Report of a newly indentified patient with mutations in BMP1 and underlying pathogenetic aspects
Osteogenesis imperfecta is a genetic condition characterized by bone fragility and recurrent fractures, which in the large majority of patients are caused by defects in the production of type I collagen. Mutations in the gene encoding bone morphogenetic protein 1 (BMP1, also known as procollagen C-e...
| Main Authors: | , , , , , , , , , , , |
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| Format: | Journal Article |
| Published: |
John Wiley & Sons, Inc.
2014
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| Online Access: | http://hdl.handle.net/20.500.11937/68226 |
| _version_ | 1848761776764616704 |
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| author | Valencia, M. Caparrós-Martín, Jose Sirerol-Piquer, M. García-Verdugo, J. Martínez-Glez, V. Lapunzina, P. Temtamy, S. Aglan, M. Lund, A. Nikkels, P. Ruiz-Perez, V. Ostergaard, E. |
| author_facet | Valencia, M. Caparrós-Martín, Jose Sirerol-Piquer, M. García-Verdugo, J. Martínez-Glez, V. Lapunzina, P. Temtamy, S. Aglan, M. Lund, A. Nikkels, P. Ruiz-Perez, V. Ostergaard, E. |
| author_sort | Valencia, M. |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | Osteogenesis imperfecta is a genetic condition characterized by bone fragility and recurrent fractures, which in the large majority of patients are caused by defects in the production of type I collagen. Mutations in the gene encoding bone morphogenetic protein 1 (BMP1, also known as procollagen C-endopeptidase) have been associated with osteogenesis imperfecta in two sib pairs. In this report, we describe an additional patient with osteogenesis imperfecta with normal bone density and a recurrent, homozygous c.34G > C mutation in BMP1. Western blot analysis of dermal fibroblasts from this patient showed decreased protein levels of the two alternatively spliced products of BMP1 and abnormal cleavage of the C-terminal propeptide of type I procollagen. In addition, fluorescence and electron microscopy showed impaired assembly of type I collagen fibrils in the extracellular matrix of cultured fibroblasts derived from two patients: the patient described here and a previously reported patient with a homozygous BMP1 c.747C > G mutation. We conclude that BMP1 is essential for human type I collagen fibrilogenesis. © 2014 Wiley Periodicals, Inc. |
| first_indexed | 2025-11-14T10:37:03Z |
| format | Journal Article |
| id | curtin-20.500.11937-68226 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-14T10:37:03Z |
| publishDate | 2014 |
| publisher | John Wiley & Sons, Inc. |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-682262018-05-18T08:07:20Z Report of a newly indentified patient with mutations in BMP1 and underlying pathogenetic aspects Valencia, M. Caparrós-Martín, Jose Sirerol-Piquer, M. García-Verdugo, J. Martínez-Glez, V. Lapunzina, P. Temtamy, S. Aglan, M. Lund, A. Nikkels, P. Ruiz-Perez, V. Ostergaard, E. Osteogenesis imperfecta is a genetic condition characterized by bone fragility and recurrent fractures, which in the large majority of patients are caused by defects in the production of type I collagen. Mutations in the gene encoding bone morphogenetic protein 1 (BMP1, also known as procollagen C-endopeptidase) have been associated with osteogenesis imperfecta in two sib pairs. In this report, we describe an additional patient with osteogenesis imperfecta with normal bone density and a recurrent, homozygous c.34G > C mutation in BMP1. Western blot analysis of dermal fibroblasts from this patient showed decreased protein levels of the two alternatively spliced products of BMP1 and abnormal cleavage of the C-terminal propeptide of type I procollagen. In addition, fluorescence and electron microscopy showed impaired assembly of type I collagen fibrils in the extracellular matrix of cultured fibroblasts derived from two patients: the patient described here and a previously reported patient with a homozygous BMP1 c.747C > G mutation. We conclude that BMP1 is essential for human type I collagen fibrilogenesis. © 2014 Wiley Periodicals, Inc. 2014 Journal Article http://hdl.handle.net/20.500.11937/68226 10.1002/ajmg.a.36427 John Wiley & Sons, Inc. restricted |
| spellingShingle | Valencia, M. Caparrós-Martín, Jose Sirerol-Piquer, M. García-Verdugo, J. Martínez-Glez, V. Lapunzina, P. Temtamy, S. Aglan, M. Lund, A. Nikkels, P. Ruiz-Perez, V. Ostergaard, E. Report of a newly indentified patient with mutations in BMP1 and underlying pathogenetic aspects |
| title | Report of a newly indentified patient with mutations in BMP1 and underlying pathogenetic aspects |
| title_full | Report of a newly indentified patient with mutations in BMP1 and underlying pathogenetic aspects |
| title_fullStr | Report of a newly indentified patient with mutations in BMP1 and underlying pathogenetic aspects |
| title_full_unstemmed | Report of a newly indentified patient with mutations in BMP1 and underlying pathogenetic aspects |
| title_short | Report of a newly indentified patient with mutations in BMP1 and underlying pathogenetic aspects |
| title_sort | report of a newly indentified patient with mutations in bmp1 and underlying pathogenetic aspects |
| url | http://hdl.handle.net/20.500.11937/68226 |