Disease relevance of MGC127742

• In conclusion, when growing cattle grazing BER were supplemented once daily with grain at approximately 1.0% BW, grain that degraded in the rumen slowly (GC, WC, and SG) resulted in live weight gain greater than that resulting from grain that degraded rapidly (B and W) [1].
• We have isolated a selectively deglycosylated form of vitamin D binding protein (DBP-maf) generated from systemically available DBP by a human pancreatic cancer cell line [2].

High impact information on MGC127742

• In contrast, the lyso-Pc-inducible beta-galactosidase of B cells alone modified mouse DBP to yield the MAF [3].
• These observations led us to conclude that bovine DBP carries a trisaccharide composed of N-acetylgalactosamine, galactose, and sialic acid, whereas mouse DBP carries a disaccharide composed of N-acetylgalactosamine and galactose [3].
• The current study demonstrates that cell replication and matrix protein synthesis are also modulated by vitamin D. Confluent, third-passage growth zone (GC) and resting zone (RC) costochondral chondrocytes were incubated in medium containing 10(-13)-10(-7) M 1,25-(OH)2D3 or 10(-12)-10(-6) M 24,25-(OH)2D3 [4].
• 1,25-(OH)2D3 stimulated CDP and percentage collagen synthesis by GC cells but had no effect on the synthesis of noncollagenous protein (NCP) [4].
• Moreover, we observed that these gene-rich bands are syntenic with the previously identified GC-richest/gene richest H3+ bands of the human chromosomes [5].

Chemical compound and disease context of MGC127742

• Live weight gain was .47, .84, .80, .68, .81, and .51 kg/d for Control, GC, WC, B, SG, and W, respectively (SE = .028) [1].

Biological context of MGC127742

• In particular, RNA polymerase I and topoisomerase I are detected for the first time late during the fourth embryonic cell cycle, which coincides with the first recognition of the DFC, FCs, and GC at the ultrastructural level [6].
• These had a much higher affinity for 24,25(OH)2D3 than that of the vitamin D binding protein (DBP) [7].
• Multi-point linkage analysis indicated that the gene locations were indistinguishable from those of serum albumin (ALB) and vitamin D-binding protein (GC) on bovine Chromosome (BTA) 6 [8].
• Both growth cartilage (GC) cells and resting cartilage (RC) cells were shown to have a single class of saturable, high affinity PTH binding sites with a dissociation constant of 0.6-0.7 nM [9].
• At as low as 0.1 microM, DPP, DBP, BBP, DCHP and DHP significantly inhibited the calcium signaling of human nAChR [10].

Anatomical context of MGC127742

• Ruminal NDF digestion (quadratic, P = .05) and duodenal microbial N flow (quadratic, P < .01) were greatest for 66% SBH/33% GC, whereas total N flow to the duodenum was similar (P > .10) among treatments [11].
• Antirat GC mouse IgG was prepared to label and sort the osteogenic cells in bone marrow by fluorescence-activated cell-sorter II (FACS II) [12].
• Linkage of bovine erythrocyte antigen loci B, C, L, S, Z, R' and T' and the serum protein loci post-transferrin 2 (PTF 2), vitamin D binding protein (GC) and albumin (ALB) to DNA microsatellite markers [13].

Associations of MGC127742 with chemical compounds

• The accumulated evidence suggests that lyso-Pc-inducible beta-galactosidase of B lymphocytes and the Neu-1 sialidase of T lymphocytes modified the bovine serum vitamin D3-binding protein (DBP) to yield the MAF, a protein with N-acetylgalactosamine as the remaining sugar [3].
• Addition of forskolin and IBMX to increase cAMP increased ALPase in GC cultures to a level similar to that seen after addition of PTH(1-34) [14].
• The great difference in competition of palmitic and arachidonic acids with 25-hydroxycholecalciferol may be related to changes in DBP conformation promoted by the binding of different ligands [15].
• Strongest to weakest potencies were observed as DPP --> BBP --> DBP --> DCHP --> DHP --> DPrP --> DEHP --> DEP [16].
• DPP, DBP, and BBP were 10 times more potent than estradiol [16].

Analytical, diagnostic and therapeutic context of MGC127742

• HPLC isolation of the presumptive e-beta Hyn residue from enzyme digests of intact C1r allowed confirmation of its structure by GC/MS [17].
• Fluorescence titration did not indicate binding of S1 to actin in complex with gelsolin segment 1 (G1) or vitamin D-binding protein (DBP) [18].
• Then we identified, by in situ hybridization of the GC-richest H3 isochores, the pig chromosomal regions endowed by the highest gene-density that largely corresponded to the telomeric chromosomal bands [5].
• These results demonstrated that the Ab3 are promising for developing an immunoassay system which is much more specific and sensitive than conventional competitive protein binding assays based on DBP [7].
• The cultured GC cells showed remarkable osteogenic potential only with the participation of certain host cells even after cultivation, while RC cells showed no osteogenic activity when transplanted as isografts loaded into Millipore chambers [12].

References