The human protein disulfide isomerase gene family
<p>Abstract</p> <p>Enzyme-mediated disulfide bond formation is a highly conserved process affecting over one-third of all eukaryotic proteins. The enzymes primarily responsible for facilitating thiol-disulfide exchange are members of an expanding family of proteins known as protein...
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| Format: | Article |
| Language: | English |
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BMC
2012-07-01
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| Series: | Human Genomics |
| Subjects: | |
| Online Access: | http://www.humgenomics.com/content/6/1/6 |
| _version_ | 1817991053302562816 |
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| author | Galligan James J Petersen Dennis R |
| author_facet | Galligan James J Petersen Dennis R |
| author_sort | Galligan James J |
| collection | DOAJ |
| description | <p>Abstract</p> <p>Enzyme-mediated disulfide bond formation is a highly conserved process affecting over one-third of all eukaryotic proteins. The enzymes primarily responsible for facilitating thiol-disulfide exchange are members of an expanding family of proteins known as protein disulfide isomerases (PDIs). These proteins are part of a larger superfamily of proteins known as the thioredoxin protein family (TRX). As members of the PDI family of proteins, all proteins contain a TRX-like structural domain and are predominantly expressed in the endoplasmic reticulum. Subcellular localization and the presence of a TRX domain, however, comprise the short list of distinguishing features required for gene family classification. To date, the <it>PDI</it> gene family contains 21 members, varying in domain composition, molecular weight, tissue expression, and cellular processing. Given their vital role in protein-folding, loss of PDI activity has been associated with the pathogenesis of numerous disease states, most commonly related to the unfolded protein response (UPR). Over the past decade, UPR has become a very attractive therapeutic target for multiple pathologies including Alzheimer disease, Parkinson disease, alcoholic and non-alcoholic liver disease, and type-2 diabetes. Understanding the mechanisms of protein-folding, specifically thiol-disulfide exchange, may lead to development of a novel class of therapeutics that would help alleviate a wide range of diseases by targeting the UPR.</p> |
| first_indexed | 2024-04-14T01:07:00Z |
| format | Article |
| id | doaj.art-3f7372832c15444eb4a2a41e55826e5f |
| institution | Directory Open Access Journal |
| issn | 1479-7364 |
| language | English |
| last_indexed | 2024-04-14T01:07:00Z |
| publishDate | 2012-07-01 |
| publisher | BMC |
| record_format | Article |
| series | Human Genomics |
| spelling | doaj.art-3f7372832c15444eb4a2a41e55826e5f2022-12-22T02:21:11ZengBMCHuman Genomics1479-73642012-07-0161610.1186/1479-7364-6-6The human protein disulfide isomerase gene familyGalligan James JPetersen Dennis R<p>Abstract</p> <p>Enzyme-mediated disulfide bond formation is a highly conserved process affecting over one-third of all eukaryotic proteins. The enzymes primarily responsible for facilitating thiol-disulfide exchange are members of an expanding family of proteins known as protein disulfide isomerases (PDIs). These proteins are part of a larger superfamily of proteins known as the thioredoxin protein family (TRX). As members of the PDI family of proteins, all proteins contain a TRX-like structural domain and are predominantly expressed in the endoplasmic reticulum. Subcellular localization and the presence of a TRX domain, however, comprise the short list of distinguishing features required for gene family classification. To date, the <it>PDI</it> gene family contains 21 members, varying in domain composition, molecular weight, tissue expression, and cellular processing. Given their vital role in protein-folding, loss of PDI activity has been associated with the pathogenesis of numerous disease states, most commonly related to the unfolded protein response (UPR). Over the past decade, UPR has become a very attractive therapeutic target for multiple pathologies including Alzheimer disease, Parkinson disease, alcoholic and non-alcoholic liver disease, and type-2 diabetes. Understanding the mechanisms of protein-folding, specifically thiol-disulfide exchange, may lead to development of a novel class of therapeutics that would help alleviate a wide range of diseases by targeting the UPR.</p>http://www.humgenomics.com/content/6/1/6Disulfide bondThioredoxinCalsequestrinUPRUnfolded protein responseER stress |
| spellingShingle | Galligan James J Petersen Dennis R The human protein disulfide isomerase gene family Human Genomics Disulfide bond Thioredoxin Calsequestrin UPR Unfolded protein response ER stress |
| title | The human protein disulfide isomerase gene family |
| title_full | The human protein disulfide isomerase gene family |
| title_fullStr | The human protein disulfide isomerase gene family |
| title_full_unstemmed | The human protein disulfide isomerase gene family |
| title_short | The human protein disulfide isomerase gene family |
| title_sort | human protein disulfide isomerase gene family |
| topic | Disulfide bond Thioredoxin Calsequestrin UPR Unfolded protein response ER stress |
| url | http://www.humgenomics.com/content/6/1/6 |
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