scholarly journals Autosomal Recessive HEM/Greenberg Skeletal Dysplasia Is Caused by 3β-Hydroxysterol Δ14-Reductase Deficiency Due to Mutations in the Lamin B Receptor Gene

2003 ◽  
Vol 72 (4) ◽  
pp. 1013-1017 ◽  
Author(s):  
Hans R. Waterham ◽  
Janet Koster ◽  
Petra Mooyer ◽  
Gerard van Noort ◽  
Richard I. Kelley ◽  
...  
Keyword(s):  
Skeletal Dysplasia ◽  
Autosomal Recessive ◽  
Receptor Gene ◽  
Lamin B ◽  
Reductase Deficiency ◽  
Lamin B Receptor

scholarly journals GREENBERG'S DYSPLASIA- A RARE GENETIC CONDITION

2020 ◽  
pp. 16-17
Author(s):  
Sundari S ◽  
Javeri Aarti Harish
Keyword(s):  
Skeletal Dysplasia ◽  
Autosomal Recessive ◽  
Ectopic Calcification ◽  
Genetic Condition ◽  
Lamin B ◽  
Lamin B Receptor

Greenberg’s Dysplasia, also known as Hydrops-Ectopic calcification-Moth-Eaten (HEM) Skeletal Dysplasia, is a rare autosomal recessive osteochondrodysplasia, caused by mutation in the Lamin B Receptor (LBR) Gene, on chromosome 1q42.

A homozygous variant in the Lamin B receptor gene LBR results in a non-lethal skeletal dysplasia without Pelger-Huët anomaly

Bone ◽  
2020 ◽  
Vol 141 ◽  
pp. 115601
Author(s):  
Meagan Collins ◽  
Valancy Miranda ◽  
Justine Rousseau ◽  
Lisa E. Kratz ◽  
Philippe M. Campeau
Keyword(s):  
Skeletal Dysplasia ◽  
Receptor Gene ◽  
Lamin B ◽  
Homozygous Variant ◽  
Lamin B Receptor ◽  
Lethal Skeletal Dysplasia

Lamin B receptor-related disorder is associated with a spectrum of skeletal dysplasia phenotypes

Bone ◽  
2019 ◽  
Vol 120 ◽  
pp. 354-363 ◽  
Author(s):  
Eliza Thompson ◽  
Ebtesam Abdalla ◽  
Andrea Superti-Furga ◽  
William McAlister ◽  
Lisa Kratz ◽  
...  
Keyword(s):  
Skeletal Dysplasia ◽  
Related Disorder ◽  
Lamin B ◽  
Lamin B Receptor

scholarly journals Cooperative Activity of GABP with PU.1 or C/EBPε Regulates Lamin B Receptor Gene Expression, Implicating Their Roles in Granulocyte Nuclear Maturation

2016 ◽  
Vol 197 (3) ◽  
pp. 910-922 ◽  
Author(s):  
Krishnakumar Malu ◽  
Rahul Garhwal ◽  
Margery G. H. Pelletier ◽  
Deepali Gotur ◽  
Stephanie Halene ◽  
...  
Keyword(s):  
Gene Expression ◽  
Receptor Gene ◽  
Lamin B ◽  
Nuclear Maturation ◽  
Lamin B Receptor ◽  
Cooperative Activity ◽  
Receptor Gene Expression

Lamin B receptor: role on chromatin structure, cellular senescence and possibly aging

2020 ◽  
Vol 477 (14) ◽  
pp. 2715-2720
Author(s):  
Susana Castro-Obregón
Keyword(s):  
Cellular Senescence ◽  
Nuclear Membrane ◽  
Chromatin Structure ◽  
Cholesterol Synthesis ◽  
Reductase Activity ◽  
Chimeric Protein ◽  
Nuclear Lamina ◽  
Lamin B ◽  
Inner Nuclear Membrane ◽  
Lamin B Receptor

The nuclear envelope is composed by an outer nuclear membrane and an inner nuclear membrane, which is underlain by the nuclear lamina that provides the nucleus with mechanical strength for maintaining structure and regulates chromatin organization for modulating gene expression and silencing. A layer of heterochromatin is beneath the nuclear lamina, attached by inner nuclear membrane integral proteins such as Lamin B receptor (LBR). LBR is a chimeric protein, having also a sterol reductase activity with which it contributes to cholesterol synthesis. Lukasova et al. showed that when DNA is damaged by ɣ-radiation in cancer cells, LBR is lost causing chromatin structure changes and promoting cellular senescence. Cellular senescence is characterized by terminal cell cycle arrest and the expression and secretion of various growth factors, cytokines, metalloproteinases, etc., collectively known as senescence-associated secretory phenotype (SASP) that cause chronic inflammation and tumor progression when they persist in the tissue. Therefore, it is fundamental to understand the molecular basis for senescence establishment, maintenance and the regulation of SASP. The work of Lukasova et al. contributed to our understanding of cellular senescence establishment and provided the basis that lead to the further discovery that chromatin changes caused by LBR reduction induce an up-regulated expression of SASP factors. LBR dysfunction has relevance in several diseases and possibly in physiological aging. The potential bifunctional role of LBR on cellular senescence establishment, namely its role in chromatin structure together with its enzymatic activity contributing to cholesterol synthesis, provide a new target to develop potential anti-aging therapies.

Alterations of nuclear envelope and chromatin organization in mandibuloacral dysplasia, a rare form of laminopathy

2005 ◽  
Vol 23 (2) ◽  
pp. 150-158 ◽  
Author(s):  
Ilaria Filesi ◽  
Francesca Gullotta ◽  
Giovanna Lattanzi ◽  
Maria Rosaria D'Apice ◽  
Cristina Capanni ◽  
...  
Keyword(s):  
Nuclear Envelope ◽  
Protein A ◽  
Nuclear Architecture ◽  
Mendelian Inheritance ◽  
Premature Aging ◽  
Lamin A ◽  
Lamin B ◽  
Lamin B Receptor ◽  
Epigenetic Events ◽  
Mandibuloacral Dysplasia

Autosomal recessive mandibuloacral dysplasia [mandibuloacral dysplasia type A (MADA); Online Mendelian Inheritance in Man (OMIM) no. 248370 ] is caused by a mutation in LMNA encoding lamin A/C. Here we show that this mutation causes accumulation of the lamin A precursor protein, a marked alteration of the nuclear architecture and, hence, chromatin disorganization. Heterochromatin domains are altered or completely lost in MADA nuclei, consistent with the finding that heterochromatin-associated protein HP1β and histone H3 methylated at lysine 9 and their nuclear envelope partner protein lamin B receptor (LBR) are delocalized and solubilized. Both accumulation of lamin A precursor and chromatin defects become more severe in older patients. These results strongly suggest that altered chromatin remodeling is a key event in the cascade of epigenetic events causing MADA and could be related to the premature-aging phenotype.

Mutations in the gene encoding the lamin B receptor produce an altered nuclear morphology in granulocytes (Pelger–Huët anomaly)

10.1038/ng925 ◽  
2002 ◽  
Vol 31 (4) ◽  
pp. 410-414 ◽  
Author(s):  
Katrin Hoffmann ◽  
Christine K. Dreger ◽  
Ada L. Olins ◽  
Donald E. Olins ◽  
Leonard D. Shultz ◽  
...  
Keyword(s):  
Nuclear Morphology ◽  
Gene Encoding ◽  
Lamin B ◽  
Lamin B Receptor

Accumulation of glycated proteins suggesting premature ageing in lamin B receptor deficient mice

2017 ◽  
Vol 19 (1) ◽  
pp. 95-100 ◽  
Author(s):  
Frank Hause ◽  
Dietmar Schlote ◽  
Andreas Simm ◽  
Katrin Hoffmann ◽  
Alexander Navarrete Santos
Keyword(s):  
Lamin B ◽  
Premature Ageing ◽  
Lamin B Receptor ◽  
Glycated Proteins ◽  
Deficient Mice

scholarly journals Autosomal recessive chondrodysplasia with severe short stature caused by a biallelic COL10A1 variant

2017 ◽  
Vol 55 (6) ◽  
pp. 403-407 ◽  
Author(s):  
Noor ul Ain ◽  
Outi Makitie ◽  
Sadaf Naz
Keyword(s):  
Short Stature ◽  
Skeletal Dysplasia ◽  
In Silico ◽  
Autosomal Recessive ◽  
Limb Deformity ◽  
Mild Phenotype ◽  
Whole Exome ◽  
New Type ◽  
Severe Short Stature ◽  
Amino Acid Conservation

BackgroundHeterozygous mutations in COL10A1 underlie metaphyseal chondrodysplasia, Schmid type (MCDS), an autosomal dominant skeletal dysplasia.ObjectiveTo identify the causative variant in a large consanguineous Pakistani family with severe skeletal dysplasia and marked lower limb deformity.MethodsWhole exome sequencing was completed followed by Sanger sequencing to verify segregation of the identified variants. In silico variant pathogenicity predictions and amino acid conservation analyses were performed.ResultsA homozygous c.133 C>T (p.Pro45Ser) variant was identified in COL10A1 in all six severely affected individuals (adult heights 119–130 cm, mean ~−6.33 SD). The individuals heterozygous for the variant had mild phenotype of short stature (adult heights 140–162 cm, mean ~−2.15 SD) but no apparent skeletal deformities. The variant was predicted to be pathogenic by in silico prediction tools and was absent from public databases and hundred control chromosomes. Pro45 is conserved in orthologues and is located in the non-collagenous 2 domain of COL10A1, variants of which have never been associated with skeletal dysplasia.ConclusionsThis first report of individuals with a homozygous variant in COL10A1 defines a new type of autosomal recessive skeletal dysplasia. The observations in COL10A1 variant carriers suggest a phenotypic overlap between the mildest forms of MCDS and idiopathic short stature.

Sign in / Sign up

Export Citation Format

Share Document