent microscope 
to compile a cohesive TIFF file that can later undergo 
analysis using Python for image analysis and Prism for 
generating time course curves. One minute into the 
sequence, we used formoterol fumarate dihydrate 
(Sigma) to invoke the cAMP response, leading to a 
downward shift in green fluorescence. 
 
 

3 RESULTS 

 
Figure 5: TFF-3 Stimulation of HASM Partially Atten-

uates Isoproterenol-Induced Reversal of Carbachol-
Induced Phosphorylation of Myosin Light Chain 
(pMLC) 

HASM were stimulated with TFF-3, and then with Cch 
± Iso, lysates collected for Western blot analysis. (Left) 
Immunoblot of pMLC and MLC from n=1 donor cell 
line (Right) Band density measurements of pMLC nor-
malized to MLC, n=4 distinct donors 

 
Figure 5 depicts a representative immunoblot from 

one of the four cell lines utilized within the experi-
ments. The red shows the total MLC and the green 
shows the phosphorylated MLC. The group mean 
data from Figure 5 shows the average fold change be-
tween the four cell lines used in the experiments, indi-
cating minimal change in the pMLC signal in the Cch 
+ TFF-3 treatment. Compared to the Cch + Iso treat-
ment, addition of the highest concentration of TFF-3 
(1.5μM) appeared to slightly attenuate the ability of 
Iso to reduce Cch-induced pMLC expression. 

 



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Figure 6: RV Stimulation Attenuates Formoterol 
(Form)-Induced Airway/HASM Relaxation 
(Left) hPCLS stimulated with RV and airway relaxation 
measured to form dose responses. n=10-18 distinct 
donors, *p < 0.05 (Right) HASM stimulated with media 
from control or RV exposed epithelial cells, then stim-
ulated with form – cAMP production assessed by 
ELISA. n=7 distinct donors, *p < 0.05 

 

 
Figure 7: TFF-3 Stimulation Attenuates Formoterol-In-
duced Airway/HASM Relaxation 
(Left) hPCLS stimulated with TFF-3 and airway relaxa-
tion measured to formoterol dose responses. n=4 dis-
tinct donors, *p < 0.05 (Right) HASM stimulated TFF-3, 
then stimulated with formoterol – cAMP production as-
sessed by ELISA. n=5 distinct donors, *p < 0.05 
 

Figures 6 and 7 depict results from the PCLS 
assays, graphing the percentage of bronchodilation 
while comparing the control to treatments with either 
RV or TFF-3 at varying concentrations. Both RV-C15 
and TFF-3 treatments of PCLS attenuated formoterol-
induced airway relaxation. These figures also depict 
cAMP assay results, showing that both RV and TFF-3 
exposure attenuates cAMP production by formoterol. 

 

 
Figure 8: cADDis assay to measure cAMP in live cells 
HASM cells received treatment with TFF-3 in varying 

concentrations, and cADDis assay measured the ef-
fects in expression when exposed to formoterol and/or 
carbochol. 

 
In addition to the ELISA-based cAMP assays, we per-

formed cADDis assays which measured the effect of 
TFF-3 treatment (24 hour pre-treatment) in the pres-
ence and absence of Cch (20 µM, 15 minutes pre-
treatment). TFF-3 pre-treatment appears to attenuate 
formoterol-induced cAMP production, which further 
decreases with co-stimulation from Cch (Figure 8). 

 

4 DISCUSSION 
TFF-3 is known to for its ability to form trimers, which 

can enhance its role in signaling. Generally, it is rec-
ognized for promoting epithelial cell health in the gas-
trointestinal tract and assisting with epithelial repair 
during wound healing by reducing cell death through 
the activation of multiple receptors. However, it re-
mains unclear whether TFF-3 affects the biology of air-
way smooth muscle. Notably, TFF-3 release increased 
following stimulation of airway epithelial cells with RV-
C15. Since TFF-3 appears to be associated with RV 
stimulation of the airways, its release may lead to acti-
vation of one or more receptors. This potentially 
causes changes in the smooth muscle biology, result-
ing in decreased cAMP production and reduced air-
way relaxation. 

We used four different cell donor lines to analyze the 
Western blot results, providing a larger pool of data. 
The group mean fold change from the Western blot re-
sults reveals the overall effects of phosphorylation of 
MLC. This serves as a readout for muscle contraction 



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following exposure to Cch and Iso reversing the phos-
phorylation. The data shows that TFF-3 partially inhibits 
the Iso-dependent reversal of carbachol induced pMLC 
despite not augmenting carbachol-induced pMLC. It is 
possible that pMLC readout is not a sensitive enough to 
measure the effects of TFF-3 on airway smooth muscle 
relaxation. Hence, it is important to examine other tar-
gets involved in relaxation going forward. 

We used precision cut lung slices (PCLS) to 
assess changes in formoterol-induced relaxation fol-
lowing RV or TFF-3 exposure since formoterol is a 
mainstay bronchodilator used in asthma therapy. RV 
and TFF-3 was able to significantly reduce for-
moterol’s effectiveness in relaxing the airways. Treat-
ment with RV or TFF-3 at varying concentrations re-
sulted in significantly less bronchodilation in response 
to formoterol compared to the control buffer stimula-
tion. Future experiments are needed to determine 
whether RV-dependent attenuation of relaxation is 
TFF-3-dependent. 

Additionally, we used human airway smooth 
muscle to measure cAMP generation to indicate mus-
cle relaxation. Results demonstrated that exposure of 
airway smooth muscle to either media from RV-stimu-
lated epithelial cells or direct exposure to TFF-3 re-
duced cAMP production by formoterol show a de-
crease in the amount of cAMP generated by for-
moterol exposure. This indicates that the relaxation of 
muscles following RV or TFF-3 stimulation decreases 
bronchodilation and relaxation responses. The cAD-
Dis results show that TFF-3 stimulation decreases the 
responsiveness of airway smooth muscle to for-
moterol, which the addition of Cch augments. These 
results suggest that TFF-3 may increase an inhibitory 
signal that Cch treatment enhances, however addi-
tional confirmation would be needed. 

A major limitation of this study is the lack of 
understanding regarding how TFF-3 can elicit these 
types of responses. The specific mechanisms by which 
RV decreases responsiveness to bronchodilators and 
the receptors to which RV binds remain unclear. There 
are gaps in understanding how TFF-3, primarily recog-
nized as a mediator in the gastrointestinal tract, modu-
lates bronchodilation in HASM within the lungs. In future 
research related to TFF-3 and RV’s effects on asthmatic 
exacerbations, N numbers can be expanded to address 

response heterogeneity and further support these find-
ings. Although animal models may be a valid choice for 
experimentation, observations reveal that mouse mod-
els have not demonstrated TFF-3 expression or respon-
siveness to bronchodilators in the same way that human 
airways do, which may limit the effectiveness of this 
model. 

 

5 CONCLUSION 
In conclusion, the data identifies potential 

therapeutic targets that researchers can modulate to 
decrease the effects of RV on asthma exacerbations. 
Western blot results indicated that the highest con-
centration of TFF-3 attenuated the ability of the Iso 
bronchodilator to reduce Cch-induced pMLC expres-
sion. PCLS Assays visually demonstrate the tissue’s 
ability to attenuate cAMP production when treated 
with RV and TFF-3. The cADDis assay results show that 
TFF-3 stimulation reduces the airway’s responsiveness 
to bronchodilators, which in turn the addition of Cch 
can enhance. Gaining a better understanding of how 
TFF-3 signaling pathways alter bronchomotor tone 
will improve the efficacy of current treatments within 
the asthma therapeutic area. Our data suggests that 
TFF-3 may function as an inhibitory molecule that 
could serve as a novel therapeutic target to prevent 
bronchodilator hyporesponsiveness. These results of-
fer hope for improving the current bronchodilators for 
those exposed to RV and for developing new thera-
peutics to treat RV-dependent asthma exacerbations. 
Further studies would need to be conducted to deter-
mine the exact mechanisms by which TFF-3 attenuates 
these responses.  

 

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Mira Yin graduated in 2023 from Rutgers University New Bruns-
wick School of Engineering and the Honors College with a B.S. in 
Biomedical Engineering with a minor in Biology. Mira worked as 
an undergraduate researcher in Dr. Cynthia Koziol-White’s lab 
within the Rutgers Institute for Translational Medicine and Science 
(RITMS) first through the Aresty Research Assistant program, and 
then continued her research post-program for an additional year. 
Her work focuses on understanding the signaling pathways tar-
geted during viral infection, more specifically those that modulate 
airway tone. Outside of research, Mira was also a School of Engi-
neering (SOE) Ambassador, President of the Habitat for Humanity 
organization, and Alumni Relations Chair for the Society of 
Women Engineers (SWE). Currently, Mira works at Merck & Co. 
within Global Clinical Trial Operations (GCTO), and is pursuing 
her M.S. in Clinical Research Management (CRM) in the Drug 
Safety and Pharmacovigilance track at Rutgers University.  

 
Mira can be contacted at mcy28@rutgers.edu. 

                                                                                                                                                                                           

mailto:mcy28@rutgers.edu.

