anti-Leucine Proline-Enriched Proteoglycan (Leprecan) 1 (LEPRE1) Antibodies

Human Leucine Proline-Enriched Proteoglycan (Leprecan) 1 (LEPRE1) interaction partners

1. P3H1 mutation is associated with Non-Lethal Type VIII Osteogenesis Imperfecta.

2. This study enhances our knowledge about the mutational pattern of the LEPRE1, CRTAP, and PPIB genes. LEPRE1 should be the first gene analyzed in mutation detection studies in patients with recessive OI.

3. An additional function of the rough endoplasmic reticulum protein complex prolyl 3-hydroxylase 1.cartilage-associated protein.cyclophilin B: the CXXXC motif reveals disulfide isomerase activity in vitro.

4. This is the first report of a mutation in LEPRE1 that eliminates only the KDEL ER-retrieval sequence, whereas other functional domains remain intact

5. 0.4% of Mid-Atlantic African Americans and 1.48% West Africans carry mutation in LEPRE1 which causes lethal recessive osteogenesis imperfecta.

6. Mutation analyses were performed for COL1A1, COL1A2, CRTAP, and LEPRE1 in a cohort of 58 unrelated Chinese patients with osteogenesis imperfecta.

7. We report a large consanguineous Turkish family in which multiple individuals are affected with autosomal recessive lethal or severe osteogenesis imperfecta (OI) due to a novel homozygous LEPRE1 mutation

8. Null mutations in LEPRE1 and CRTAP cause severe recessive osteogenesis imperfecta.

9. CRTAP and P3H1 are mutually stabilized in the collagen prolyl 3-hydroxylation complex in endoplasmic reticulum.

10. Screening of 78 subjects diagnosed with osteogenesis imperfecta type II or III, identified three probands with mutations in CRTAP and 16 with mutations in LEPRE1.

11. Mutations in CRTAP and LEPRE1 are found in 3 patients with type II osteogenesis imperfecta.

12. Findings suggest that the 3-hydroxylation function of P3H1 is restricted to the 736AA splice form.

Mouse (Murine) Leucine Proline-Enriched Proteoglycan (Leprecan) 1 (LEPRE1) interaction partners

1. P3H1 deficiency leads to decreased deposition of extracellular matrix by osteoblasts and increased incorporation of mineral into the matrix.

2. we generated knock-in mice carrying a single amino acid substitution in the catalytic site of P3h1 (Lepre1(H662A) ). This substitution abolished P3h1 activity but retained ability to form a complex with Crtap and thus the collagen chaperone

3. An additional function of the rough endoplasmic reticulum protein complex prolyl 3-hydroxylase 1.cartilage-associated protein.cyclophilin B: the CXXXC motif reveals disulfide isomerase activity in vitro.

4. The absence of 3-hydroxyproline and/or the increased glycosylation of hydroxylysine in type I collagen disturbs the lateral growth of the fibrils.

5. The LEPRE1 knockout mouse is a valuable model system to investigate the mechanism of hearing loss in recessive osteogenesis imperfecta.

6. Prolyl 3-hydroxylase 1 null mice display abnormalities in fibrillar collagen-rich tissues such as tendons, skin, and bones

7. Study found that all 3 mouse Leprecan genes Lepre1, leprel1 and leprel2 are expressed in the notochord; additionally, they are expressed in dorsal root ganglia, limb buds, branchial arches, and developing kidneys.

8. This report characterizes expression of the P3H1, P3H2 and P3H3 genes in embryonic and adult mice.