Clinical, radiographic and molecular characterization of two unrelated families with multicentric osteolysis, nodulosis, and arthropathy.


Journal

BMC musculoskeletal disorders
ISSN: 1471-2474
Titre abrégé: BMC Musculoskelet Disord
Pays: England
ID NLM: 100968565

Informations de publication

Date de publication:
14 Sep 2023
Historique:
received: 27 03 2023
accepted: 05 09 2023
medline: 18 9 2023
pubmed: 15 9 2023
entrez: 14 9 2023
Statut: epublish

Résumé

Multicentric osteolysis nodulosis and arthropathy (MONA) is a rare autosomal recessive disorder characterized by marked progressive bone loss and joint destruction resulting in skeletal deformities. MONA is caused by MMP2 deficiency. Here we report clinical and molecular analyses of four patients in two families from Pakistan and Finland. Clinical analyses including radiography were completed and blood samples were collected. The extracted DNA was subjected to whole-exome analysis or target gene sequencing. Segregation analyses were performed in the nuclear pedigree. Pathogenicity prediction scores for the selected variants and conservation analyses of affected amino acids were observed. The phenotype in the four affected individuals was consistent with multicentric osteolysis or MONA, as the patients had multiple affected joints, osteolysis of hands and feet, immobility of knee joint and progressive bone loss. Long-term follow up of the patients revealed the progression of the disease. We found a novel MMP2 c.1336 + 2T > G homozygous splice donor variant segregating with the phenotype in the Pakistani family while a MMP2 missense variant c.1188 C > A, p.(Ser396Arg) was homozygous in both Finnish patients. In-silico analysis predicted that the splicing variant may eventually introduce a premature stop codon in MMP2. Molecular modeling for the p.(Ser396Arg) variant suggested that the change may disturb MMP2 collagen-binding region. Our findings expand the genetic spectrum of Multicentric osteolysis nodulosis and arthropathy. We also suggest that the age of onset of this disorder may vary from childhood up to late adolescence and that a significant degree of intrafamilial variability may be present.

Sections du résumé

BACKGROUND BACKGROUND
Multicentric osteolysis nodulosis and arthropathy (MONA) is a rare autosomal recessive disorder characterized by marked progressive bone loss and joint destruction resulting in skeletal deformities. MONA is caused by MMP2 deficiency. Here we report clinical and molecular analyses of four patients in two families from Pakistan and Finland.
METHODS METHODS
Clinical analyses including radiography were completed and blood samples were collected. The extracted DNA was subjected to whole-exome analysis or target gene sequencing. Segregation analyses were performed in the nuclear pedigree. Pathogenicity prediction scores for the selected variants and conservation analyses of affected amino acids were observed.
RESULTS RESULTS
The phenotype in the four affected individuals was consistent with multicentric osteolysis or MONA, as the patients had multiple affected joints, osteolysis of hands and feet, immobility of knee joint and progressive bone loss. Long-term follow up of the patients revealed the progression of the disease. We found a novel MMP2 c.1336 + 2T > G homozygous splice donor variant segregating with the phenotype in the Pakistani family while a MMP2 missense variant c.1188 C > A, p.(Ser396Arg) was homozygous in both Finnish patients. In-silico analysis predicted that the splicing variant may eventually introduce a premature stop codon in MMP2. Molecular modeling for the p.(Ser396Arg) variant suggested that the change may disturb MMP2 collagen-binding region.
CONCLUSION CONCLUSIONS
Our findings expand the genetic spectrum of Multicentric osteolysis nodulosis and arthropathy. We also suggest that the age of onset of this disorder may vary from childhood up to late adolescence and that a significant degree of intrafamilial variability may be present.

Identifiants

pubmed: 37710205
doi: 10.1186/s12891-023-06856-2
pii: 10.1186/s12891-023-06856-2
pmc: PMC10503101
doi:

Substances chimiques

Matrix Metalloproteinase 2 EC 3.4.24.24

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

735

Subventions

Organisme : Pakistan Science Foundation
ID : PSF/Res/P-PU/Biotech (239)

Informations de copyright

© 2023. BioMed Central Ltd., part of Springer Nature.

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Auteurs

Tayyaba Ishaq (T)

School of Biological Sciences, University of the Punjab, Quaid-i-Azam Campus, Lahore, 54590, Pakistan.

Petra Loid (P)

Folkhälsan Research Center, Genetics Research Program, Helsinki, Finland.
Children's Hospital, University of Helsinki and Helsinki University Hospital, Helsinki, Finland.
Department of Clinical Genetics, Helsinki University Hospital, Helsinki, Finland.
Research Program for Clinical and Molecular Metabolism, University of Helsinki, Helsinki, Finland.

Hafiza Abida Ishaq (HA)

Services Hospital Lahore, Lahore, Pakistan.

Go Hun Seo (GH)

3billion, Inc, Seoul, Republic of Korea.

Outi Mäkitie (O)

Folkhälsan Research Center, Genetics Research Program, Helsinki, Finland. outi.makitie@helsinki.fi.
Children's Hospital, University of Helsinki and Helsinki University Hospital, Helsinki, Finland. outi.makitie@helsinki.fi.
Department of Clinical Genetics, Helsinki University Hospital, Helsinki, Finland. outi.makitie@helsinki.fi.
Research Program for Clinical and Molecular Metabolism, University of Helsinki, Helsinki, Finland. outi.makitie@helsinki.fi.
Department of Molecular Medicine and Surgery, Center for Molecular Medicine, Karolinska Institute, Stockholm, Sweden. outi.makitie@helsinki.fi.

Sadaf Naz (S)

School of Biological Sciences, University of the Punjab, Quaid-i-Azam Campus, Lahore, 54590, Pakistan. naz.sbs@pu.edu.pk.

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Classifications MeSH