Disease relevance of Comp

• Mutations in the COMP gene result in the autosomal dominant chondrodysplasias pseudoachondroplasia (PSACH) and some types of multiple epiphyseal dysplasia (MED), which are characterized by mild to severe short-limb dwarfism and early-onset osteoarthritis [1].
• Mutations in the human cartilage oligomeric matrix protein (COMP) gene have been linked to the development of pseudoachondroplasia and multiple epiphyseal dysplasia [2].
• In comparisons of the pathogenicity of simian alphaherpesviruses in mice, two isolates of the baboon virus HVP2 were nearly as lethal as monkey B virus, a biological safety level 4 agent (J. W. Ritchey, K. A. Ealey, M. Payton, and R. Eberle, J. Comp. Pathol. 127:150-161, 2002) [3].
• Dorsal root ganglion (DRG) neurons project their axons to specific target layers in the gray matter of the spinal cord, according to their sensory modality (Neuron 30 (2001), 707; Cell 101 (2000), 485; Neuron 31 (2001), 59; J. Comp. Neurol. 380 (1997), 215; Sensory Neurons, Oxford Univ. Press, New York, 1992, p. 131) [4].
• Methyl 5(6)-4-2-pyridyl piperazino carbamoyl benzimidazole-2-carbamate (CDRI Comp. 81-470) was tested against various nematode and cestode infections in different experimental and domestic animals [5].

High impact information on Comp

• COMP-angiopoietin-1 promotes wound healing through enhanced angiogenesis, lymphangiogenesis, and blood flow in a diabetic mouse model [6].
• Thus, COMP-Ang1 could be used as a therapeutic protein for specific protection against endothelial cell injury [7].
• A fusion gene was constructed encoding peptide S, followed by the 24 aa hinge region from camel IgG and a modified 55 aa cartilage oligomeric matrix protein pentamerization domain [8].
• Newborn collagen IX knockout mice exhibited significantly decreased matrilin-3 and cartilage oligomeric matrix protein (COMP) signals, particularly in the cartilage primordium of vertebral bodies and ribs [9].
• In the absence of collagen IX, a substantial amount of matrilin-3 is released into the medium of cultured chondrocytes instead of being integrated into the cell layer as in wild-type and COMP-deficient cells [9].

Biological context of Comp

• The results also show that the phenotype in PSACH/MED cartilage disorders is not caused by the reduced amount of COMP [1].
• A silencer element in the cartilage oligomeric matrix protein gene regulates chondrocyte-specific expression [10].
• The restricted tissue distribution and expression of cartilage oligomeric matrix protein in developing as well as adult mouse tissues suggest the regulation of this protein at the transcriptional level [11].
• We have previously cloned 1.9 kilobases of the 5(') flanking promoter sequence of the murine COMP gene and by deletion analysis have identified two spatially distant chondrocyte-specific regulatory regions [10].
• The open reading frame encoded a product of 755 amino acids that shares a high degree of identity to and possesses all the characteristic molecular features of both rat and human cartilage oligomeric matrix protein [11].

Anatomical context of Comp

• Fibromodulin may function in the early genesis of articular cartilage and COMP may be associated with elaboration of a weight-bearing chondrocyte matrix [12].
• COMP was not detected in the cells at the articular surface prior to cavitation but by 18 dpc, as coordinated movement of the mouse forelimb intensifies, staining for COMP was most intense around the maturing articular chondrocytes [12].
• As development progressed, accumulation of cartilage oligomeric matrix protein was marked in the growth plate [11].
• Competition experiments localized the binding site of these protein complexes from -1775 to -1746; deletion of this 30-bp site results in a selective increase in COMP promoter activity in fibroblasts [10].
• Immunohistology revealed that cartilage oligomeric matrix was deposited as early as 10 days post coitus in predifferentiated mouse embryo mesenchyme [11].

Associations of Comp with chemical compounds

• In addition, it was demonstrated that, similarly to modified cortical endings (Hámori et al., J. Comp. Neurol. 254:166-183, '86), many GABA positive terminals appeared as specific afferent endings, replacing the missing "specific" vibrissal afferents [13].
• This alternative approach to physiologically characterize neurons in the retina was introduced by Marc (1999, J Comp Neurol 407:47-64, 407:65-76), and allows the simultaneous mapping of responses of glutamate receptor-gated channels from an entire population of neurons [14].
• Within the CN, the MOC collaterals tended to ramify in and near regions with high densities of granule cells, regions also associated with the terminals of type II afferent axons (Brown et al.: J. Comp. Neurol. 278:581-590, '88) [15].
• The activity of 2,2'-dicarbomethoxyamino-5,5'-dibenzimidazolyl ketone (II, C.D.R.I. Comp. 82/437) has been evaluated for its micro- and macro-filaricidal efficacy against Litomosoides carinii in rodents [16].
• 2-Phenyl-1H-phenantro [9, 10-d] imidazole (comp.1) and 2-(4-chlorophenyl)-1H-phenantro [9, 10-d] imidazole (comp. 6) were found to be more active than the others and their LD50 values were found to be greater than 100 mg/kg (i.p.) [17].

Other interactions of Comp

• The cartilage oligomeric matrix protein gene (COMP) encodes a noncollagenous extracellular matrix protein whose expression pattern correlates with chondrocyte differentiation and arthritis [10].
• Dlx1 and Dlx2 are detected in retinal neuroprogenitors by embryonic day (E) 12.5 (Eisenstat et al. [1999] J. Comp. Neurol. 217-237) [18].
• Variation in the cerebellar folial pattern of mice is influenced by genetic elements [Inouye, M. and Oda, S., J. Comp. Neurol., 190 (1980) 357-362] [19].
• As previously suggested from a study on postnatal mice (Suzuki et al. J Comp Neurol 2005;482:74-84), IGFBP-4 acts in the epithelial invagination to form the trenches, grooves, or furrows of lingual papillae during development [20].
• Several phenotypes corresponded in relative mobility and relative isoelectric point among inbred strains to that recently reported for esterase-22 by Eisenhardt and von Deimling [(1982). Comp. Biochem. Physiol. 73B:719] [21].

Analytical, diagnostic and therapeutic context of Comp

• Northern blot analysis and immunohistochemical analysis of cartilage indicate that the lack of COMP is not compensated for by any other member of the thrombospondin family [1].
• In addition, when ISEL+ was combined with in situ hybridization for postmitotic neural gene-1 (png-1; Weiner and Chun [1997] J. Comp. Neurol. 381:130-142), which identifies newly postmitotic neurons, a positive correlation was found between the start of differentiation and the onset of PCD [22].
• Neuron number was compared in neonates and adults to determine if sensory neurons are added as body size increases as found in the frog [J. Comp. Neurol. 314 (1991) 106] and the rat [J. Comp. Neurol. 386 (1997) 8] [23].
• Immunohistochemistry was used to determine the distribution of COMP in articular cartilage, and serum levels of COMP were measured by immunoassay [24].
• Molecular cloning and expression patterns of mouse cartilage oligomeric matrix protein gene [25].

References