Disease relevance of Mtpn

• Knowledge of the changes that take place as a result of overexpression of myotrophin at both the cellular and molecular levels will suggest novel strategies for treatment to prevent hypertrophy and its progression to heart failure [1].
• Our data show that overexpression of myotrophin results in initiation of cardiac hypertrophy that progresses to heart failure, similar to changes in human heart failure [1].
• Attempts to show that V-1 produced in Escherichia coli could induce the cardiac myocyte hypertrophy ascribed to myotrophin were unsuccessful [2].
• The ability of anti-PC Abs using H chains other than the V1 H chain to protect against pneumococcal infection remains controversial [3].
• Medulloblastoma tumorigenesis diverges from cerebellar granule cell differentiation in patched heterozygous mice [4].

High impact information on Mtpn

• The anti-PC Abs in V1(-/-) mice were heteroclitic, binding to nitrophenyl-PC better than to PC [3].
• None of nine hybridomas produced from V1(-/-) mice provided passive protection [3].
• Math1 controls cerebellar granule cell differentiation by regulating multiple components of the Notch signaling pathway [5].
• Mouse cerebellar granule cell differentiation: electrical activity regulates the GABAA receptor alpha 6 subunit gene [6].
• (The ostensibly 'normal' meander tail posterior lobe also benefited from repletion of a more subtle granule cell deficiency.) Donor-derived neurons were well-integrated within the neuropil, suggesting that these progenitors' developmental programs for granule cell differentiation were unperturbed [7].

Chemical compound and disease context of Mtpn

• Structural proteins V1, V2 and V3 of Japanese encephalitis virus (JEV) were isolated and purified by means of polyacrylamide gel electrophoresis (PAGE) in the presence of sodium dodecyl sulfate (SDS) and extracted from the sliced gel [8].

Biological context of Mtpn

• Inhibition of Mtpn by small interfering (si)RNA mimicked the effects of miR-375 on glucose-stimulated insulin secretion and exocytosis [9].
• Thus, our results suggest that V-1 is a novel component that regulates the dynamics of actin polymerization by interacting with CP and thereby participates in a variety of cellular processes such as actin-driven cell movements and motility during neuronal development [10].
• Myotrophin (whose gene is localized on human chromosome 7q33) stimulates myocyte growth and participates in cellular interaction that initiates cardiac hypertrophy in vitro [1].
• Myotrophin induces early response genes and enhances cardiac gene expression [11].
• Our data suggested that myotrophin appears to be a primary modulator for myocardial cell growth and differentiation and may play an important role in the pathogenesis of cardiac hypertrophy [11].

Anatomical context of Mtpn

• The V-1.CP complex was detected not only in cultured cells transfected with the V-1 cDNA but also endogenously in cells as well as in murine cerebellar extracts [10].
• In situ hybridization histochemistry revealed that the expression of the V-1 gene is transiently increased in postmigratory granule cells during postnatal rat cerebellar development and thereafter is markedly suppressed, whereas Purkinje cells constitutively express V-1 mRNA [12].
• When rat neonatal cardiac myocytes maintained in culture were incubated with myotrophin for 30 minutes, they showed a marked increase in c-myc, c-fos, and c-jun messenger RNA levels [11].
• Myotrophin may be involved in the upregulation of myofibrillar protein and the activation of cardiac gene transcription during growth and hypertrophy of the myocardium, and the induction of early response gene expression may be linked to this response [11].
• In the present study we examined the distribution of V-1 mRNA in the murine central nervous system (CNS) [13].

Other interactions of Mtpn

• The amino acid (aa) sequence of rat V-1, a developmentally regulated brain protein, was used to isolate clones encoding mouse V-1, a protein of 118 aa, from an embryoid body cDNA library [2].
• In comparison with our previous data obtained in another mutant, staggerer, we discussed the effects of target deprivation on the expression of V-1 mRNA in cerebellar granule cells [13].
• Although Ptc+/- mouse medulloblastomas express neurodevelopmental genes, they diverge from granule cell differentiation in their discordant coexpression of postmitotic markers despite their ongoing growth [4].
• To gain insights into mechanisms that underlie the formation of this laminar structure, we studied mice deficient for BETA2/NeuroD, a basic helix-loop-helix transcription factor essential for granule cell differentiation [14].
• The time course of their expression suggest, that these NMDA receptor subtypes may contribute to specific aspects of granule cell differentiation in the cerebellum [15].

Analytical, diagnostic and therapeutic context of Mtpn

• An analysis of the V-1/CP interaction by surface plasmon resonance spectroscopy showed that V-1 formed a stable complex with the CP heterodimer with a dissociation constant of 1.2 x 10(-7) m and a molecular stoichiometry of approximately 1:1 [10].
• Co-immunoprecipitation studies reveal that myotrophin/V-1 interacts with NFkappaB proteins in vitro; however, it remains physically associated only with p65 and c-Rel proteins in vivo during NFkappaB activation [16].
• Analysis of DNA by Southern blot hybridization revealed that none of the hybridomas utilized the T15 V1 gene segment, nor did they share use of a common VDJ gene product [17].

References