Disease relevance of Myh10

• Expression of the contractile protein isoforms, especially SMemb, should serve as a new marker for the subsequent glomerular hypertrophy and sclerosis [1].
• In the anti-GBM nephritis rats, SMemb expression was increased in epithelial cells [2].
• However, the expression profile was shifted from alpha-SM actin to SMemb dominant pattern over the course of glomerulonephritis [2].
• CONCLUSIONS: In rats with PAN nephrosis, findings suggest that restriction of dietary protein leads to a reduction in glomerular SMemb expression [3].
• In contrast, glomerular SMemb mRNA increased on days 2 and 4 (before and soon after the onset of proteinuria, respectively), but declined on day 8 (the peak of proteinuria) [4].

High impact information on Myh10

• These SMemb-positive cells were activated fibroblasts or myofibroblasts [5].
• In the coronary arteries of chronically rejected allografts, enhanced SMemb and reduced SM2 expression was observed in both thickened intima and media [5].
• SMemb was expressed in spindle-shaped cells located in acutely rejected myocardium in the rats and monkeys [5].
• Increased expression of SMemb at the mRNA and protein levels was demonstrated at 1 week after STZ administration in the rat [1].
• Immunological analyses and reverse transcriptase-polymerase chain reaction indicated that the differentiated cells expressed smooth-muscle-specific marker proteins such as SM-1, SM-2, and SMemb myosin heavy chains, SM-22, basic calponin and alpha-smooth-muscle actin, but not the astrocyte marker glial fibrillary acidic protein [6].

Chemical compound and disease context of Myh10

• 1. We investigated the glomerular expression of three types of myosin heavy-chain isoforms, including S-myosin heavy-chain 40 (SM1), S-myosin heavy-chain 29 (SM2) and FS-myosin heavy-chain 34 (SMemb) in puromycin aminonucleoside nephrosis [4].
• The SMemb isoform was barely detectable in normal glomeruli, but substantial amounts of SMemb were demonstrated in the glomeruli of rats with puromycin aminonucleoside nephrosis [4].
• These data suggest that SMemb is a molecular marker for phenotypic alteration and that the beneficial effect of enalapril on proteinuria and renal function may be, at least in part, associated with reducing SMemb mRNA expression in diabetic glomeruli [7].

Biological context of Myh10

• Molecular cloning and functional analysis of the promoter region of rat nonmuscle myosin heavy chain-B gene [8].
• In both control and CDH groups, SMemb expression was positive from 16 days' gestation [9].
• Myosin heavy chain (MHC) isoforms such as SMemb, SM1 and SM2 are important molecular markers used to study vascular smooth muscle cell differentiation [9].
• Compared to the vehicle-treated SHRSP group, both drugs significantly and equally shifted the aortic SMC phenotype in SHRSP toward the differentiated state by reducing NMHC-B/SMemb and increasing SM2 [10].
• Two isoforms of nonmuscle myosin heavy chain IIB (MHC-IIB) are generated by alternative splicing; MHC-IIB(B2) differs from MHC-IIB(DeltaB2) by the insertion of B2 exon cassette near the actin binding region [11].

Anatomical context of Myh10

• CONCLUSION: All induced a phenotypic alteration in mesangial cells, enhanced the mesangial expression of SMemb and stimulated the fibronectin synthesis [12].
• SMemb is predominantly expressed in immature smooth muscle cells (SMC), and SM2 is expressed in mature SMCs [9].
• The expression of SMemb was also increased in epithelial cells in this model [2].
• In the aortas of vehicle-treated SHRSP, the level of contractile-type smooth muscle (SM) myosin heavy chain (MHC) SM2 was significantly lower, whereas the level of synthetic-type MHC NMHC-B/SMemb was significantly higher compared with those in the WKY aortas [10].
• In normotensive Wistar-Kyoto rats, alpha-smooth muscle actin was not expressed in any glomerular cells and a non-muscle myosin heavy chain isoform, SMemb, was slightly expressed in glomerular visceral epithelial cells [13].

Associations of Myh10 with chemical compounds

• On the other hand, hydralazine did not change the glomerular expression of SMemb enhanced by AII administration [12].
• Angiotensin II enhances glomerular expression of a nonmuscle myosin heavy chain, SMemb, with extracellular matrix accumulation [12].
• In the puromycin aminonucleoside-treated rats, the number of SMemb-positive glomerular cells increased on days 2 and 4 [4].
• However, methylprednisolone did not affect SMemb mRNA or immunostaining in a glomeruli of rats with puromycin aminonucleoside nephrosis.(ABSTRACT TRUNCATED AT 250 WORDS)[4]
• However, enalapril had no effect on SMemb mRNA levels in controls [7].

Regulatory relationships of Myh10

• Northern blot analysis revealed increased mRNA levels of SMemb both in aorta-constricted rat hearts and in cultured cardiac fibroblasts stimulated by TGF-beta1 or by mechanical stretch [14].

Other interactions of Myh10

• Thus, we investigated the effect of AII on the mesangial expression of SMemb and synthesis of fibronectin [12].

Analytical, diagnostic and therapeutic context of Myh10

• RESULTS: Semiquantitative immunohistochemical evaluation and Western blot analysis showed that AII significantly enhanced glomerular expression of SMemb (0.87 +/- 0.33 vs. 0.40 +/- 0.19 for immunohistochemical grading, p < 0.05; 2.55 +/- 0.88 vs. 1.16 +/- 0.75 for Western blot analysis, p < 0.05) [12].
• In all models examined, mesangial and epithelial expression of SMemb was confirmed by immunoelectron microscopy, and enhanced expression of SMemb mRNA in glomeruli was verified by RNase protection assay [2].
• However, the low-protein diet did not affect SMemb mRNA and protein levels in the glomeruli of control rats [3].
• To evaluate the role of SMemb in the development of kidney rejection, we examined its expression in rat kidney transplantation models [15].
• In Northern blot analysis, SMemb mRNA was not detected in control glomeruli, whereas it was transiently upregulated in glomeruli on day 48 in rats with focal glomerulosclerosis [16].

References