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Sieck, Gary C.

https://orcid.org/0000-0003-3040-9424

Mayo Clinic

Mayo Clinic

Citations 422

Response to letter by Dr. Marc Hershenson (exposure of airway smooth muscle cells to cigarette smoke extract)
Aravamudan, Bharathi, Delmotte, Philippe , Vassallo, Robert , Sieck, Gary C. , Prakash, Y. S. , Thompson, Michael D. , Pabelick, Christina M. , Prakash, Y S , Sieck, Gary , Vassallo, Robert

American Journal of Physiology-Lung Cellular and Molecular Physiology | August 15, 2014 | Volume: 307 | Issue: 4 | Pages: L346-L346

10.1152/ajplung.00194.2014 Get It

Localized Delivery of Brain-Derived Neurotrophic Factor-Expressing Mesenchymal Stem Cells Enhances Functional Recovery following Cervical Spinal Cord Injury
Gransee, Heather M. , Zhan, Wen-Zhi, Sieck, Gary C. , Mantilla, Carlos B. , Zhan, Wen‐Zhi, Sieck, Gary , Gransee, Heather M , Mantilla, Carlos B

Journal of Neurotrauma | August 5, 2014 | Volume: 32 | Issue: 3 | Pages: 185-193

10.1089/neu.2014.3464 Get It

Cigarette smoke-induced mitochondrial fragmentation and dysfunction in human airway smooth muscle
Aravamudan, Bharathi, Kiel, Alexander , Freeman, Michelle, Delmotte, P. , Vassallo, Robert , Sieck, Gary C. , Prakash, Y. S. , Thompson, Michael James , Pabelick, Christina M. , Prakash, Y S , Sieck, Gary , Vassallo, Robert , Kiel, Alexander M

American Journal of Physiology-Lung Cellular and Molecular Physiology | March 8, 2014 | Volume: 306 | Issue: 9 | Pages: L840-L854

10.1152/ajplung.00155.2013 Get It

The balance between mitochondrial fission and fusion is crucial for mitochondria to perform its normal cellular functions. We hypothesized that cigarette smoke (CS) disrupts this balance and enhances mitochondrial dysfunction in the airway. In nonasthmatic human airway smooth muscle (ASM) cells, CS extract (CSE) induced mitochondrial fragmentation and damages their networked morphology in a concentration-dependent fashion, via increased expression of mitochondrial fission protein dynamin-related protein 1 (Drp1) and decreased fusion protein mitofusin (Mfn) 2. CSE effects on Drp1 vs. Mfn2 and mitochondrial network morphology involved reactive oxygen species (ROS), activation of extracellular signal-regulated kinase (ERK), phosphatidylinositol 3-kinase (PI3K)/protein kinase B (Akt), protein kinase C (PKC) and proteasome pathways, as well as transcriptional regulation via factors such as NF-κB and nuclear erythroid 2-related factor 2. Inhibiting Drp1 prevented CSE effects on mitochondrial networks and ROS generation, whereas blocking Mfn2 had the opposite, detrimental effect. In ASM from asmatic patients, mitochondria exhibited substantial morphological defects at baseline and showed increased Drp1 but decreased Mfn2 expression, with exacerbating effects of CSE. Overall, these results highlight the importance of mitochondrial networks and their regulation in the context of cellular changes induced by insults such as inflammation (as in asthma) or CS. Altered mitochondrial fission/fusion proteins have a further potential to influence parameters such as ROS and cell proliferation and apoptosis relevant to airway diseases.
Physiology's Impact: Stop Ignoring the Obvious–SEX MATTERS!
Miller, Virginia M. , Sieck, Gary C. , Reckelhoff, Jane F. , Sieck, Gary

Physiology | January 1, 2014 | Volume: 29 | Issue: 1 | Pages: 4-5

10.1152/physiol.00064.2013 Get It

Effects of the Inflammatory Cytokines TNF-α and IL-13 on Stromal Interaction Molecule–1 Aggregation in Human Airway Smooth Muscle Intracellular Ca2+ Regulation
Li, Jia , Delmotte, Philippe , Aravamudan, Bharathi, Prakash, Y. S. , Sieck, Gary C. , Pabelick, Christina M. , Prakash, Y S , Sieck, Gary

American Journal of Respiratory Cell and Molecular Biology | May 28, 2013 | Volume: 49 | Issue: 4 | Pages: 601-608

10.1165/rcmb.2013-0040oc Get It

Abstract Inflammation elevates intracellular Ca2+ ([Ca2+]i) concentrations in airway smooth muscle (ASM). Store-operated Ca2+ entry (SOCE) is an important source of [Ca2+]i mediated by stromal interaction molecule–1 (STIM1), a sarcoplasmic reticulum (SR) protein. In transducing SR Ca2+ depletion, STIM1 aggregates to form puncta, thereby activating SOCE via interactions with a Ca2+ release-activated Ca2+ channel protein (Orai1) in the plasma membrane. We hypothesized that STIM1 aggregation is enhanced by inflammatory cytokines, thereby augmenting SOCE in human ASM cells. We used real-time fluorescence microscopic imaging to assess the dynamics of STIM1 aggregation and SOCE after exposure to TNF-α or IL-13 in ASM cells overexpressing yellow fluorescent protein–tagged wild-type STIM1 (WT-STIM1) and STIM1 mutants lacking the Ca2+-sensing EF-hand (STIM1-D76A), or lacking the cytoplasmic membrane binding site (STIM1ΔK). STIM1 aggregation was analyzed by monitoring puncta size during the SR Ca2+ depletion induced by cyclopiazonic acid (CPA). We found that puncta size was increased in cells expressing WT-STIM1 after CPA. However, STIM1-D76A constitutively formed puncta, whereas STIM1ΔK failed to form puncta. Furthermore, cytokines increased basal WT-STIM1 puncta size, and the SOCE triggered by SR Ca2+ depletion was increased in cells expressing WT-STIM1 or STIM1-D76A. Meanwhile, SOCE in cells expressing STIM1ΔK and STIM1 short, interfering RNA (siRNA) was decreased. Similarly, in cells overexpressing STIM1, the siRNA knockdown of Orai1 blunted SOCE. However, exposure to cytokines increased SOCE in all cells, increased basal [Ca2+]i, and decreased SR Ca2+ content. These data suggest that cytokines induce a constitutive increase in STIM1 aggregation that contributes to enhanced SOCE in human ASM after inflammation. Such effects of inflammation on STIM1 aggregations may contribute to airway hyperresponsiveness.
Electromyogram-triggered inspiratory event detection algorithm
Dow, Douglas E. , Petrilli, Anita M., Mantilla, Carlos B. , Zhan, Wen‐Zhi, Sieck, Gary C. , Sieck, Gary , Mantilla, Carlos B

The 6th International Conference on Soft Computing and Intelligent Systems, and The 13th International Symposium on Advanced Int | April 26, 2013 | Volume: No volume available | Issue: No issue available | Pages: 789-794

10.1109/scis-isis.2012.6505353 Get It

Age-Related Changes in Diaphragm Muscle Contractile Properties and Myosin Heavy Chain Isoforms
Gosselin, Luc E., Johnson, Brian , Sieck, Gary C. , Sieck, Gary

American journal of respiratory and critical care medicine | April 4, 2013 | Volume: 150 | Issue: 1 | Pages: 174-178

10.1164/ajrccm.150.1.8025746 Get It

Abstract The present study sought to examine the effects of aging on the isometric contractile and fatigue properties as well as the myosin heavy chain (MCH) isoform composition of the rat diaphragm muscle. Male Fischer 344 (F344) specific pathogen-free rats 6 and 24 mo old were used in the study. Peak twitch force was approximately 23% lower (p < 0.05) in the senescent diaphragm compared with the young. Time to peak twitch force and one-half relaxation time of twitch force did not differ between groups. There was a significant decrease (15 to 18%, p < 0.05) in the specific force (N/cm2) of the senescent diaphragm at all stimulation frequencies (10 to 100 Hz) examined. In addition, the fatigability of the diaphragm did not significantly differ between the two groups. No significant changes in the distribution of MHC 1 and 2A isoforms were observed with aging. However, the contribution of MHC 2X significantly decreased with senescence (young, 37.5%; senescent, 30.5%), whereas the contribution of MHC 2B in the senescent diaphragm was significantly higher (young, 6.5%; senescent, 15.0%; p < 0.05). We conclude that the age-related decline in diaphragm muscle specific force is caused by intrinsic factors other than changes in MHC composition.
Muscle dysfunction in COPD
Barreiro, Esther , Sieck, Gary C. , Sieck, Gary

Journal of Applied Physiology | February 8, 2013 | Volume: 114 | Issue: 9 | Pages: 1220-1221

10.1152/japplphysiol.00162.2013 Get It

Neuromotor control in chronic obstructive pulmonary disease
Mantilla, Carlos B. , Sieck, Gary C. , Sieck, Gary , Mantilla, Carlos B

Journal of Applied Physiology | January 18, 2013 | Volume: 114 | Issue: 9 | Pages: 1246-1252

10.1152/japplphysiol.01212.2012 Get It

Neuromotor control of skeletal muscles, including respiratory muscles, is ultimately dependent on the structure and function of the motor units (motoneurons and the muscle fibers they innervate) comprising the muscle. In most muscles, considerable diversity of contractile and fatigue properties exists across motor units, allowing a range of motor behaviors. In diseases such as chronic obstructive pulmonary disease (COPD), there may be disproportional primary (disease related) or secondary effects (related to treatment or other concomitant factors) on the size and contractility of specific muscle fiber types that would influence the relative contribution of different motor units. For example, with COPD there is a disproportionate atrophy of type IIx and/or IIb fibers that comprise more fatigable motor units. Thus fatigue resistance may appear to improve, while overall motor performance (e.g., 6-min walk test) and endurance (e.g., reduced aerobic exercise capacity) are diminished. There are many coexisting factors that might also influence motor performance. For example, in COPD patients, there may be concomitant hypoxia and/or hypercapnia, physical inactivity and unloading of muscles, and corticosteroid treatment, all of which may disproportionately affect specific muscle fiber types, thereby influencing neuromotor control. Future studies should address how plasticity in motor units can be harnessed to mitigate the functional impact of COPD-induced changes.
Prolonged C 2 spinal hemisection-induced inactivity reduces diaphragm muscle specific force with modest, selective atrophy of type IIx and/or IIb fibers
Mantilla, Carlos B. , Greising, Sarah M. , Zhan, Wen-Zhi, Seven, Yasin B. , Sieck, Gary C. , Sieck, Gary , Mantilla, Carlos B

Journal of Applied Physiology | November 30, 2012 | Volume: 114 | Issue: 3 | Pages: 380-386

10.1152/japplphysiol.01122.2012 Get It

The diaphragm muscle (DIAm) is critically responsible for sustaining ventilation. Previously we showed in a commonly used model of spinal cord injury, unilateral spinal cord hemisection at C 2 (SH), that there are minimal changes to muscle fiber cross-sectional area (CSA) and fiber type distribution following 14 days of SH-induced ipsilateral DIAm inactivity. In the present study, effects of long-term SH-induced inactivity on DIAm fiber size and force were examined. We hypothesized that prolonged inactivity would not result in substantial DIAm atrophy or force loss. Adult rats were randomized to control or SH groups ( n = 34 total). Chronic bilateral DIAm electromyographic (EMG) activity was monitored during resting breathing. Minimal levels of spontaneous recovery of ipsilateral DIAm EMG activity were evident in 42% of SH rats (<25% of preinjury root mean square amplitude). Following 42 days of SH, DIAm specific force was reduced 39%. There was no difference in CSA for type I or IIa DIAm fibers in SH rats compared with age, weight-matched controls (classification based on myosin heavy chain isoform expression). Type IIx and/or IIb DIAm fibers displayed a modest 20% reduction in CSA ( P < 0.05). Overall, there were no differences in the distribution of fiber types or the contribution of each fiber type to the total DIAm CSA. These data indicate that reduced specific force following prolonged inactivity of the DIAm is associated with modest, fiber type selective adaptations in muscle fiber size and fiber type distribution.