Post-translationally Abnormal Collagens of Prolyl 3-Hydroxylase-2 Null Mice Offer a Pathobiological Mechanism for the High Myopia Linked to Human LEPREL1 Mutations
Myopia, the leading cause of visual impairment worldwide, results from an increase in the axial length of the eyeball. Mutations in LEPREL1, the gene encoding prolyl 3-hydroxylase-2 (P3H2), have recently been identified in individuals with recessively inherited nonsyndromic severe myopia. P3H2 is a...
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Published in | The Journal of biological chemistry Vol. 290; no. 13; pp. 8613 - 8622 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
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Elsevier Inc
27.03.2015
American Society for Biochemistry and Molecular Biology |
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Abstract | Myopia, the leading cause of visual impairment worldwide, results from an increase in the axial length of the eyeball. Mutations in LEPREL1, the gene encoding prolyl 3-hydroxylase-2 (P3H2), have recently been identified in individuals with recessively inherited nonsyndromic severe myopia. P3H2 is a member of a family of genes that includes three isoenzymes of prolyl 3-hydroxylase (P3H), P3H1, P3H2, and P3H3. Fundamentally, it is understood that P3H1 is responsible for converting proline to 3-hydroxyproline. This limited additional knowledge also suggests that each isoenzyme has evolved different collagen sequence-preferred substrate specificities. In this study, differences in prolyl 3-hydroxylation were screened in eye tissues from P3h2-null (P3h2n/n) and wild-type mice to seek tissue-specific effects due the lack of P3H2 activity on post-translational collagen chemistry that could explain myopia. The mice were viable and had no gross musculoskeletal phenotypes. Tissues from sclera and cornea (type I collagen) and lens capsule (type IV collagen) were dissected from mouse eyes, and multiple sites of prolyl 3-hydroxylation were identified by mass spectrometry. The level of prolyl 3-hydroxylation at multiple substrate sites from type I collagen chains was high in sclera, similar to tendon. Almost every known site of prolyl 3-hydroxylation in types I and IV collagen from P3h2n/n mouse eye tissues was significantly under-hydroxylated compared with their wild-type littermates. We conclude that altered collagen prolyl 3-hydroxylation is caused by loss of P3H2. We hypothesize that this leads to structural abnormalities in multiple eye tissues, but particularly sclera, causing progressive myopia.
Background: Mutations in LEPREL1, the gene encoding prolyl 3-hydroxylase-2 (P3H2), cause severe nonsyndromic myopia.
Results: Collagens I and IV from P3h2-null mouse eye tissues were significantly reduced in 3-hydroxylation compared with wild-type littermates.
Conclusion: Loss of P3h2 causes altered collagen prolyl 3-hydroxylation from multiple tissues.
Significance: Improved understanding of molecular mechanisms of myopia could aid in early diagnosis and treatment of irreversible vision loss. |
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AbstractList | Background:
Mutations in
LEPREL1
, the gene encoding prolyl 3-hydroxylase-2 (P3H2), cause severe nonsyndromic myopia.
Results:
Collagens I and IV from P3h2-null mouse eye tissues were significantly reduced in 3-hydroxylation compared with wild-type littermates.
Conclusion:
Loss of P3h2 causes altered collagen prolyl 3-hydroxylation from multiple tissues.
Significance:
Improved understanding of molecular mechanisms of myopia could aid in early diagnosis and treatment of irreversible vision loss.
Myopia, the leading cause of visual impairment worldwide, results from an increase in the axial length of the eyeball. Mutations in
LEPREL1
, the gene encoding prolyl 3-hydroxylase-2 (P3H2), have recently been identified in individuals with recessively inherited nonsyndromic severe myopia. P3H2 is a member of a family of genes that includes three isoenzymes of prolyl 3-hydroxylase (P3H), P3H1, P3H2, and P3H3. Fundamentally, it is understood that P3H1 is responsible for converting proline to 3-hydroxyproline. This limited additional knowledge also suggests that each isoenzyme has evolved different collagen sequence-preferred substrate specificities. In this study, differences in prolyl 3-hydroxylation were screened in eye tissues from P3h2-null (
P3h2
n/n
) and wild-type mice to seek tissue-specific effects due the lack of P3H2 activity on post-translational collagen chemistry that could explain myopia. The mice were viable and had no gross musculoskeletal phenotypes. Tissues from sclera and cornea (type I collagen) and lens capsule (type IV collagen) were dissected from mouse eyes, and multiple sites of prolyl 3-hydroxylation were identified by mass spectrometry. The level of prolyl 3-hydroxylation at multiple substrate sites from type I collagen chains was high in sclera, similar to tendon. Almost every known site of prolyl 3-hydroxylation in types I and IV collagen from
P3h2
n/n
mouse eye tissues was significantly under-hydroxylated compared with their wild-type littermates. We conclude that altered collagen prolyl 3-hydroxylation is caused by loss of P3H2. We hypothesize that this leads to structural abnormalities in multiple eye tissues, but particularly sclera, causing progressive myopia. Myopia, the leading cause of visual impairment worldwide, results from an increase in the axial length of the eyeball. Mutations in LEPREL1, the gene encoding prolyl 3-hydroxylase-2 (P3H2), have recently been identified in individuals with recessively inherited nonsyndromic severe myopia. P3H2 is a member of a family of genes that includes three isoenzymes of prolyl 3-hydroxylase (P3H), P3H1, P3H2, and P3H3. Fundamentally, it is understood that P3H1 is responsible for converting proline to 3-hydroxyproline. This limited additional knowledge also suggests that each isoenzyme has evolved different collagen sequence-preferred substrate specificities. In this study, differences in prolyl 3-hydroxylation were screened in eye tissues from P3h2-null (P3h2n/n) and wild-type mice to seek tissue-specific effects due the lack of P3H2 activity on post-translational collagen chemistry that could explain myopia. The mice were viable and had no gross musculoskeletal phenotypes. Tissues from sclera and cornea (type I collagen) and lens capsule (type IV collagen) were dissected from mouse eyes, and multiple sites of prolyl 3-hydroxylation were identified by mass spectrometry. The level of prolyl 3-hydroxylation at multiple substrate sites from type I collagen chains was high in sclera, similar to tendon. Almost every known site of prolyl 3-hydroxylation in types I and IV collagen from P3h2n/n mouse eye tissues was significantly under-hydroxylated compared with their wild-type littermates. We conclude that altered collagen prolyl 3-hydroxylation is caused by loss of P3H2. We hypothesize that this leads to structural abnormalities in multiple eye tissues, but particularly sclera, causing progressive myopia. Background: Mutations in LEPREL1, the gene encoding prolyl 3-hydroxylase-2 (P3H2), cause severe nonsyndromic myopia. Results: Collagens I and IV from P3h2-null mouse eye tissues were significantly reduced in 3-hydroxylation compared with wild-type littermates. Conclusion: Loss of P3h2 causes altered collagen prolyl 3-hydroxylation from multiple tissues. Significance: Improved understanding of molecular mechanisms of myopia could aid in early diagnosis and treatment of irreversible vision loss. Myopia, the leading cause of visual impairment worldwide, results from an increase in the axial length of the eyeball. Mutations in LEPREL1, the gene encoding prolyl 3-hydroxylase-2 (P3H2), have recently been identified in individuals with recessively inherited nonsyndromic severe myopia. P3H2 is a member of a family of genes that includes three isoenzymes of prolyl 3-hydroxylase (P3H), P3H1, P3H2, and P3H3. Fundamentally, it is understood that P3H1 is responsible for converting proline to 3-hydroxyproline. This limited additional knowledge also suggests that each isoenzyme has evolved different collagen sequence-preferred substrate specificities. In this study, differences in prolyl 3-hydroxylation were screened in eye tissues from P3h2-null (P3h2(n/n)) and wild-type mice to seek tissue-specific effects due the lack of P3H2 activity on post-translational collagen chemistry that could explain myopia. The mice were viable and had no gross musculoskeletal phenotypes. Tissues from sclera and cornea (type I collagen) and lens capsule (type IV collagen) were dissected from mouse eyes, and multiple sites of prolyl 3-hydroxylation were identified by mass spectrometry. The level of prolyl 3-hydroxylation at multiple substrate sites from type I collagen chains was high in sclera, similar to tendon. Almost every known site of prolyl 3-hydroxylation in types I and IV collagen from P3h2(n/n) mouse eye tissues was significantly under-hydroxylated compared with their wild-type littermates. We conclude that altered collagen prolyl 3-hydroxylation is caused by loss of P3H2. We hypothesize that this leads to structural abnormalities in multiple eye tissues, but particularly sclera, causing progressive myopia. |
Author | Lee, Brendan H. Eyre, David R. Joeng, Kyu Sang Werther, Rachel Rajagopal, Abbhirami Hudson, David M. Weis, MaryAnn |
Author_xml | – sequence: 1 givenname: David M. surname: Hudson fullname: Hudson, David M. organization: From the Department of Orthopaedics and Sports Medicine, University of Washington, Seattle, Washington 98195 and the – sequence: 2 givenname: Kyu Sang surname: Joeng fullname: Joeng, Kyu Sang organization: Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, Texas 77030 – sequence: 3 givenname: Rachel surname: Werther fullname: Werther, Rachel organization: From the Department of Orthopaedics and Sports Medicine, University of Washington, Seattle, Washington 98195 and the – sequence: 4 givenname: Abbhirami surname: Rajagopal fullname: Rajagopal, Abbhirami organization: Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, Texas 77030 – sequence: 5 givenname: MaryAnn surname: Weis fullname: Weis, MaryAnn organization: From the Department of Orthopaedics and Sports Medicine, University of Washington, Seattle, Washington 98195 and the – sequence: 6 givenname: Brendan H. surname: Lee fullname: Lee, Brendan H. organization: Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, Texas 77030 – sequence: 7 givenname: David R. surname: Eyre fullname: Eyre, David R. email: deyre@u.washington.edu organization: From the Department of Orthopaedics and Sports Medicine, University of Washington, Seattle, Washington 98195 and the |
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Copyright | 2015 © 2015 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. 2015 by The American Society for Biochemistry and Molecular Biology, Inc. 2015 by The American Society for Biochemistry and Molecular Biology, Inc. 2015 |
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DocumentTitleAlternate | Prolyl 3-Hydroxylation in High Myopia |
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Keywords | Animal Model Extracellular Matrix Collagen Mass Spectrometry (MS) Post-translational Modification (PTM) Prolyl 3-Hydroxylase 3-Hydroxyproline Sclera |
Language | English |
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Snippet | Myopia, the leading cause of visual impairment worldwide, results from an increase in the axial length of the eyeball. Mutations in LEPREL1, the gene encoding... Background: Mutations in LEPREL1 , the gene encoding prolyl 3-hydroxylase-2 (P3H2), cause severe nonsyndromic myopia. Results: Collagens I and IV from... |
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SubjectTerms | 3-Hydroxyproline Amino Acid Sequence Animal Model Animals Collagen Collagen Type I - metabolism Collagen Type IV - metabolism Cornea - metabolism Extracellular Matrix Genetic Predisposition to Disease Humans Hydroxylation Lens Capsule, Crystalline - metabolism Mass Spectrometry (MS) Mice, Inbred C57BL Mice, Knockout Molecular Bases of Disease Molecular Sequence Data Mutation Myopia - genetics Organ Specificity Phenotype Post-translational Modification (PTM) Procollagen-Proline Dioxygenase - genetics Procollagen-Proline Dioxygenase - metabolism Prolyl 3-Hydroxylase Protein Processing, Post-Translational Sclera Sclera - enzymology Sclera - pathology |
Title | Post-translationally Abnormal Collagens of Prolyl 3-Hydroxylase-2 Null Mice Offer a Pathobiological Mechanism for the High Myopia Linked to Human LEPREL1 Mutations |
URI | https://dx.doi.org/10.1074/jbc.M114.634915 https://www.ncbi.nlm.nih.gov/pubmed/25645914 https://search.proquest.com/docview/1667957756 https://pubmed.ncbi.nlm.nih.gov/PMC4375510 |
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