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promotes assembly and secretion of human apolipoprotein B (show APOB Proteins)
the phospholipid transfer activity of MTP is sufficient for the assembly and secretion of primordial apoB (show APOB Proteins) lipoproteins
analysis of developmental expression and nutritional regulation of zebrafish homolog to mammalian microsomal triglyceride transfer protein large subunit
In a genetic study of lipid transport and metabolism, larval levels of microsomal triglyceride transfer protein (Mtp), the protein responsible for packaging triacylglycerol and beta-lipoproteins into lipoprotein particles, are unchanged by feeding.
MTTP is regulated by apo A-IV in manner to promote increased packaging of triglyceride into chylomicron core, which may be important in neonatal fat absorption.
There appears to be an interaction between the porcine MTTP genotype and the type of fat source in the pig diet, which would agree with the previous results on the biology of MTTP biology.
Nonesterified fatty acids significantly inhibit the expression of ApoB100 (show APOB Proteins), ApoE (show APOE Proteins), MTP, and LDLR (show LDLR Proteins), thereby decreasing the synthesis and assembly of VLDL and inducing TG accumulation in bovine hepatocytes.
after calving the apolipoprotein B(100 (show APOB Proteins)) mRNA synthesis was lower, whereas microsomal triglyceride transfer protein (MTP) and apolipoprotein E (show APOE Proteins) messenger RNA abundance were higher in the liver
measurements of the transfer of phospholipids (PLs (show CTSC Proteins)) and cholesteryl esters (CEs)to acceptor vesicles by purified MTP showed TAG transfer activity was the most robust, and CE and PL transfer activities were 60-71% and 5-13% of the TAG transfer activity
Fasting upregulates Fpn1 (show SLC40A1 Proteins) expression in spleen and peritoneal macrophages, probably via a ghrelin (show GHRL Proteins)/GHSR1a/MAPK (show MAPK1 Proteins) signaling pathway.
Microsomal triglyceride transfer protein protein plays a critical role in lipid droplet maturation, but does not regulate total body fat accumulation.
Expression of Hepcidin (show HAMP Proteins) and Ferroportin (show SLC40A1 Proteins) in the Placenta, and Ferritin (show FTL Proteins) and Transferrin Receptor 1 (show TFR Proteins) Levels in Maternal and Umbilical Cord Blood in Pregnant Women with and without Gestational Diabetes
findings show that ferroportin (show SLC40A1 Proteins) expression by macrophages at the site of injury represents a requirement for appropriate activation of myogenic precursors and eventual healing of injured skeletal muscle
data provide the first in vivo evidence of the transcriptional regulatory activity of beta-apocarotenoids and identify microsomal triglyceride transfer protein and its transcription factors as the targets of their action. This study demonstrates that beta-carotene induces a feed-forward mechanism in the placenta to enhance the assimilation of beta-carotene for proper embryogenesis.
The results suggest that physiologic hepcidin (show HAMP Proteins) levels are insufficient to alter Fpn levels within the retinal pigment epithelium and Muller cells, but may limit iron transport into the retina from vascular endothelial cells.
PHARMACOLOGICAL STUDY OF NEW COMPOUNDS ACTING AS REGULATORS OF 18-KDA TRANSLOCATOR PROTEIN (show TSPO Proteins) LIGANDS
In Angiotensin II treated mice, duodenal divalent metal transporter-1 (show SLC11A2 Proteins) and ferroportin (show SLC40A1 Proteins) expression levels were increased and hepatic hepcidin (show HAMP Proteins) mRNA expression and serum hepcidin (show HAMP Proteins) concentration were reduced.
Intestine-specific MTP (show LAPTM4A Proteins) and global ACAT2 (show SOAT2 Proteins) deficiency lowers acute cholesterol absorption with chylomicrons and HDLs (show CSF1R Proteins)
Mice infected with Salmonella typhimurium have increased duodenal expression of the iron exporter ferroportin-1 (show SLC40A1 Proteins), consistent with increased uptake of dietary iron.
two new hypolipidemic patients with very low plasma triglyceride and apolipoprotein B (apoB (show APOB Proteins)) levels with plasma lipid profiles similar to abetalipoproteinemia (ABL (show ABL1 Proteins)) patients, are reported.
results of this study, examining a cohort of obese children, suggest that the genetic variation at MTTP rs2306986 was associated with higher susceptibility to NAFLD
Data suggest that amphipathic beta-strands in 200 N-terminal residues of beta1 domain of APOB (show APOB Proteins) are required for secretion of lipid-rich or lipid-poor particles; residues 300-700 or 1050-1500 of beta1 domain appear to be required for secretion of lipid-rich particles; MTTP is required for secretion of intact APOB (show APOB Proteins) but not of truncated APOB (show APOB Proteins). (APOB (show APOB Proteins) = apolipoprotein B (show APOB Proteins); MTTP = microsomal triglyceride transfer protein)
In chronic hepatitis C patients infected with HCV genotype 3 and with the TT/GT genotype of the MTTP -493G/T SNP, a significant increase in hepatic steatosis was observed, which may indicate that this SNP has a significant influence on the accumulation of triglycerides in hepatocytes.
High expression of MTTP is associated with high carotid intima-media thickness.
MTP (show MT1B Proteins) Gene Variants are associated with Homozygous Familial Hypercholesterolemia.
the N-terminal domain of MTP (show MT1B Proteins) is important for its lipid transfer activity
These studies indicated that SAP18 (show SAP18 Proteins) expression enhanced the recruitment of mSin3A in coordination with TRIB1 (show TRIB1 Proteins) to MTTP regulatory elements and increased MTTP expression.
Results present evidence that MTTP polymorphisms could modulate the lipid homeostasis to determine the serum lipids and increase risk of non-alcoholic fatty liver disease.
Findings from meta-analysis indicate that the MTP (show MT1B Proteins) -493G/T polymorphism may contribute to the development of non-alcoholic fatty liver disease. Thus, the MTP (show MT1B Proteins) -493G/T polymorphism may be a biomarker for the early detection of the disease.
MTP encodes the large subunit of the heterodimeric microsomal triglyceride transfer protein. Protein disulfide isomerase (PDI) completes the heterodimeric microsomal triglyceride transfer protein, which has been shown to play a central role in lipoprotein assembly. Mutations in MTP can cause abetalipoproteinemia.
microsomal triacylglycerol transfer protein
, microsomal triglyceride transfer protein
, microsomal triglyceride transfer protein large subunit
, microsomal triglyceride transfer protein (large polypeptide, 88kDa)
, microsomal triglyceride transfer protein B
, microsomal triglyceride transfer protein, large subunit
, SLC11A3 iron transporter
, ferroportin 1
, iron-regulated transporter 1
, metal transporter protein 1
, metal transporting protein 1
, solute carrier family 11 (proton-coupled divalent metal ion transporters), member 3
, solute carrier family 39 (iron-regulated transporter), member 1
, solute carrier family 40 member 1