![]() For additional information, please contact the SKC IRB Chair, Dr. Data restrictions are imposed by the Salish Kootenai College Institutional Review Board (SKC IRB). The study data belong to the Confederated Salish and Kootenai Tribes. Not for resale without express authorization.GUID: 5D676BE5-9EBC-45C5-A312-6EB801DA1ADD Data Availability Statement Its functions include roles in growth and the cell cycle as well as in signal transduction and the synthesis and release of neurotransmitters.įor Research Use Only. Calmodulin contains 149 amino acids and has 4 calcium-binding domains. They are identified by their occurrence in the cytosol or on membranes facing the cytosol and by a high affinity for calcium. Calmodulin is the archetype of the family of calcium-modulated proteins of which nearly 20 members have been found. Studies have found that calmodulin participates in the regulation of several biological processes including energy and biosynthetic metabolism, cell motility, exocytosis, cytoskeletal assembly, and intracellular modulation of both cAMP and calcium concentrations. It acts both directly, through interaction with key target enzymes, and indirectly, via specific kinases. As it binds calcium, calmodulin undergoes conformational changes which can increase its affinity for target proteins. With the capacity to bind up to four calcium ions, this 17 kDa protein acts as an important intracellular receptor for regulatory calcium signals. ![]() Calmodulin is a small, highly conserved calcium binding protein found in all eukaryotic cells. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Among the enzymes to be stimulated by the calmodulin-Ca2+ complex are a number of protein kinases and phosphatases. CT and the other ILM showed similar levels of the proteins studied.Ĭalmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins by Ca2+. SERCA1 was less than SERCA2 in ILM and higher compared with TA. In ILM, CASQ 1 was more abundant than CASQ2 compared with TA. Asterisks and different letter combination indicate statistical significance (* P < 0.05 and ab, ac, ad, bc, or bd P < 0.05, respectively). Quantifications from three independent muscle samples, each sample containing muscles pooled from three or four different rats. ![]() The molecular weight, expressed in kDa, for each protein is indicated. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was used as a control for protein loading, Western blot transfer and nonspecific changes in protein levels. Western blot analysis showing relative abundance of indicated proteins: calsequestrins 1 and 2 (CASQ1 and CASQ2), Sercas 1 and 2 (SERCA1 and SERCA2), calmodulin (CaM), calmodulin kinase II (CaMKII), and Orai1. įigure 2 Protein levels of sarcoplasmic reticulum Ca 2+ -handling proteins in intrinsic laryngeal muscles (ILM), cricothyroid (CT) muscle, extraocular muscles (EOM), and tibialis anterior (TA) muscle. Tissue structure terminology follows nomenclature in Allemand et al and Peters. Labels include: End-endoderm Mes-mesoglea Ect-ectoderm Muc-mucus PS-primary septum SW-seawater at the time the polyps were collected and Sk-skeleton. ( D ) Line tracing of C indicating individual Symbiodiniaceae are found in both the oral endoderm and the calicoblastic epithelium. faveolata collected in May 2008 exhibiting superimposed emissions from mucus (blue fluorescence), carbonic anhydrase (green fluorescence), and calmodulin (red fluorescence). S5, S6 ) image of a horizontal cross-section of decalcified polyp tissues of O. ( C ) A second enlargement (from area shown in Supplementary Figs. ( B ) Line tracing of A indicating individual Symbiodiniaceae. faveolata collected in March 2008 exhibiting superimposed emissions from mucus (blue fluorescence), carbonic anhydrase (green fluorescence), and calmodulin (red fluorescence). 6 A) of a horizontal cross-section of decalcified polyp tissues of O. ![]() ![]() ( A ) Original enlarged image (from box 7A-B shown in Fig. Figure 7 Enlargement of immunohistochemical fluorescence microscopy of the distributions and abundance of carbonic anhydrase, calmodulin and mucus within tagged polyp tissues of O. ![]()
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