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Full-Text Articles in Medicine and Health Sciences
A Role For Shps-1/Sirpα In Concanavalin A-Dependent Production Of Mmp-9, Arm R. Amin, M. Helal Uddin Biswas, Takeshi Senga, Gen-Sheng Feng, Reiji Kannagi, Munna L. Agarwal, Michinari Hamaguchi
A Role For Shps-1/Sirpα In Concanavalin A-Dependent Production Of Mmp-9, Arm R. Amin, M. Helal Uddin Biswas, Takeshi Senga, Gen-Sheng Feng, Reiji Kannagi, Munna L. Agarwal, Michinari Hamaguchi
Pharmaceutical Science and Research
SHPS‐1/SIRPα1 is a transmembrane glycoprotein that belongs to the immunoglobulin (Ig) super family. In the present study, we show that SHPS‐1 strongly associates with Concanavalin A (Con A), a plant lectin obtained from jack beans. Further studies with SHPS‐1 mutants reveal that the extracellular domain of SHPS‐1 containing the Ig sequence is responsible for its association with Con A. Con A treatment induces cross‐linking and multimerization of the SHPS‐1 protein in the plasma membrane, accompanied by its tyrosine phosphorylation and recruitment of SHP‐2. In contrast, Ricinus communis agglutinin (RCA), another lectin obtained from castor bean, does not bind or activate …
Age-Related Dgc Structure And Function In The F344/N X Bn Rat Heart, Sunil K. Kakarla
Age-Related Dgc Structure And Function In The F344/N X Bn Rat Heart, Sunil K. Kakarla
Theses, Dissertations and Capstones
Recent data has suggested that disruption of the dystrophin-glycoprotein complex (DGC) may be involved in mediating the progression of cardiac hypertrophy and failure. Here we examined the regulation of DGC proteins in the hearts of adult (6 months), aged (30 months), and very aged (36 months) F344/N X BN rats . Compared to adult animals, the content of α- and β-dystroglycan were 6.93 ± 5.16% and 58.36 ± 3.64% higher, respectively (P < 0.05) in very aged animals. Immunoblotting and immunhistochemical analysis suggested that aging appeared to diminish alpha-sarcoglycan, beta-sarcoglycan and delta-sarcoglycan content by 13.89 ± 3.1%,15.8 ± 2.8% and 18.63 ± 3.04%, respectively (P < 0.05). These alterations in the DGC occurred coincident with age- associated alterations in cytoplasmic anti-rat IgG immunoreactivity, TUNEL positive nuclei, alpha-fodrin cleavage, indices of caspase-3 activation and diminished AKT phosphoryation (Ser 308). Taken together, these data suggest that aging alters cardiac DGC structure and function.