Disease relevance of Smc1l1

• These results indicate that SMC is a novel product of normal mammary gland and milk, which is post-transcriptionally regulated by transforming growth factor beta in normal mammary gland, but not in 13762 mammary adenocarcinoma cells [1].
• SMC is highly expressed on the surface of ascites 13762 rat mammary adenocarcinoma cells, approximately 100 times the level in lactating mammary gland and 10(4) times that in virgin mammary gland [1].

High impact information on Smc1l1

• We found that the promyogenic SRF coactivator myocardin increased SRF association with methylated histones and CArG box chromatin during activation of SMC gene expression [2].
• Serum response factor (SRF) controls SMC gene transcription via binding to CArG box DNA sequences found within genes that exhibit SMC-restricted expression [2].
• Here we report that SMC-restricted binding of SRF to murine SMC gene CArG box chromatin is associated with patterns of posttranslational histone modifications within this chromatin that are specific to the SMC lineage in culture and in vivo, including methylation and acetylation to histone H3 and H4 residues [2].
• Up-regulation of the Muc4/SMC gene in the 13762 sublines of the rat mammary adenocarcinoma correlates with the overexpression of transcription factor PEA3 and the receptor tyrosine kinase ErbB2 [3].
• These data suggest that expression of PEA3 in mammary tumors leads to up-regulation of Muc4/SMC transcription, the gene product of which may contribute to the metastatic potential of mammary tumors [3].

Chemical compound and disease context of Smc1l1

• Sialomucin complex (SMC/rat Muc4) is a heterodimeric glycoprotein complex composed of an anti-adhesive mucin subunit ascites sialoglycoprotein (ASGP)-1 and a transmembrane subunit ASGP-2 [4].

Biological context of Smc1l1

• Immunofluorescence analysis of testis sections showed intense chromatin association in meiotic prophase cells, weaker staining in round spermatids and absence of the SMC proteins in elongated spermatids [5].
• Here we report that PEA3 is capable of transactivating the Muc4/SMC promoter in a dose-dependent manner via direct attachment to a PEA3 binding site [3].
• SMC expression at the uterine luminal surface, but not in glandular epithelium, is hormonally regulated and varies with the estrous cycle [6].
• The stirred culture of SMC-seeded polymer matrices resulted in tissues with a cell density of 6.4 +/- 0.8 x 10(8) cells/cm3 after 5 weeks, compared to 2.0 +/- 1.1 x 10(8) cells/cm3 with static culture [7].
• Increased progesterone levels lead to downregulation of SMC in the uterine luminal epithelium at the time of receptivity for implantation [4].

Anatomical context of Smc1l1

• Both SMC proteins are present in rat spermatocytes and enriched in preparations of synaptonemal complexes [5].
• Its transcript is present in both virgin and pregnant mammary tissue, and SMC synthesis is induced rapidly in cultured primary mammary epithelial cells from either normal pregnant or virgin rats [1].
• SMC protein, but not transcript, levels are significantly reduced when mammary cells are cultured in Matrigel, a reconstituted basement membrane which stimulates casein expression [1].
• SMC is also downregulated when RULEC are co-cultured with isolated uterine stromal cells [6].
• RESULTS: Northern blot analyses of rat lacrimal glands, with a probe for SMC/Muc4, demonstrated the presence of a approximately 9-kb transcript, consistent with observations in other tissues [8].

Associations of Smc1l1 with chemical compounds

• SMC is lost from the luminal uterine surface at the period of receptivity [6].
• Analyses of SMC regulation in hormone-responsive primary cultures of rat uterine luminal epithelial cells (RULEC) demonstrated robust SMC expression by the RULEC, which is not altered by treatments with estrogen or progesterone [6].
• This study reports on the effects of SM cell (SMC) seeding and culture conditions on the cellularity and composition of SM tissues engineered using biodegradable matrices (5 x 5 mm, 2-mm thick) of polyglycolic acid (PGA) fibers [7].
• Neither pyruvate formation nor mutagenicity were observed with SMC [9].
• To date little is known about the molecular enzymology of this reaction but a previous investigation revealed that rat activated phenylalanine 4-monooxygenase (PAH) could S-oxidise both Met- and S-methyl-L-cysteine (SMC) to their S-oxide metabolites [10].

Regulatory relationships of Smc1l1

• Studies on primary rat uterine luminal epithelial cells showed that both SMC protein and transcript are downregulated by TGF-beta1, although SMC expression is not altered by treatments with oestrogen or progesterone [4].

Other interactions of Smc1l1

• However, both SMC protein and transcript are downregulated by transforming growth factor-beta (TGF-beta1) [6].

Analytical, diagnostic and therapeutic context of Smc1l1

• Sequential immunoprecipitation and immunoblot were performed to analyze complexes of the SMC/Muc4 and ErbB2 in the lacrimal tissue [8].

References