Psychiatry related information on Kalrn

• In general, levels of NPY, PAM and kalirin mRNA showed similar transient increases after acute and repeated electroconvulsive shock [1].

High impact information on Kalrn

• The effects of Kalirin on TrkA provide a molecular basis for the requirement of Kalirin in process extension from PC12 cells and for previously observed effects on axonal extension and dendritic maintenance [2].
• Kalirin proteins with four different NH(2) termini are generated through the use of five different 5'-ends; three of the proteins differ only at the extreme NH(2) terminus, and one is truncated because translation is initiated at a methionine in the 5th spectrin repeat [3].
• In primary cultures of neurons, Kalirin-7 is detected in spine-like structures, while other forms of Kalirin are visualized in the cell soma and throughout the neurites [4].
• Kalirin is a brain-specific protein, first identified through its interaction with peptidylglycine-alpha-amidating monooxygenase [4].
• P-CIP10 is a 217-kDa cytosolic protein with nine spectrin-like repeats and adjacent Dbl homology and pleckstrin homology domains typical of GDP/GTP exchange factors [5].

Biological context of Kalrn

• P-CIP10 (kalirin), a member of the Dbl family of proteins, may serve as part of a signal transduction system linking the catalytic domains of PAM in the lumen of the secretory pathway to cytosolic factors regulating the cytoskeleton and signal transduction pathways [5].
• Comparisons of the rat and human Kalirin promoter regions reveal numerous shared potential regulatory elements [6].
• During embryonic development, Trio, the Drosophila orthologue of Kalirin, plays an essential role in axon guidance; localization of Kalirin to the somatodendritic region of adult neurons provides the basis for future studies of regulation and function [7].
• We have previously described multiple isoforms of Kalirin derived through alternative splicing and multiple transcription start sites, but multiple isoforms of Trio containing different functional domains have not been described [8].

Anatomical context of Kalrn

• Although many factors determine dendrite shape and spine formation, expression of Kalirin is necessary for the normal function of these many regulatory elements [9].
• However, scattered interneurons contained increased levels of kalirin only after repeated shocks [1].
• Expression of kalirin, a neuronal GDP/GTP exchange factor of the trio family, in the central nervous system of the adult rat [7].
• Low levels of Kalirin mRNA were detected in the paraventricular, supraoptic, and reticular thalamic nuclei and in the ventromedial hypothalamic nucleus [7].
• By in situ hybridization, the highest levels of Kalirin mRNA were found in the cerebral cortex, hippocampal formation, and Purkinje cells, with high levels also in thalamus, caudate putamen, septal nucleus, nucleus accumbens, amygdala, and anterior olfactory nucleus [7].

Associations of Kalrn with chemical compounds

• P-CIP2 was homologous to several serine/threonine and dual specificity protein kinases, while P-CIP10 contained spectrin-like repeats [10].
• Kalirin is a multidomain guanine nucleotide exchange factor for small GTPbinding proteins of the Rho family [6].

Regulatory relationships of Kalrn

• The presence of Thr1590 in each major Kalirin isoform would allow Cdk5 to regulate Kalirin function throughout development [11].

Other interactions of Kalrn

• In mammals, Kalirin is expressed predominantly in the nervous system, whereas Trio, broadly expressed throughout the body, is expressed at a lower level in the nervous system [12].
• Kalirin, a dual Rho GDP-GTP exchange factor, causes spine formation when overexpressed [9].
• Kalirin, a multifunctional Rho guanine nucleotide exchange factor, is necessary for maintenance of hippocampal pyramidal neuron dendrites and dendritic spines [9].

Analytical, diagnostic and therapeutic context of Kalrn

• Northern blot analysis indicates brain-specific expression of Duo [13].
• Western blotting analysis indicated that kalirin-7, the major adult isoform, was a minor component of embryonic kalirin; the main isoform expressed in the embryo was kalirin-9 [14].

References