A Ca<sup>2+</sup>-Calmodulin-Dependent Protein Kinase II Inhibitor Suppresses Cell Migration of CD38-Expressing Human Embryonic Kidney Cells: A Preliminary Report

Hashii, Minako; Tanaka, Yukië; Higuchi, Yoshinori; Gabata, Ryosuke; Tsubomoto, Makoto; Iwatsuka, Noriko; Teramachi, Mitsuyo; Kamijima, Taiki; Yokoyama, Shigeru; Matsukawa, Shigeru; Higashida, Haruhiro

doi:10.1166/msr.2018.1064

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“…The molecular weight of CD38 bound to CAMKIIβ in HEK cells is lower than that of glycosylated CD38 [56]. It was reported that type III CD38 is not usually glycosylated [63].…”

Section: Binding Of Cd38 To Calcium Calmodulin-dependent Kinasementioning

confidence: 89%

“…CD38 produces Ca 2+ -mobilizing second messengers via its catalytic site [3]. With respect to molecular mechanisms of enzyme activity modulation, we recently detected CD38-interacting proteins by proteomic analysis using two-dimensional gel electrophoresis followed by mass spectrometry [56]. We identified the β-isoform of Ca 2+ -calmodulin-dependent protein kinase II (CAMKII) as the human CD38 (hCD38)-binding protein from HEK-293 cells overexpressing hCD38 ( Figure 2).…”

Section: Binding Of Cd38 To Calcium Calmodulin-dependent Kinasementioning

confidence: 99%

“…The corresponding portions of "Chain A, crystal structure of CAMKIIβ isoform 1" (CAMK IiB isoform 1) and isoform CRA_A are marked as blue and green bars, respectively. The numbers 1-3 and 4 indicate the domains of CAMKIIβ at which CD38 binds, and sequences of four tryptic peptides of CAMKIIβ identified by MALDI-TOF/MS, respectively.Pharmacological methods confirmed the functional interaction of CAMKIIβ and CD38[56].Briefly, in human influenza hemagglutinin (HA)-CD38 complementary DNA (cDNA)-transfected human embryonic kidney (HEK) culture cells, the wound open space surrounded with a healing border became small after 24 h. The transfected cells treated with an inhibitor of CAMKII, KN-62, did not close the open space without wound healing…”

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confidence: 97%

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CD38, CD157, and RAGE as Molecular Determinants for Social Behavior

Higashida

Hashii

Tanaka

et al. 2019

Cells

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Recent studies provide evidence to support that cluster of differentiation 38 (CD38) and CD157 meaningfully act in the brain as neuroregulators. They primarily affect social behaviors. Social behaviors are impaired in Cd38 and Cd157 knockout mice. Single-nucleotide polymorphisms of the CD38 and CD157/BST1 genes are associated with multiple neurological and psychiatric conditions, including autism spectrum disorder, Parkinson’s disease, and schizophrenia. In addition, both antigens are related to infectious and immunoregulational processes. The most important clues to demonstrate how these molecules play a role in the brain are oxytocin (OT) and the OT system. OT is axo-dendritically secreted into the brain from OT-containing neurons and causes activation of OT receptors mainly on hypothalamic neurons. Here, we overview the CD38/CD157-dependent OT release mechanism as the initiation step for social behavior. The receptor for advanced glycation end-products (RAGE) is a newly identified molecule as an OT binding protein and serves as a transporter of OT to the brain, crossing over the blood–brain barrier, resulting in the regulation of brain OT levels. We point out new roles of CD38 and CD157 during neuronal development and aging in relation to nicotinamide adenine dinucleotide+ levels in embryonic and adult nervous systems. Finally, we discuss how CD38, CD157, and RAGE are crucial for social recognition and behavior in daily life.

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“…The molecular weight of CD38 bound to CAMKIIβ in HEK cells is lower than that of glycosylated CD38 [56]. It was reported that type III CD38 is not usually glycosylated [63].…”

Section: Binding Of Cd38 To Calcium Calmodulin-dependent Kinasementioning

confidence: 89%

Section: Binding Of Cd38 To Calcium Calmodulin-dependent Kinasementioning

confidence: 99%

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confidence: 97%

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