True Pulp Stones in Compound Odontome: An Unusual Finding

ABSTRACT Calcifications within dental pulp are not a rare phenomenon. Rarely, they can be seen in association with dentin dysplasia type II, pulpal dysplasia, tumoral calcinosis, Ehlers-Danlos syndrome type I, Saethre-Chotzen syndrome, Elfin-Facies syndrome, familial expansile osteolysis, osteogenesis imperfecta type I and otodental syndrome. We came across a case of compound odontome in the maxillary posterior region with multiple true pulp stone formation at the microscopic level. Such an unusual association has not been reported in the English medical literature till date. How to cite this article Sarode GS, Sarode SC, Anand R, Waknis P. True Pulp Stones in Compound Odontome: An Unusual Finding. World J Dent 2015;6(4):241-242.

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A novel transgenic murine model with persistently brittle bones simulating osteogenesis imperfecta type I

Bone ◽

10.1016/j.bone.2019.07.021 ◽

2019 ◽

Vol 127 ◽

pp. 646-655 ◽

Cited By ~ 3

Author(s):

Yi Liu ◽

Jianhai Wang ◽

Shuo Liu ◽

Mingjie Kuang ◽

Yaqing Jing ◽

...

Keyword(s):

Osteogenesis Imperfecta ◽

Murine Model ◽

Type I ◽

Osteogenesis Imperfecta Type ◽

Transgenic Murine Model ◽

Brittle Bones ◽

Osteogenesis Imperfecta Type I

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Ehlers Danlos syndrome type VIIB. Incomplete cleavage of abnormal type I procollagen by N-proteinase in vitro results in the formation of copolymers of collagen and partially cleaved pNcollagen that are near circular in cross-section.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)50393-3 ◽

1992 ◽

Vol 267 (13) ◽

pp. 9093-9100

Author(s):

R.B. Watson ◽

G.A. Wallis ◽

D.F. Holmes ◽

D Viljoen ◽

P.H. Byers ◽

...

Keyword(s):

Cross Section ◽

Type I ◽

Syndrome Type ◽

Ehlers Danlos Syndrome ◽

Type I Procollagen ◽

Danlos Syndrome ◽

Incomplete Cleavage

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Muscle Anatomy and Dynamic Muscle Function in Osteogenesis Imperfecta Type I

The Journal of Clinical Endocrinology & Metabolism ◽

10.1210/jc.2013-3209 ◽

2014 ◽

Vol 99 (2) ◽

pp. E356-E362 ◽

Cited By ~ 26

Author(s):

Louis-Nicolas Veilleux ◽

Martin Lemay ◽

Annie Pouliot-Laforte ◽

Moira S. Cheung ◽

Francis H. Glorieux ◽

...

Keyword(s):

Osteogenesis Imperfecta ◽

Muscle Function ◽

Type I ◽

Osteogenesis Imperfecta Type ◽

Osteogenesis Imperfecta Type I

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Mutations of the alpha2(V) chain of type V collagen impair matrix assembly and produce ehlers-danlos syndrome type I

Human Molecular Genetics ◽

10.1093/hmg/7.2.249 ◽

1998 ◽

Vol 7 (2) ◽

pp. 249-255 ◽

Cited By ~ 86

Author(s):

K Michalickova

Keyword(s):

Type I ◽

Syndrome Type ◽

Matrix Assembly ◽

Ehlers Danlos Syndrome ◽

Type V Collagen ◽

Type V ◽

Danlos Syndrome

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

Clinical Science ◽

10.1042/cs0890069 ◽

1995 ◽

Vol 89 (1) ◽

pp. 69-73 ◽

Cited By ~ 7

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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