Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex.

Wetterau, John R.; Combs, Kelly A.; Spinner, Sara N.; Joiner, B.

doi:10.1016/s0021-9258(19)38742-3

Cited by 332 publications

(67 citation statements)

References 36 publications

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“…Wetterau, Sharp, Shoulders et al (4 -6) have delineated that ABL is caused by molecular abnormalities in microsomal triglyceride transfer protein (MTP). MTP forms a heterodimer with protein disulfide isomerase (PDI), an ubiquitous endoplasmic reticulum (ER) resident protein involved in disulfide bond formation (7) and functions in the assembly of apoB-containing lipoproteins. Without MTP, as in the case of ABL, apoB is unable to be properly lipidated and undergoes rapid presecretory degradation (8)(9)(10)(11).…”

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confidence: 99%

Novel mutations in the microsomal triglyceride transfer protein gene causing abetalipoproteinemia

Ohashi

Ishibashi

Osuga

et al. 2000

Journal of Lipid Research

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Abetalipoproteinemia (ABL) is an inherited disease characterized by the virtual absence of apolipoprotein B (apoB)-containing lipoproteins from plasma. Only limited numbers of families have been screened for mutations in the microsomal triglyceride transfer protein (MTP) gene. To clarify the genetic basis of clinical diversity of ABL, mutations of the MTP gene have been screened in 4 unrelated patients with ABL. Three novel mutations have been identified: a frameshift mutation caused by a single adenine deletion at position 1389 of the cDNA, and a missense mutation, Asn780Tyr, each in homozygous forms; and a splice site mutation, 2218-2A ¨ G, in a compound heterozygous form. The frameshift and splice site mutations are predicted to encode truncated forms of MTP. When transiently expressed in Cos-1 cells, the Asn780Tyr mutant MTP bound protein disulfide isomerase (PDI) but displayed negligible MTP activity. It is of interest that the patient having the Asn780Tyr mutation, a 27-year-old male, has none of the manifestations characteristic of classic ABL even though his plasma apoB and vitamin E were virtually undetectable. These results indicated that defects of the MTP gene are the proximal cause of ABL.

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confidence: 99%

Novel mutations in the microsomal triglyceride transfer protein gene causing abetalipoproteinemia

Ohashi

Ishibashi

Osuga

et al. 2000

Journal of Lipid Research

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“…For example, PDI is a permanent structural subunit of two important ER‐located enzymes, prolyl 4‐hydroxylase (P4H) [ 17,18 ] and microsomal triglyceride transfer protein (MTP). [ 19 ] P4H is an α 2 β 2 heterotetramer, [ 20 ] and MTP is an αβ heterodimer. [ 19,21 ] In both cases, the functional sites are located in the α subunits, with PDI serving as the β‐subunits.…”

Section: Introduction: An Overview Of Protein Disulfide Isomerase (Pdi)mentioning

confidence: 99%

“…[ 19 ] P4H is an α 2 β 2 heterotetramer, [ 20 ] and MTP is an αβ heterodimer. [ 19,21 ] In both cases, the functional sites are located in the α subunits, with PDI serving as the β‐subunits. In these complexes, PDI acts as a undissociated molecular chaperone that is critical for the assembly and stability of the complex.…”

Section: Introduction: An Overview Of Protein Disulfide Isomerase (Pdi)mentioning

confidence: 99%

Protein disulfide isomerase is regulated in multiple ways: Consequences for conformation, activities, and pathophysiological functions

Wang

2020

BioEssays

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Protein disulfide isomerase (PDI) is one of the most abundant and critical protein folding catalysts in the endoplasmic reticulum of eukaryotic cells. PDI consists of four thioredoxin domains and interacts with a wide range of substrate and partner proteins due to its intrinsic conformational flexibility. PDI plays multifunctional roles in a variety of pathophysiological events, both as an oxidoreductase and a molecular chaperone. Recent studies have revealed that the conformation and activity of PDI can be regulated in multiple ways, including posttranslational modification and substrate/ligand binding. Here, we summarize recent advances in understanding the function and regulation of PDI in different pathological and physiological events. We propose that the multifunctional roles of PDI are regulated by multiple mechanisms. Furthermore, we discuss future directions for the study of PDI, emphasizing how different regulatory modes are linked to the conformational changes and biological functions of PDI in the context of diverse pathophysiologies.

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“…The assembly of apolipoprotein B (apoB) with lipids to form hepatic triglyceride-rich VLDL requires the dedicated cofactor microsomal triglyceride transfer protein (MTP) (1). MTP is composed of a 97-kDa unique subunit complexed with the ubiquitous endoplasmic reticulum (ER)-localized folding enzyme protein disulfide isomerase (2). Although the complete dimensions of its functional roles in VLDL formation are not fully understood, MTP may transfer lipids to apoB during its translation and translocation into the ER and may participate in the posttranslational enlargement of nascent VLDL particles (3 -7).…”

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confidence: 99%

Lipoprotein assembly capacity of the mammary tumor-derived cell line C127 is due to the expression of functional microsomal triglyceride transfer protein

Sellers

Shelness

2001

Journal of Lipid Research

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C127, a murine mammary tumor-derived cell line, is capable of lipidating and secreting apolipoprotein B-41 (apoB-41) in the apparent absence of microsomal triglyceride transfer protein (MTP). Using a semiquantitative reverse transcriptase-coupled polymerase chain reaction, mouse MTP mRNA was detected in C127 cells at ϳ 10-20% of the relative abundance of human MTP in HepG2 cells. Radiolabeling of C127 cells with [ 35 S]methionine and [ 35 S]cysteine followed by immunoprecipitation with anti-MTP antibodies identified a band with an electrophoretic mobility identical to that of authentic mouse MTP. Cotransfection of apoB-41 and the MTP 97-kDa subunit in C127 cells enhanced apoB secretion by ϳ 5-fold relative to apoB-41 transfection alone, suggesting that MTP is limiting in these cells. To establish that MTP expression is responsible for apoBcontaining lipoprotein assembly in C127 cells, the effects of the MTP inhibitor BMS-200150 were examined. Secretion of apoB-41 by C127 cells was inhibited to the same extent observed in COS-1 cells cotransfected with apoB-41 and MTP. These results suggest that low MTP expression, and not the expression or overexpression of another known or novel factor(s), is responsible for apoB assembly and secretion in C127 cells and further supports the essential nature of MTP in the biogenesis of apoB-containing lipoproteins. -Sellers, J. A., and G. S. Shelness. Lipoprotein assembly capacity of the mammary tumor-derived cell line C127 is due to the expression of functional microsomal triglyceride transfer protein.

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Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex.

Cited by 332 publications

References 36 publications

Novel mutations in the microsomal triglyceride transfer protein gene causing abetalipoproteinemia

Novel mutations in the microsomal triglyceride transfer protein gene causing abetalipoproteinemia

Protein disulfide isomerase is regulated in multiple ways: Consequences for conformation, activities, and pathophysiological functions

Lipoprotein assembly capacity of the mammary tumor-derived cell line C127 is due to the expression of functional microsomal triglyceride transfer protein

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