Regulatory effects of S-100 protein and parvalbumin on protein kinases and phosphoprotein phosphatases from brain and skeletal muscle

1986 ◽  
Vol 71 (1) ◽  
Author(s):  
Wu-Nan Kuo ◽  
Thomas Blake ◽  
IjazR. Cheema ◽  
Jorge Dominguez ◽  
James Nicholson ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinases ◽  
Phosphoprotein Phosphatases ◽  
S 100 ◽  
Regulatory Effects

Melatonin: a novel strategy for prevention of obesity and fat accumulation in peripheral organs through the improvements of circadian rhythms and antioxidative capacity

2020 ◽  
Vol 3 (1) ◽  
pp. 58-76 ◽  
Author(s):  
Bohan Rong ◽  
Qiong Wu ◽  
Chao Sun
Keyword(s):  
Oxidative Stress ◽  
Skeletal Muscle ◽  
Circadian Rhythms ◽  
Regulatory Mechanisms ◽  
Antioxidative Capacity ◽  
Unicellular Alga ◽  
Peripheral Tissues ◽  
Peripheral Organs ◽  
Regulatory Effects ◽  
Novel Strategy

Melatonin is a well-known molecule for its involvement in circadian rhythm regulation and its contribution to protection against oxidative stress in organisms including unicellular alga, animals and plants. Currently, the bio-regulatory effects of melatonin on the physiology of various peripheral tissues have drawn a great attention of scientists. Although melatonin was previously defined as a neurohormone secreted from pineal gland, recently it has been identified that virtually, every cell has the capacity to synthesize melatonin and the locally generated melatonin has multiple pathophysiological functions, including regulations of obesity and metabolic syndromes. Herein, we focus on the effects of melatonin on fat deposition in various peripheral organs/tissues. The two important regulatory mechanisms related to the topic, i.e., the improvements of circadian rhythms and antioxidative capacity will be thoroughly discussed since they are linked to several biomarkers involved in obesity and energy imbalance, including metabolism and immunity. Furthermore, several other functions of melatonin which may serve to prevent or promote obesity and energy dysmetabolism-induced pathological states are also addressed. The organs of special interest include liver, pancreas, skeletal muscle, adipose tissue and the gut microbiota.

scholarly journals Characterization of insulin-stimulated seryl/threonyl protein kinases in rat skeletal muscle

1993 ◽  
Vol 268 (18) ◽  
pp. 13203-13213
Author(s):  
Y.J. Hei ◽  
J.H. McNeill ◽  
J.S. Sanghera ◽  
J. Diamond ◽  
M. Bryer-Ash ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinases ◽  
Rat Skeletal Muscle

scholarly journals Melanoma maligno em búfalos (Bubalus bubalis) albinos

2015 ◽  
Vol 36 (5) ◽  
pp. 3239 ◽  
Author(s):  
Maria Cecília Florisbal Damé ◽  
Clairton Marcolongo-Pereira ◽  
Letícia Fiss ◽  
Maria de Lourdes Adrién ◽  
Ana Lucia Schild
Keyword(s):  
Skeletal Muscle ◽  
Water Buffalo ◽  
Bubalus Bubalis ◽  
Renal Capsule ◽  
Southern Brazil ◽  
Epithelioid Cells ◽  
Melanocytic Tumors ◽  
Immunohistochemistry Staining ◽  
S 100 ◽  
Collagenous Stroma

<p>Two albino water buffalo affected by multiple melanocytic tumors in Southern Brazil are described. Grossly, there were multiple dark tumors within the skin, skeletal muscle, lungs, and lymph nodes. The tumor was also present in the pericardial sac, renal capsule, mediastinum and pleura. Microscopically, the tumors consisted of polyhedral epithelioid cells arranged in solid nests or interwoven fascicles supported by a thin and sparse collagenous stroma. The cytoplasm was eosinophilic and sometimes contained varying amounts of melanin pigment. The mitotic rates were low. Immunohistochemistry staining with Tyrosinase, Melan-A, Vimentin, S-100 protein, and neurofilament were positive. It is possible that the polymorphisms related to pigmentation in albino buffalo contributed with a high risk of developing melanoma as suggested in humans.</p>

scholarly journals The regulatory domain of protein kinase C delta positively regulates insulin receptor signaling

2009 ◽  
Vol 44 (3) ◽  
pp. 155-169 ◽  
Author(s):  
Avraham I Jacob ◽  
Miriam Horovitz-Fried ◽  
Shlomit Aga-Mizrachi ◽  
Tamar Brutman-Barazani ◽  
Hana Okhrimenko ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Insulin Receptor ◽  
Glycogen Synthase ◽  
Regulatory Domain ◽  
Protein Kinase C Delta ◽  
Kinase C ◽  
Regulatory Effects ◽  
In Cells

Protein kinase C delta (PKCδ) is induced by insulin to rapidly associate with insulin receptor (IR) and upregulates insulin signaling. We utilized specific JM and CT receptor domains and chimeras of PKCα and PKCδ regulatory and catalytic domains to elucidate which components of PKCδ are responsible for positive regulatory effects of PKCδ on IR signaling. Studies were performed on L6 and L8 skeletal muscle myoblasts and myotubes. PKCδ was preferentially bound to the JM domain of IR, and insulin stimulation increased this binding. Both PKCδ/α and PKCα/δ chimeras (regulatory/catalytic) were bound preferentially to the JM but not to the CT domain of IR. Although IR–PKCδ binding was higher in cells expressing either the PKCδ/α or PKCα/δ chimera than in control cells, upregulation of IR signaling was observed only in PKCδ/α cells. Thus, in response to insulin increases in tyrosine phosphorylation of IR and insulin receptor substrate-1, downstream signaling to protein kinase B and glycogen synthase kinase 3 (GSK3) and glucose uptake were greater in cells overexpressing PKCδ/α and the PKCδ/δ domains than in cells expressing the PKCα/δ domains. Basal binding of Src to PKCδ was higher in both PKCδ/α- and PKCα/δ-expressing cells compared to control. Binding of Src to IR was decreased in PKCα/δ cells but remained elevated in the PKCδ/α cells in response to insulin. Finally, insulin increased Src activity in PKCδ/α-expressing cells but decreased it in PKCα/δ-expressing cells. Thus, the regulatory domain of PKCδ via interaction with Src appears to determine the role of PKCδ as a positive regulator of IR signaling in skeletal muscle.

Metallophosphoesterases: structural fidelity with functional promiscuity

2015 ◽  
Vol 467 (2) ◽  
pp. 201-216 ◽  
Author(s):  
Nishad Matange ◽  
Marjetka Podobnik ◽  
Sandhya S. Visweswariah
Keyword(s):  
Active Site ◽  
Metal Ion ◽  
Active Sites ◽  
Dependent Manner ◽  
The Core ◽  
Repair Enzymes ◽  
Phosphoprotein Phosphatases ◽  
Purple Acid Phosphatases ◽  
Binuclear Metal ◽  
Regulatory Effects

Calcineurin-like metallophosphoesterases (MPEs) form a large superfamily of binuclear metal-ion-centre-containing enzymes that hydrolyse phosphomono-, phosphodi- or phosphotri-esters in a metal-dependent manner. The MPE domain is found in Mre11/SbcD DNA-repair enzymes, mammalian phosphoprotein phosphatases, acid sphingomyelinases, purple acid phosphatases, nucleotidases and bacterial cyclic nucleotide phosphodiesterases. Despite this functional diversity, MPEs show a remarkably similar structural fold and active-site architecture. In the present review, we summarize the available structural, biochemical and functional information on these proteins. We also describe how diversification and specialization of the core MPE fold in various MPEs is achieved by amino acid substitution in their active sites, metal ions and regulatory effects of accessory domains. Finally, we discuss emerging roles of these proteins as non-catalytic protein-interaction scaffolds. Thus we view the MPE superfamily as a set of proteins with a highly conserved structural core that allows embellishment to result in dramatic and niche-specific diversification of function.

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