Unique calcium-dependent hydrophobic binding proteins: possible independent mediators of intracellular calcium distinct from calmodulin

Calcium-dependent regulation of cellular processes is mediated by specific intracellular proteins. A newly described set of proteins isolated from chicken gizzard with Mr of 67 X 10(3), 35 X 10(3), 33 X 10(3) and 30 X 10(3) also express a hydrophobic site in the presence of calcium. These proteins are isolated from several other cellular tissues and are termed calcimedins. These proteins differ from calmodulin in isoelectric point, DEAE-cellulose binding characteristics and heat stability. The calcimedins do not activate calmodulin-dependent cyclic nucleotide phosphodiesterase but do activate a hepatic microsomal Ca2+ -ATPase system. Hence, the possibility is opened that calcium regulation of cellular processes is mediated by calcium-binding proteins in addition to calmodulin.

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Calmodulin and Calmodulin Binding Proteins in Dictyostelium: A Primer

International Journal of Molecular Sciences ◽

10.3390/ijms21041210 ◽

2020 ◽

Vol 21 (4) ◽

pp. 1210

Author(s):

Danton H. O’Day ◽

Ryan J. Taylor ◽

Michael A. Myre

Keyword(s):

Conformational Changes ◽

Calcium Binding ◽

Binding Proteins ◽

Regulatory Protein ◽

Model Organism ◽

Ion Binding ◽

Calcium Dependent ◽

Calmodulin Binding ◽

Human Counterpart ◽

Ef Hands

Dictyostelium discoideum is gaining increasing attention as a model organism for the study of calcium binding and calmodulin function in basic biological events as well as human diseases. After a short overview of calcium-binding proteins, the structure of Dictyostelium calmodulin and the conformational changes effected by calcium ion binding to its four EF hands are compared to its human counterpart, emphasizing the highly conserved nature of this central regulatory protein. The calcium-dependent and -independent motifs involved in calmodulin binding to target proteins are discussed with examples of the diversity of calmodulin binding proteins that have been studied in this amoebozoan. The methods used to identify and characterize calmodulin binding proteins is covered followed by the ways Dictyostelium is currently being used as a system to study several neurodegenerative diseases and how it could serve as a model for studying calmodulinopathies such as those associated with specific types of heart arrythmia. Because of its rapid developmental cycles, its genetic tractability, and a richly endowed stock center, Dictyostelium is in a position to become a leader in the field of calmodulin research.

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Purification of vitamin D-dependent 28,000-Mr calcium-binding protein from bovine cerebellum and kidney by calcium-dependent elution from DEAE-cellulose DE-52 column chromatography

Analytical Biochemistry ◽

10.1016/0003-2697(85)90043-0 ◽

1985 ◽

Vol 151 (1) ◽

pp. 1-6 ◽

Cited By ~ 24

Author(s):

Kei Maruyama ◽

Ken Ebisawa ◽

Yoshiaki Nonomura

Keyword(s):

Vitamin D ◽

Column Chromatography ◽

Calcium Binding ◽

Binding Protein ◽

Deae Cellulose ◽

Calcium Binding Protein ◽

Calcium Dependent

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Specificity of the binding of trifluoperazine to the calcium-dependent activator of phosphodiesterase and to a series of other calcium-binding proteins

Biochimica et Biophysica Acta (BBA) - General Subjects ◽

10.1016/0304-4165(78)90132-0 ◽

1978 ◽

Vol 540 (2) ◽

pp. 197-204 ◽

Cited By ~ 155

Author(s):

Robert M. Levin ◽

Benjamin Weiss

Keyword(s):

Calcium Binding ◽

Binding Proteins ◽

Calcium Binding Proteins ◽

Calcium Dependent

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Annexins and their role in the control of symbioses development of plants with nitrogen-fixing bacteria and arbuscular mycorrhizal fungi

Ecological genetics ◽

10.17816/ecogen18533 ◽

2020 ◽

Author(s):

Elena Anatolyevna Dolgikh ◽

Darya Vladimirovna Kustova

Keyword(s):

Mycorrhizal Fungi ◽

Calcium Binding ◽

Structural Organization ◽

Physiological Role ◽

Arbuscular Mycorrhizal ◽

Structural Similarity ◽

Binding Motifs ◽

Calcium Dependent ◽

Cellular Processes

Annexins belong to the superfamily of calcium-dependent phospholipid binding proteins. The participation of these proteins in the regulation of structural organization of membranes, vesicular transport and a variety of signal transduction pathways is important for many cellular processes. Despite the structural similarity with animal annexins, plant annexins are characterized by significant variability of the N-terminal region and modification of calcium-binding motifs in II and III repeats, while calcium-binding motifs in I and IV repetitions remain conservative. However, the physiological role of animal and plant annexins, as well as mechanisms of their influence on calcium metabolism, may be similar. This review focused on the latest data about the structure and functioning of plant annexins.

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Calcium-Binding Proteins are Altered in the Cerebellum in Schizophrenia

10.1101/2020.03.02.972810 ◽

2020 ◽

Author(s):

Francisco Vidal-Domènech ◽

Gemma Riquelme ◽

Raquel Pinacho ◽

Ricard Rodriguez-Mias ◽

América Vera ◽

...

Keyword(s):

Calcium Binding ◽

Binding Proteins ◽

Cell Communication ◽

Chronic Schizophrenia ◽

Calcium Binding Proteins ◽

Calcium Dependent ◽

Enriched Category ◽

Ef Hand ◽

Altered Proteins ◽

Independent Cohort

AbstractAlterations in the cortico-cerebellar-thalamic-cortical circuit might underlie the diversity of symptoms in schizophrenia. However, molecular changes in cerebellar neuronal circuits, part of this network, have not yet been fully determined. Using LC-MS/MS, we screened altered candidates in pooled grey matter of cerebellum from schizophrenia subjects who committed suicide (n=4) and healthy individuals (n=4). Further validation by immunoblotting of three selected candidates was performed in two cohorts comprising schizophrenia (n=20), non-schizophrenia suicide (n=6) and healthy controls (n=21). We found 99 significantly altered proteins, 31 of them previously reported in other brain areas by proteomic studies. Transport function was the most enriched category, while cell communication was the most prevalent function. For validation, we selected the vacuolar proton pump subunit 1 (VPP1), from transport, and two EF-hand calcium-binding proteins, calmodulin and parvalbumin from cell communication. All candidates showed significant changes in schizophrenia (n=7) compared to controls (n=7). VPP1 was altered in the non-schizophrenia suicide group and increased levels of parvalbumin were linked to antipsychotics. Further validation in an independent cohort of non-suicidal chronic schizophrenia subjects (n=13) and non-psychiatric controls (n=14) showed that parvalbumin was increased while calmodulin was decrease in schizophrenia. Our findings provide evidence of an dysregulation of calcium-binding proteins in the cerebellum in schizophrenia, suggesting an impact on normal calcium-dependent synaptic functioning of cerebellar circuits. Our study also links VPP1 to suicide behaviours, suggesting a possible impairment in vesicle neurotransmitter refilling and release in these phenotypes.

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Interactive Effects of PEG-induced Water Stress and CaCl2 on the Status of Calcium and Ca2+ Binding Proteins During Seedling Growth of Peanut (Arachis hypogaea L.) Cultivars

Peanut Science ◽

10.3146/pnut.31.1.0001 ◽

2004 ◽

Vol 31 (1) ◽

pp. 1-6

Author(s):

Ch Sulochana ◽

N. Savithramma

Keyword(s):

Water Stress ◽

Calcium Binding ◽

Binding Proteins ◽

Deae Cellulose ◽

Calcium Content ◽

Bovine Brain ◽

Calcium Binding Proteins ◽

Interactive Effects ◽

The Status ◽

Ameliorative Effect

Abstract Seedlings of two peanut cultivars (TPT-1 and TPT-4) grown in distilled water for 12 d were subjected to polyethylene glycal (PEG-6000) induced water stress. Twenty mM CaCl2 was added to the stressed seedlings to examine the ameliorative effect of PEG induced water stress. The seedlings were analysed for calcium content at 2-d intervals for 7 d. Calcium-binding proteins (CaBPs) were quantified in the seedlings of different treatments in the two cultivars. Water stressed seedlings had significantly lower calcium content. The seedlings of the two cultivars showed differences in the accumulation of calcium under treatments. CaBPs fractionated through DEAE cellulose columns. The pooled fractions of the proteins separated by SDS-PAGE contained different molecular weights of polypeptides. The polypeptides were resolved on the CaCl2-treated seedlings better than either control or water stressed and PEG + CaCl2 treated seedlings. Calmodulin isolated from the seedlings of both the cultivars showed a single band co-migrating with 15 kDa protein of Bovine brain calmodulin. Differences between the cultivars, treatments and interaction for the parameters were significant. The two cultivars showed differences in calcium-binding proteins under PEG-induced water stress and its alleviation by CaCl2 in peanut seedlings.

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