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Literature summary for 1.14.11.7 extracted from

  • Pokidysheva, E.; Boudko, S.; Vranka, J.; Zientek, K.; Maddox, K.; Moser, M.; Faessler, R.; Ware, J.; Baechinger, H.
    Biological role of prolyl 3-hydroxylation in type IV collagen (2014), Proc. Natl. Acad. Sci. USA, 111, 161-166 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
additional information construction of P3H2-null mice, the mutants are embryonic-lethal by embryonic day 8.5. The mechanism of the unexpectedly early lethality involves the interaction of non-3-hydroxylated embryonic type IV collagen with the maternal platelet-specific glycoprotein VI (GPVI). This interaction results in maternal platelet aggregation, thrombosis of the maternal blood, and death of the embryo. The phenotype is completely rescued by producing double KOs of P3H2 and GPVI. Double nulls are viable and fertile. Epigenetic silencing of P3H2 in breast cancers implies that the interaction between GPVI and nonย–3-hydroxylated type IV collagen might also play a role in the progression of malignant tumors and metastasis Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[procollagen]-L-proline + 2-oxoglutarate + O2 Mus musculus type IV collagen [procollagen]-trans-3-hydroxy-L-proline + succinate + CO2
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?

Organism

Organism UniProt Comment Textmining
Mus musculus Q8CG71
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-

Source Tissue

Source Tissue Comment Organism Textmining
embryo
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Mus musculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[procollagen]-L-proline + 2-oxoglutarate + O2 type IV collagen Mus musculus [procollagen]-trans-3-hydroxy-L-proline + succinate + CO2
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?

Synonyms

Synonyms Comment Organism
Leprel1
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Mus musculus
P3H2
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Mus musculus
prolyl 3-hydroxylase-2
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Mus musculus

General Information

General Information Comment Organism
malfunction P3H2-null mice are embryonic-lethal by embryonic day 8.5. The mechanism of the unexpectedly early lethality involves the interaction of non-3-hydroxylated embryonic type IV collagen with the maternal platelet-specific glycoprotein VI (GPVI). This interaction results in maternal platelet aggregation, thrombosis of the maternal blood, and death of the embryo. The phenotype is completely rescued by producing double knockouts of P3H2 and GPVI. Double nulls are viable and fertile. Epigenetic silencing of P3H2 in breast cancers implies that the interaction between GPVI and nonย–3-hydroxylated type IV collagen might also play a role in the progression of malignant tumors and metastasis Mus musculus
physiological function role of prolyl 3-hydroxylation in type IV collagen. Subendothelial collagens bear platelet-specific glycoprotein VI, GPVI, binding sites that initiate platelet aggregation upon blood exposure during injuries. In type IV collagen, these sites are normally 3-hydroxylated. Prolyl 3-hydroxylation of type IV collagen has an important function preventing maternal platelet aggregation in response to the early developing embryo. 3-Hydroxylation of type IV collagen is indispensable for embryonic development in mice Mus musculus