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At least 631 records · Page 35Linked to original sources
PubMed1998

Disrupted expression of matrix genes in the growth plate of the mouse cartilage matrix deficiency (cmd) mutant.

Chondrodysplasia in the autosomal recessive cartilage matrix deficiency (cmd) mutant is caused by lack of the proteoglycan aggrecan arising from a mutation in the gene. Homozygous cmd/cmd mice are characterized by disorganisation of chondrocytes in the growth plate, disproportionate dwarfism, cleft palate, and perinatal lethality. We have studied the impact of the aggrecan deficiency on the expression of other matrix genes during the differentiation of chondrocytes in the growth plate of cmd/cmd 18.5 day fetuses. Compared with the wild-type, there are significant differences in the growth plates of cmd mutants in the combinations of co-expression of genes encoding the glycoprotein link protein, proteoglycan syndecan 3, collagens alpha 1 (X) [Col10a1], alpha 2(XI) [Col11a2], and the alternative transcripts of alpha 1 (II) [Col2a1 type IIA form], and alpha 1 (IX) [Col9a1 long and short forms]. The discordance of gene expression in cmd chondrocytes may be additional factors contributing to the disrupted cellular architecture of the growth plate resulting from the primary absence of aggrecan.

Aggrecans↗
PubMed1990

Chondrosarcoma of bone in children.

Chondrosarcoma of bone rarely occurs in children. This report analyzes the clinicopathologic features in a series of 47 patients with conventional chondrosarcoma who were less than 17 years of age. Of the 47 cases, 14 were from the Mayo Clinic files, and 33 were from our consultation files. Most of the lesions occurred in the trunk and upper ends of the long bones, with the humerus being the most frequent skeletal site. Twelve of the 47 tumors were secondary. The radiographic findings were the same as those seen in adult chondrosarcoma. Pathologically, the tumors were low grade. En bloc resection is the treatment of choice because of the high incidence of local recurrence with lesser surgical margins. Prognosis in childhood chondrosarcoma is no different from that in adult chondrosarcoma. None of the patients with follow-up data had metastasis.

Adolescent↗
PubMed2001

Metaphyseal dysplasia: a new autosomal dominant type in a large German kindred.

We describe a new autosomal dominant type of metaphyseal dysplasia (MD) in five generations of a German kindred. The main characteristics are metaphyseal widening and undermodeling of the tubular bones with Erlenmeyer flask-like appearance of the distal femora (typical of MD), with unusually severe varus deformity of the radii and flat exostoses of the long bones localized in the metaphyses. The skull is unaffected. Allelism with craniometaphyseal dysplasia (CMD) was excluded by linkage analysis.

Child↗
PubMed1984

The Jansen type of metaphyseal chondrodysplasia: confirmation of dominant inheritance and review of radiographic manifestations in the newborn and adult.

We describe a mother and infant girl with the Jansen type of metaphyseal chondrodysplasia. The transmission of the syndrome from mother to daughter in this family establishes this as a dominant condition. Characteristic radiographic manifestations of the disorder were obvious at birth. The mother and infant illustrate the two extremes of age where the radiographic manifestations are less characteristic than in middle childhood, since the marked metaphyseal calcifications are absent.

Adult↗
PubMed1989

Type II collagen screening in the human chondrodysplasias.

Abnormalities of type II collagen have been considered strong candidates for causing human condrodysplasias. We have employed peptide mapping to screen for several types of type II colagen abnormalities in cartilage samples from 66 patients with 20 separate disorders. Except for achondrogenesis type II (Langer-Saldino) and spondyloepiphyseal dysplasia (SED) congenita in which abnormalities have been described and diastrophic dysplasia in which the changes were probably secondary, no abnormalities were detected. Within the limitations of the screening technique, the results combined with other data from the literature suggest that abnormalities of this molecule are not common causes of chondrodysplasias outside of the achondrogenesis type II-SED congenita family of disorders.

Adolescent↗
PubMed1991

Fibrochondrogenesis in male twins at 24 weeks gestation.

Fibrochondrogenesis is a rare lethal chondrodysplasia. Only 5 cases have been reported. We report on a pair of affected twins diagnosed at 24 weeks of gestation. Occurrence in sibs and consanguinity in the parents in a previous report support autosomal recessive transmission.

Alkaline Phosphatase↗
PubMed1993

Genetic skeletal dysplasias in the Museum of Pathological Anatomy, Vienna.

Skeletal material in the Museum of Pathological Anatomy, Vienna, has been appraised in order to modify existing descriptive designations and to establish diagnoses of specific genetic disorders. In this way osseous material relating to classical genetic syndromes has been identified and will be available for further study. Among the skeletons of adults in the museum, the following genetic conditions could be diagnosed: achondroplasia, Marfan syndrome, cleidocranial dysostosis, and diaphyseal aclasia. In adult sisters with dwarfism and a rickety bone disorder, the final diagnosis was uncertain. Infantile bone dysplasias, genetic conditions involving the skull, and malformation syndromes which are all represented in the museum are currently being analyzed.

Achondroplasia↗
PubMed2006

ColVa1 and ColXIa1 are required for myocardial morphogenesis and heart valve development.

Genetic mutations in minor fibrillar collagen types Va1 (ColVa1) and XIa1 (ColXI) have been identified in connective tissue disorders including Ehlers-Danlos syndrome and chondrodysplasias. ColVa1+/- and ColXIa1-/- mutant mice recapitulate these human disorders and show aberrations in collagen fiber organization in connective tissue of the skin, cornea, cartilage, and tendon. In the heart, fibrous networks of collagen fibers form throughout the ventricular myocardium and heart valves, and alterations in collagen fiber homeostasis are apparent in many forms of cardiac disease associated with myocardial dysfunction and valvular insufficiency. There is increasing evidence for cardiac dysfunction in connective tissue disorders, but the mechanisms have not been addressed. ColVa1+/- and ColXIa1-/- mutant mice were used to identify roles for ColVa1 and ColXIa1 in ventricular myocardial morphogenesis and heart valve development. These affected cardiac structures show a compensatory increase in type I collagen deposition, similar to that previously described in valvular and cardiomyopathic disease. Morphological cardiac defects associated with changes in collagen fiber homeostasis identified in ColVa1+/- and ColXIa1-/- mice provide an insight into previously unappreciated forms of cardiac dysfunction associated with connective tissue disorders.

Animals↗
PubMed1988

Histochemical, immunofluorescence, and ultrastructural differences in fetal cartilage among three genetically distinct chondrodystrophic mice.

The severe lethal chondrodystrophies in man result in a common clinical syndrome including shortening of the face, mandible, and limbs. Studies of three lethal chondrodystrophic mutants in mice, viz., chondrodysplasia (cho), cartilage matrix deficiency (cmd), and disproportionate micromelia (Dmm), which share this syndrome, were performed with the aim of identifying histochemical, immunofluorescence, or ultrastructural differences which might exist among these hereditary cartilage disorders. We examined limb cartilage epiphyses from day 18 normal and mutant fetuses and observed repeatable, mostly qualitative differences. All observations were made relative to the normal control. Histochemical staining of matrix proteoglycan was moderately decreased in cho and Dmm cartilage and markedly decreased in cmd when compared to the normal control. Staining of matrix collagen was irregular in distribution in cho, increased in cmd, and decreased in Dmm. Immunofluorescence of proteoglycan was increased in the matrix of cho and Dmm and decreased in cmd. Immunofluorescence of type II collagen was heterogeneous and moderately decreased in the matrix of cho, increased in cmd, and markedly decreased in Dmm. Immunofluorescence of link protein in cho was localized in the cellular-pericellular region as in the normal and appeared increased in the matrix of cmd and Dmm. Immunofluorescence of chondronectin was localized in the cellular-pericellular region and appeared normal in all three mutants. Major differences in cellular and matrix ultrastructure were observed among the mutants, including a decreased frequency of small-diameter collagen fibrils in cho and Dmm, increased density of collagen fibrils in cmd, and dilated RER in Dmm. These observations demonstrate that distinct structural and possibly molecular differences exist among the chondrodystrophies. In the case of cmd, the differences correlated with a previously reported molecular defect, viz., absence of core protein of cartilage specific proteoglycan in the cartilage of this mutant. It is anticipated that the methods used in the present study can be applied to humans in case classification and in identifying potential mouse-human correlates.

Animals↗
PubMed1995

A novel mutation substituting tryptophan with arginine in the carboxyl-terminal, non-collagenous domain of collagen X in a case of Schmid metaphyseal chondrodysplasia.

A novel nucleotide change in the collagen X gene was identified in a Japanese family with Schmid metaphyseal chondrodysplasia (SMCD). The T to C change at nucleotide 1951 resulted in replacement of tryptophan by arginine at residue 651 (W651R). This missense mutation is considered to be responsible for SMCD because 1, the same mutation was not be identified in the collagen X gene from normal individuals; 2, the mutation segregated with the SMCD phenotype in the index family; 3, the substituted amino acid is highly conserved in type X collagens, and 4, the mutation causes a marked change in the hydrophobicity profile of the surrounding region in the NC1 domain. This novel mutation (W651) seems to have the same impact on bone development as W651X mutation.

Amino Acid Sequence↗