Microsomal triglyceride transfer protein

From Wikipedia, the free encyclopedia

Identifiers

MTTP; ABL; MTP; MGC149819; MGC149820

External IDs

OMIM: 157147 MGI: 106926 HomoloGene: 212

Gene ontology
Molecular Function:	• lipid transporter activity • lipid binding
Cellular Component:	• soluble fraction • endoplasmic reticulum • microsome
Biological Process:	• lipid metabolic process • lipid transport

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_000253 (mRNA)
NP_000244 (protein)

NM_008642 (mRNA)
NP_032668 (protein)

Location

Chr 4: 100.72 - 100.76 Mb

Chr 3: 138.03 - 138.07 Mb

Pubmed search

[1]

[2]

Microsomal triglyceride transfer protein, also known as MTTP, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: MTTP microsomal triglyceride transfer protein.

[edit] Further reading

Luz JM, Lennarz WJ (1996). "Protein disulfide isomerase: a multifunctional protein of the endoplasmic reticulum.". EXS 77: 97–117. PMID 8856971.
Wetterau JR, Lin MC, Jamil H (1997). "Microsomal triglyceride transfer protein.". Biochim. Biophys. Acta 1345 (2): 136–50. PMID 9106493.
Gordon DA (1997). "Recent advances in elucidating the role of the microsomal triglyceride transfer protein in apolipoprotein B lipoprotein assembly.". Curr. Opin. Lipidol. 8 (3): 131–7. PMID 9211060.
Ye J (2007). "Reliance of host cholesterol metabolic pathways for the life cycle of hepatitis C virus.". PLoS Pathog. 3 (8): e108. doi:10.1371/journal.ppat.0030108. PMID 17784784.
Wetterau JR, Aggerbeck LP, Bouma ME, et al. (1992). "Absence of microsomal triglyceride transfer protein in individuals with abetalipoproteinemia.". Science 258 (5084): 999–1001. PMID 1439810.
Sharp D, Ricci B, Kienzle B, et al. (1994). "Human microsomal triglyceride transfer protein large subunit gene structure.". Biochemistry 33 (31): 9057–61. PMID 7545943.
Shoulders CC, Narcisi TM, Read J, et al. (1995). "The abetalipoproteinemia gene is a member of the vitellogenin family and encodes an alpha-helical domain.". Nat. Struct. Biol. 1 (5): 285–6. PMID 7664034.
Hagan DL, Kienzle B, Jamil H, Hariharan N (1994). "Transcriptional regulation of human and hamster microsomal triglyceride transfer protein genes. Cell type-specific expression and response to metabolic regulators.". J. Biol. Chem. 269 (46): 28737–44. PMID 7961826.
Shoulders CC, Brett DJ, Bayliss JD, et al. (1994). "Abetalipoproteinemia is caused by defects of the gene encoding the 97 kDa subunit of a microsomal triglyceride transfer protein.". Hum. Mol. Genet. 2 (12): 2109–16. PMID 8111381.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
Sharp D, Blinderman L, Combs KA, et al. (1993). "Cloning and gene defects in microsomal triglyceride transfer protein associated with abetalipoproteinaemia.". Nature 365 (6441): 65–9. doi:10.1038/365065a0. PMID 8361539.
Narcisi TM, Shoulders CC, Chester SA, et al. (1996). "Mutations of the microsomal triglyceride-transfer-protein gene in abetalipoproteinemia.". Am. J. Hum. Genet. 57 (6): 1298–310. PMID 8533758.
Rehberg EF, Samson-Bouma ME, Kienzle B, et al. (1997). "A novel abetalipoproteinemia genotype. Identification of a missense mutation in the 97-kDa subunit of the microsomal triglyceride transfer protein that prevents complex formation with protein disulfide isomerase.". J. Biol. Chem. 271 (47): 29945–52. PMID 8939939.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
Linnik KM, Herscovitz H (1998). "Multiple molecular chaperones interact with apolipoprotein B during its maturation. The network of endoplasmic reticulum-resident chaperones (ERp72, GRP94, calreticulin, and BiP) interacts with apolipoprotein b regardless of its lipidation state.". J. Biol. Chem. 273 (33): 21368–73. PMID 9694898.
Bradbury P, Mann CJ, Köchl S, et al. (1999). "A common binding site on the microsomal triglyceride transfer protein for apolipoprotein B and protein disulfide isomerase.". J. Biol. Chem. 274 (5): 3159–64. PMID 9915855.
Wang J, Hegele RA (2000). "Microsomal triglyceride transfer protein (MTP) gene mutations in Canadian subjects with abetalipoproteinemia.". Hum. Mutat. 15 (3): 294–5. doi:10.1002/(SICI)1098-1004(200003)15:3<294::AID-HUMU14>3.0.CO;2-E. PMID 10679949.

This article on a gene on chromosome 4 is a stub. You can help Wikipedia by expanding it.

v • d • e Lipids: lipoprotein metabolism

General	Chylomicron - HDL - LDL - IDL - VLDL - Lp(a)

Apolipoproteins	APOA (1, 2, 5) - APOB - APOC (1, 2, 3, 4) - APOD - APOE - APOH

Other	Lipoprotein lipase - HDL (Cholesterylester transfer protein Acetyl-CoA C-acyltransferase, LCAT) - LDL receptor - Microsomal triglyceride transfer protein - ABCA1 - Lecithin-cholesterol acyltransferase

see also disorders