Journal: Journal of Sport and Health Science

Article Title: Exercise attenuates stress-related signaling as sensed by higher phosphorylation of small heat shock proteins in skeletal muscle from older individuals

doi: 10.1016/j.jshs.2025.101111

Figure Lengend Snippet: Relative HSP abundances in whole skeletal muscle homogenates from young adults and older adults pre and post HIT exercise. Representative Westen blots of (A) HSP72, HSP27, and αB-crystallin and (B) phosphorylated HSP27 Ser15 (pHSP27 Ser15) and pαB-crystallin Ser59 in whole muscle homogenates from the vastus lateralis of the same individuals. Calibration curves of mixed muscle homogenates are indicated and were used to determine the relative number of given proteins (see Methods). Stain-free gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Relative abundances of (C) HSP72, (D) HSP27, (E) pHSP27 Ser15, (F) αB-crystallin, and (G) pαB-crystallin Ser59 from young (circle) and older adults Pre (square) and older adults Post (triangle) HIT exercise are shown relative to average Old (pre) on a given gel (data are presented as mean ± SD). Individuals indicated by the number of symbols ( n : 5–7), with the same color assigned to the same individual and consistent across all graphs. * p ≤ 0.05 indicates Brown-Forsye and Welch’s and post hoc analysis using Games-Horwell. HIT = high-intensity training; HSP = heat shock protein; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.

Article Snippet: Details of antibodies used are as follows: HSP72 (1 in 500 mouse monoclonal, SMC100A; StressMarq Biosciences, Victoria, Canada); HSP27 (1 in 1000 mouse monoclonal, G3.1 ab2790; Abcam, Cambridge, UK); pHSP27 Ser15 (1 in 2000 monoclonal rabbit, ab76313; Abcam), pHSP27 Ser82 (1 in 2000 polyclonal mouse, ADI-SPA-524; Enzo Biochem, Farmingdale, NY, USA), αB-crystallin (1 in 1000 mouse monoclonal, SPA-222; StressGen Biotechnologies), pαB-crystallin Ser59 (1 in 1000 rabbit polyclonal, SPA-227; StressGen Biotechnologies).

Techniques: Staining, Membrane

Journal: Journal of Sport and Health Science

Article Title: Exercise attenuates stress-related signaling as sensed by higher phosphorylation of small heat shock proteins in skeletal muscle from older individuals

doi: 10.1016/j.jshs.2025.101111

Figure Lengend Snippet: HSP abundances in type I and II skeletal muscle fibers from young and older adults. (A, C, and F) The MHC isoform present was determined in individual muscle fiber segments from the vastus lateralis and, following pooling into type I and type II groups from a given biopsy, were analyzed by Westen blotting. Westen blots of (A) HSP72, (C) HSP27 and pHSP27 Ser15, (F) αB-crystallin and pαB-crystallin Ser59, with MHC isoforms in groups of fibers. Stain-free gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Calibration curves of mixed muscle homogenates are indicated. Relative protein abundances of (B) HSP72, (D) HSP27, (E) pHSP27 Ser15, (G) αB-crystallin, and (H) pαB-crystallin Ser59 in fibers from young (circle) and older adults (square) type I fibers (no outline) and type II fibers (outline). All fibers are expressed relative to the average older adult’s type I fibers. The same color is assigned to the same individual and is consistent with (data are presented as mean ± SD). * p < 0.05 and ** p < 0.01, mixed effect model Univariant using either Tukey’s or Games-Horwell’s multiple comparison test (see Methods). HIT = high-intensity training; HSP = heat shock protein; MHC = myosin heavy chain; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.

Article Snippet: Details of antibodies used are as follows: HSP72 (1 in 500 mouse monoclonal, SMC100A; StressMarq Biosciences, Victoria, Canada); HSP27 (1 in 1000 mouse monoclonal, G3.1 ab2790; Abcam, Cambridge, UK); pHSP27 Ser15 (1 in 2000 monoclonal rabbit, ab76313; Abcam), pHSP27 Ser82 (1 in 2000 polyclonal mouse, ADI-SPA-524; Enzo Biochem, Farmingdale, NY, USA), αB-crystallin (1 in 1000 mouse monoclonal, SPA-222; StressGen Biotechnologies), pαB-crystallin Ser59 (1 in 1000 rabbit polyclonal, SPA-227; StressGen Biotechnologies).

Techniques: Staining, Membrane, Comparison

Journal: Journal of Sport and Health Science

Article Title: Exercise attenuates stress-related signaling as sensed by higher phosphorylation of small heat shock proteins in skeletal muscle from older individuals

doi: 10.1016/j.jshs.2025.101111

Figure Lengend Snippet: HSP abundances in type I and II skeletal fibers from older adults pre- and post HIT exercise. Relative protein abundances of (A and B) HSP72, (C and D) HSP27, (E and F) pHSP27 Ser15, (G and H) αB-crystallin, and (I and J) pαB-crystallin Ser59 in fibers from old pre and old post HIT exercise. All fibers are expressed relative to the average old pre type I fibers or relative pre type II depending on fiber type. The same color is assigned to the same Individual, consistent in both graphs and all figures. * p < 0.05 and ** p < 0.01 indicated significant difference in paired t -test (except pHSP27 Ser15 Wilcoxon match-pair rank test). Representative blots are shown in . HIT = high-intensity training; HSP = heat shock protein; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.

Article Snippet: Details of antibodies used are as follows: HSP72 (1 in 500 mouse monoclonal, SMC100A; StressMarq Biosciences, Victoria, Canada); HSP27 (1 in 1000 mouse monoclonal, G3.1 ab2790; Abcam, Cambridge, UK); pHSP27 Ser15 (1 in 2000 monoclonal rabbit, ab76313; Abcam), pHSP27 Ser82 (1 in 2000 polyclonal mouse, ADI-SPA-524; Enzo Biochem, Farmingdale, NY, USA), αB-crystallin (1 in 1000 mouse monoclonal, SPA-222; StressGen Biotechnologies), pαB-crystallin Ser59 (1 in 1000 rabbit polyclonal, SPA-227; StressGen Biotechnologies).

Techniques:

Journal: Bioactive Materials

Article Title: Near infrared enhanced palladium loaded siraitia grosvenorii carbon dots amplify mitophagy for acute lung injury immunotherapy

doi: 10.1016/j.bioactmat.2026.02.040

Figure Lengend Snippet: In vivo ALI therapy evaluation. A) Time schedule of in vivo animal experiment. B) Macroscopic observation in the lung tissue of treated rats. C) Wet/dry ratio in the lung tissue of treated rats. D) Inflammatory factors expression levels in the blood of treated rats. E) Inflammatory factors expression levels in the lung tissue of treated rats. F) ROS levels in the lung tissue of treated rats. (Scale bar = 50 μm) G) H&E staining images in the lung tissue of treated rats. (Scale bar = 100 μm) H) TNF-α expression levels in the lung tissue of treated rats, (Scale bar = 100 μm) and the corresponding quantified results (I). J) HSP70 expression levels in the lung tissue of treated rats, (Scale bar = 100 μm) and the corresponding quantified results (K). L) CD31 expression levels in the lung tissue of treated rats, (Scale bar = 100 μm) and the corresponding quantified results (M). The corresponding groups were: rats without treatments (sham group), and rats pretreated with LPS followed by IT administration of PBS (ALI group), CPs (CPs), CPs@SS31 (CPs@SS31) and CPs@SS31 combining with NIR irradiation (CPs@SS31+NIR). (”∗” symbol compared with sham group, ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001 and ∗∗∗∗p < 0.0001).

Article Snippet: And then, the cells were incubated with primary antibodies (anti-IL-6, TNF-α, CD206, CD86, CD31, HSP70 and PINK1, 1 : 200, Proteintech, USA) overnight.

Techniques: In Vivo, Expressing, Staining, Irradiation

Journal: Materials Today Bio

Article Title: Exercise-primed exosomes in an injectable hydrogel promote myocardial repair via angiogenesis and ferroptosis inhibition

doi: 10.1016/j.mtbio.2026.103035

Figure Lengend Snippet: Characterization and distribution of exercise-derived serum exosomes . A, Schematic diagram illustrating the proposed mode of action and therapeutic strategy. B, TEM image showing the typical cup-shaped morphology of isolated exosomes. Scale bar = 100 nm. C, Size distribution profile of exosomes measured by DLS. D, Confocal microscopy image showing the incorporation of exosomes (green) within the hydrogel matrix. Scale bar = 50 μm. E, Cellular uptake of DiO-labeled exosomes (green) by HUVECs in vitro. Nuclei were stained with DAPI (blue). Scale bar = 25 μm. F, Western blot analysis of Exosome positive marker proteins TSG101, CD81, HSP70 and exosome negative marker protein Histone. G, Flowchart for isolating exosomes from the serum of exercise and sedentary mice. H, In vivo distribution and sustained release of exosomes in cardiac tissue of MI-Exos and MI-Exos@Gel-PEG treated mice. I, Quantitative analysis of exosomal fluorescence intensity in heart tissues (n = 3). (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

Article Snippet: F, Western blot analysis of Exosome positive marker proteins TSG101, CD81, HSP70 and exosome negative marker protein Histone.

Techniques: Derivative Assay, Isolation, Confocal Microscopy, Labeling, In Vitro, Staining, Western Blot, Marker, In Vivo, Fluorescence

Journal: Plant Reproduction

Article Title: Low-temperature stress modulates pollen tube growth through temperature-dependent multi-level regulatory mechanisms in Camellia sinensis

doi: 10.1007/s00497-026-00539-3

Figure Lengend Snippet: Effects of low-temperature stress on stress-related protein levels. (a) Representative raw immunoblot results for HSP70. (b) Representative raw immunoblot results for SuSy (c) HSP70 band intensity. (d) SuSy band intensity

Article Snippet: Membranes were incubated with primary antibodies against HSP70 (rabbit polyclonal,1:5000; Agrisera) (Piccini et al. ) and SuSy1 (rabbit polyclonal, 1:5000; Agrisera) for 1 h at room temperature (Persia et al. ), followed by incubation with an Alexa Fluor 594-conjugated secondary antibody (1:50) for 1 h at room temperature.

Techniques: Western Blot

Journal: Frontiers in Microbiology

Article Title: Mycoplasma bovis infection alters small extracellular vesicle cargo derived from bovine endometrial epithelial cells cultured in static bioreactors

doi: 10.3389/fmicb.2026.1770401

Figure Lengend Snippet: Western blotting revealed proteins associated with small extracellular vesicles (sEVs) using specific/exclusion antibodies. Anti–protein rabbit primary antibodies against Syntenin–1 (expected kDa of ∼32) (A) CD63 (expected kDa of ∼26) (B) , Heat Shock Protein 70 (expected kDa of 66–78) (C) , and Calnexin (expected kDa of ∼98) (D) , were diluted 1/1,000 in blocking solution. A goat anti–rabbit horse radish peroxidase secondary antibody, diluted 1/10,000 in blocking solution was used. A SeeBlue Plus2 Pre–stained Protein Standard (Lane 1) was used for size comparison of fractions 2–11 (F2–11).

Article Snippet: Membranes were blocked for 1 h at room temperature in 5% skim milk (w/v) in 1 × TBS-T (0.1% Tween-20), then washed twice in TBS-T. Primary antibodies (1:1,000 in blocking buffer) targeting CD63, CD9, HSP70 (Exo-Ab-Kit-1, System Biosciences), Syntenin-1 (Ab19903, Abcam), and Calnexin (Ab22595, Abcam) were incubated overnight at 4°C with agitation.

Techniques: Western Blot, Blocking Assay, Staining, Comparison