Osteogenesis imperfecta in Three Dogs from a Single Litter

2000 ◽  
Vol 13 (01) ◽  
pp. 23-27
Author(s):  
J. J. deHaan ◽  
J. N. Peck ◽  
Bonnie Campbell ◽  
Pamela Ginn ◽  
Lynette Phillips ◽  
...  
Keyword(s):  
Osteogenesis Imperfecta ◽  
Type I Collagen ◽  
Type I ◽  
Fibroblast Cells ◽  
Pathological Fractures ◽  
Presumptive Diagnosis ◽  
Cultured Skin ◽  
Pathologic Features ◽  
History Of ◽  
Collagen Analysis

SummaryThree American Cream puppies from a litter of six were admitted for evaluation and treatment of lameness caused by multiple pathological fractures. Because of a poor prognosis, all three of the affected dogs were ultimately euthanatized. Based on the histopathological findings of the bones and a collagen analysis from cultured skin fibroblast cells which confirmed the presence of abnormal type I collagen, the presumptive diagnosis was osteogenesis imperfecta. In humans, more than 90% of the cases of osteogenesis imperfecta are caused by defects in type I collagen (11). Osteogenesis imperfecta has rarely been described in animals and none of the previous reports document the disease in more than one dog from a single litter.Three American Cream puppies from a litter of six developed multiple pathologic features without a history of trauma. A diagnosis of osteogenesis imperfecta was made based on histopathology and results of type I collagen analysis from cultured skin fibroblasts.

scholarly journals A novel Gly to Arg substitution at position 388 of the alpha1 chain of type I collagen in lethal form of osteogenesis imperfecta.

2002 ◽  
Vol 49 (2) ◽  
pp. 443-450 ◽  
Author(s):  
Anna Galicka ◽  
Slawomir Wolczynski ◽  
Ryszard Lesniewicz ◽  
Lech Chyczewski ◽  
Andrzej Gindzienski
Keyword(s):  
Osteogenesis Imperfecta ◽  
Type I Collagen ◽  
Peptide Mapping ◽  
Novel Mutation ◽  
Direct Sequencing ◽  
Base Change ◽  
Clinical Severity ◽  
Restriction Enzyme Digestion ◽  
Type I ◽  
Cultured Skin

Cultured skin fibroblasts from a proband with a lethal form of osteogenesis imperfecta produce two forms of type I collagen chains, with normal and delayed electrophoretic migration; collagen of the proband's mother was normal. Peptide mapping experiments localized the structural defect in the proband to alpha1(I) CB8 peptide in which residues 123 to 402 are spaned. Direct sequencing of amplified cDNA covering this region revealed a G to A single base change in one allele of the alpha1(I) chain, that converted glycine 388 to arginine. Restriction enzyme digestion of the RT-PCR product was consistent with a heterozygous COL1A1 mutation. The novel mutation conforms to the linear gradient of clinical severity for the alpha1(I) chain and results in reduced thermal stability by 3 degrees C and intracellular retention of abnormal molecules.

scholarly journals Energy Alterations in Patient with Osteogenesis Imperfecta

2022 ◽  
Vol 4 (1) ◽  
pp. 01-07
Author(s):  
Huang Wei Ling
Keyword(s):  
Chinese Medicine ◽  
Traditional Chinese Medicine ◽  
Osteogenesis Imperfecta ◽  
Type I Collagen ◽  
Point Of View ◽  
Auricular Acupuncture ◽  
Type I ◽  
Dietary Counseling ◽  
Energy Deficiency ◽  
History Of

Introduction; Osteogenesis imperfecta is according to Western medicine, a disorder of the connective tissue caused by an abnormal synthesis or processing type I collagen of genetic origin, a protein that is important to strengthen bones. The clinical manifestation of this problem can cause blue sclera, short stature, and deafness in adulthood, dentinogenesis imperfecta. In traditional Chinese medicine (TCM), osteogenesis imperfecta is related to Kidney energy deficiency (second chakra). Purpose: the purpose of this study is to show that patients with osteogenesis imperfecta has energy deficiency in the Kidney energy (second chakra) and the treatment of this condition, replenishing this energy using highly diluted medications is very important to treat the root of the problem and not just treating the symptoms. Methods: through one case report of 30 years-old man with history of several fractures since childhood. He went acupuncture clinic to treat his anxiety symptoms and I saw that his sclera was blue. Treatment was done using Chinese dietary counseling, auricular acupuncture with apex ear bloodletting and systemic acupuncture. Radiesthesia procedure were used to measure his chakras’ energy centers. Results: All his chakras’ were in the lowest level of energy, including the second that was the Kidney, responsible for the bone and teeth. The treatment began replenishing this chakras’ energy centers using highly diluted medications, such as homeopathies, according to the theory created by me (2020) entitled Constitutional Homeopathy of the Five Elements Based on Traditional Chinese Medicine and crystal-based medications. Conclusion: through this case reported in this article, I can say that patient with osteogenesis imperfecta has energy deficiency in the five internal massive organ, especially in the Kidney and the treatment of these energy deficiency, is very important to treat patients with osteogenesis imperfecta in the deepest level, in the energy point of view.

scholarly journals Restoration of Osteogenesis by CRISPR/Cas9 Genome Editing of the Mutated COL1A1 Gene in Osteogenesis Imperfecta

2021 ◽  
Vol 10 (14) ◽  
pp. 3141
Author(s):  
Hyerin Jung ◽  
Yeri Alice Rim ◽  
Narae Park ◽  
Yoojun Nam ◽  
Ji Hyeon Ju
Keyword(s):  
Osteogenesis Imperfecta ◽  
Type I Collagen ◽  
Disease Modeling ◽  
Bone Fragility ◽  
Osteogenic Potential ◽  
Type I ◽  
Gene Correction ◽  
Col1a1 Gene ◽  
Collagen Formation

Osteogenesis imperfecta (OI) is a genetic disease characterized by bone fragility and repeated fractures. The bone fragility associated with OI is caused by a defect in collagen formation due to mutation of COL1A1 or COL1A2. Current strategies for treating OI are not curative. In this study, we generated induced pluripotent stem cells (iPSCs) from OI patient-derived blood cells harboring a mutation in the COL1A1 gene. Osteoblast (OB) differentiated from OI-iPSCs showed abnormally decreased levels of type I collagen and osteogenic differentiation ability. Gene correction of the COL1A1 gene using CRISPR/Cas9 recovered the decreased type I collagen expression in OBs differentiated from OI-iPSCs. The osteogenic potential of OI-iPSCs was also recovered by the gene correction. This study suggests a new possibility of treatment and in vitro disease modeling using patient-derived iPSCs and gene editing with CRISPR/Cas9.

scholarly journals Intracellular and Extracellular Markers of Lethality in Osteogenesis Imperfecta: A Quantitative Proteomic Approach

2021 ◽  
Vol 22 (1) ◽  
pp. 429
Author(s):  
Luca Bini ◽  
Domitille Schvartz ◽  
Chiara Carnemolla ◽  
Roberta Besio ◽  
Nadia Garibaldi ◽  
...  
Keyword(s):  
Osteogenesis Imperfecta ◽  
Type I Collagen ◽  
Type I ◽  
Tandem Mass ◽  
Type Ii ◽  
Type Iii ◽  
Bioinformatic Tools ◽  
Proteomic Approach ◽  
Fibrillin 1 ◽  
Heritable Disorder

Osteogenesis imperfecta (OI) is a heritable disorder that mainly affects the skeleton. The inheritance is mostly autosomal dominant and associated to mutations in one of the two genes, COL1A1 and COL1A2, encoding for the type I collagen α chains. According to more than 1500 described mutation sites and to outcome spanning from very mild cases to perinatal-lethality, OI is characterized by a wide genotype/phenotype heterogeneity. In order to identify common affected molecular-pathways and disease biomarkers in OI probands with different mutations and lethal or surviving phenotypes, primary fibroblasts from dominant OI patients, carrying COL1A1 or COL1A2 defects, were investigated by applying a Tandem Mass Tag labeling-Liquid Chromatography-Tandem Mass Spectrometry (TMT LC-MS/MS) proteomics approach and bioinformatic tools for comparative protein-abundance profiling. While no difference in α1 or α2 abundance was detected among lethal (type II) and not-lethal (type III) OI patients, 17 proteins, with key effects on matrix structure and organization, cell signaling, and cell and tissue development and differentiation, were significantly different between type II and type III OI patients. Among them, some non–collagenous extracellular matrix (ECM) proteins (e.g., decorin and fibrillin-1) and proteins modulating cytoskeleton (e.g., nestin and palladin) directly correlate to the severity of the disease. Their defective presence may define proband-failure in balancing aberrances related to mutant collagen.

Intracranial meningioma in a patient with osteogenesis imperfecta

Open Medicine ◽  
2008 ◽  
Vol 3 (4) ◽  
pp. 517-520
Author(s):  
Parmenion Tsitsopoulos ◽  
Ioannis Anagnostopoulos ◽  
Vasileios Tsitouras ◽  
Ioannis Venizelos ◽  
Philippos Tsitsopoulos
Keyword(s):  
Osteogenesis Imperfecta ◽  
Muscle Power ◽  
Brain Mri ◽  
Intracranial Meningioma ◽  
Type I ◽  
Mri Scans ◽  
Heritable Disorder ◽  
History Of ◽  
One Year ◽  
Gait Disturbances

AbstractOsteogenesis imperfecta (OI) is a heritable disorder characterized mainly by connective tissue manifestations. In dinstinct cases, several neurological features have also been described. A 46-year-old male with a known family history of OI type I presented with progressive gait disturbances and diminished muscle strength. Brain MRI scans revealed an infiltrative intracranial mass occupying both frontoparietal lobes. The patient underwent surgical intervention. The histological diagnosis was an atypical (Grade II) meningioma. The bony parts demonstrated a mixture of osseous defects due to OI and infiltration by the tumor. At one-year follow up the patient′s muscle power partially returned while repeat MRI scans were negative for tumor recurrence.

Type I Collagen Biosynthesis by Skin Fibroblasts from Patients with Idiopathic Juvenile Osteoporosis

1995 ◽  
Vol 89 (1) ◽  
pp. 69-73 ◽  
Author(s):  
Andrew E. Pocock ◽  
Martin J. O. Francis ◽  
Roger Smith
Keyword(s):  
Osteogenesis Imperfecta ◽  
Type I Collagen ◽  
The Other ◽  
Type I ◽  
Osteogenesis Imperfecta Type ◽  
Unrelated Control ◽  
Type Iii ◽  
Collagen Peptides ◽  
Idiopathic Juvenile Osteoporosis ◽  
Osteogenesis Imperfecta Type I

1. Skin fibroblast lines were cultured from nine patients who had the features of idiopathic juvenile osteoporosis, six relatives, five unrelated control subjects and three unrelated patients with osteogenesis imperfecta type I. Some patients with idiopathic juvenile osteoporosis were adults whose previous osteoporosis was in remission. Two patients with idiopathic juvenile osteoporosis were siblings and one patient with idiopathic juvenile osteoporosis had a daughter with severe osteogenesis imperfecta (type III). 2. The ratio of type III to type I collagen, synthesized by fibroblasts, was increased in two of the patients with osteogenesis imperfecta type I and in the daughter with osteogenesis imperfecta type III, but was normal in all the other patients with idiopathic juvenile osteoporosis and the other relatives. 3. Radiolabelled collagen was digested by cyanogen bromide and separated on SDS-PAGE. Unreduced collagen peptides migrated normally, except those from both the two siblings with idiopathic juvenile osteoporosis. In these two lines, abnormal migration suggested the presence of collagen I mutations. 4. The secretion of synthesized collagen by these two idiopathic juvenile osteoporosis lines and two others was reduced to only 43–45% as compared with a line from a 13-year-old control subject, which was defined as 100%. The three osteogenesis imperfecta type I lines secreted 18–37%, the other five idiopathic juvenile osteoporosis lines secreted 57–75%, the relatives (including the daughter with severe osteogenesis imperfecta) secreted 49–115% and the controls secreted 69–102%. 5. We conclude that qualitative abnormalities of type I collagen associated with a reduction in total secreted collagen synthesis may occur in a minority of patients with idiopathic juvenile osteoporosis; these patients could represent a subset of patients with this disorder.

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