Disease relevance of LOC396874

• Such discrimination could be achieved as a result of post-translational modification of the gelsolin; only in this way can differences between apparently identical proteins isolated from human plasma and expressed in E. coli be reconciled [1].

High impact information on LOC396874

• Cofilin also has in the carboxyl-terminal portion a region homologous to the sequence shared by gelsolin, fragmin, and Acanthamoeba profilin [2].
• Nucleotide sequence of pig plasma gelsolin. Comparison of protein sequence with human gelsolin and other actin-severing proteins shows strong homologies and evidence for large internal repeats [3].
• Probably due to changes in the C-terminal part of gelsolin, a stable ternary complex is only formed at [Ca(2+)] >10(-5) M [Khaitlina, S., and Hinssen, H. (2002) FEBS Lett. 521, 14-18] [4].
• The inhibitory effect was increased with a combination of both (up to 67%) although it was evident that even under these conditions the actin filaments were not fully protected from being severed by gelsolin [5].
• Direct analysis of the actin-severing activity of gelsolin by a fluorimetric assay using pyrene-labelled actin confirmed this conclusion [5].

Biological context of LOC396874

• We therefore conclude that the binding site of the antibody is covered by the N-terminal extension in plasma gelsolin and thus sterically hinders antibody binding [6].
• The actin-binding protein gelsolin is highly conserved in vertebrates and exists in two isoforms, a cytoplasmic and an extracellular variant, generated by alternative splicing [6].
• We have purified the two functionally distinct domains of gelsolin, a Ca(2+)-dependent actin binding protein, by proteolytic cleavage and characterized their size and shape in solution by dynamic light scattering [7].
• Gelsolin canceled sperm motility within 20 min of treatment while 0.6 M KI had immediate effects [8].
• The effect of gelsolin to enhance the ATPase activity of actomyosin is potentiated by tropomyosin, which is a Ca2+-insensitive actomyosin enhancer [9].

Anatomical context of LOC396874

• We have investigated the cumulative effects of three smooth-muscle actin-binding proteins, gelsolin, caldesmon and tropomyosin, on actin activation of myosin Mg(2+)-ATPase activity under low-ionic-strength conditions [5].
• From double labeling of gelsolin and actin it became evident that the staining patterns for both proteins were practically coincident: The width and location of the fluorescent bands varied with the degree of contraction of the myofibrils [10].
• From these observations it was concluded that a significant part of the total gelsolin in skeletal muscle cells is tightly associated with the thin filaments, and is an integral part of the myofibrils even at low Ca(++)-concentrations [10].
• Exogenous gelsolin stimulates AR assayed in a permeabilized spermatozoa model [11].
• Immunocytochemical localization of gelsolin in fibroblasts, myogenic cells, and isolated myofibrils [10].

Associations of LOC396874 with chemical compounds

• The tight direct association of the dimer to gelsolin is shown by the titration of gelsolin with the fluorescently labeled dimer and by the higher concentration of phosphatidylinositol 4,5-bisphosphate required to inhibit the formation of BPM-dimer complex with gelsolin than that of BPM-monomer complex [12].
• The amino-terminal fragment of gelsolin is cross-linked to Cys-374 of actin in the EGTA-resistant actin-gelsolin complex [13].
• Gelsolin treatment after high salt extraction affected neither actin nor nebulin in the thin filaments [14].
• Over 90% of the gelsolin bound to F-actin in 0.1 mM CaCl2 in experiments using 24 microM actin and 2-10 nM 125I-gelsolin, but only 40-50% bound in 1 mM EGTA [15].
• Inhibition of three different pathways of PIP2 hydrolysis during capacitation did not cancel gelsolin loss from membranes [11].

Other interactions of LOC396874

• Since contractile proteins often vary with the cell type and may require different conditions for their interactions, we have developed a procedure which allows the parallel purification of actin-binding protein (ABP), vinculin, alpha-actinin, gelsolin as well as actin and tropomyosin from the same batch of cells [16].

Analytical, diagnostic and therapeutic context of LOC396874

• In titration experiments in which actin at different concentrations was reacted with a fixed concentration of gelsolin, end points were obtained for the formation of both cross-linked species at about two actins per gelsolin, implying that a 2:1 noncovalent complex is cross-linked [17].
• Circular dichroism measurement of plasma gelsolin indicated that most change in secondary structure was associated with Ca2+ binding to the high-affinity sites [18].
• When a chymotryptic digest of gelsolin containing the amino-terminal 15-kDa fragment was mixed with BPM-actin (42 kDa) and irradiated for cross-linking, a band of 58 kDa appeared on SDS-PAGE which was shown to contain actin molecule by using fluorescently labeled actin [13].
• Immunofluorescence microscopy localized both endogenous and exogenous gelsolin in the I-Z-I-regions of the sarcomers [14].
• The presence of gelsolin in myofibrils after this treatment was also confirmed by immunoblotting [10].

References