Disease relevance of LECT1

• The products of chondromodulin-I precursor processing were seen in cultured chondrocytes, a stable long-term culture chondrosarcoma cell line, as well as Chinese hamster ovary (CHO) cells transfected with an expression plasmid that contained cDNA coding for the chondromodulin-I precursor [1].
• Here we have investigated the regulatory mechanism of the expression of the chondromodulin-I (ChM-I) gene, one of the chondrocyte-specific genes, in osteogenic cells using osteosarcoma (OS) cells as a model [2].
• Moreover, ChM-I also inhibited the growth of HT-29 colon adenocarcinoma in vivo, implying its therapeutic potential for solid tumors [3].
• In conclusion, pleomorphic adenoma expressed ChM-I, which is involved in hypovascularity and chondroid formation in this type of tumor [4].
• Comparison of GC-Lect and modified Thayer-Martin media for isolation of Neisseria gonorrhoeae [5].

Psychiatry related information on LECT1

• Therefore, activation differences between episodic and semantic retrieval may ref lect variation along a continuum of processing during task performance within the context of a single memory system [6].
• Skilled speechreading was also associated with activations and deactivations in other brain regions, suggesting that individual differences ref lect the efficiency of a circuit linking sensory, perceptual, memory, cognitive, and linguistic processes rather than the operation of a single component process [7].

High impact information on LECT1

• The inhibition of Sp3 expression by small interfering RNA reduced the expression of the ChM-I gene in ChM-I-positive normal chondrocytes, indicating Sp3 as a physiological transcriptional activator of the ChM-I gene [2].
• 5-Aza-deoxycytidine treatment induced the expression of the ChM-I gene in ChM-I-negative OS cell lines, and the induction of expression was associated tightly with the demethylation of cytosine at -52 (C(-52)) in the middle of an Sp1/3 binding site to which the Sp3, but not Sp1, bound [2].
• Methylation in the core-promoter region of the chondromodulin-I gene determines the cell-specific expression by regulating the binding of transcriptional activator Sp3 [2].
• To further dissect the processing events, three constructs that express recombinant wild-type or mutant chondromodulin-I were transfected into CHO cells [1].
• Chondromodulin-I (ChM-I) is a small glycoprotein that is abundant in fetal cartilage [1].

Chemical compound and disease context of LECT1

• This architecture is almost identical to 5-carboxymethyl-2-hydroxymuconate isomerase (CHMI) and is related to the E. coli signal transducing protein PII [8].

Biological context of LECT1

• Specific loss of chondromodulin-I gene expression in chondrosarcoma and the suppression of tumor angiogenesis and growth by its recombinant protein in vivo [3].
• The deduced amino acid sequence revealed that mature human ChM-I consists of 120 amino acids [9].
• Multiple transfection of the precursor cDNA into CHO cells enabled us to isolate the mature form of human ChM-I from the culture supernatant [9].
• These results suggest that ChM-I participates in the angiogenic switching of cartilage, and that the withdrawal of its expression allows capillary in-growth, which triggers the replacement of cartilage by bone during endochondral bone development [10].
• Expression of ChM-I cDNA in CHO cells indicated that mature ChM-I molecules were secreted from the cells after post-translational modifications and cleavage from the precursor protein at the predicted processing site [10].

Anatomical context of LECT1

• Here, we demonstrated that the level of ChM-I transcripts was substantially reduced to 100 or even less in the lower-grade chondrosarcomas, in articular cartilage or other benign cartilage tumors [3].
• Expression of cartilage-specific functional matrix chondromodulin-I mRNA in rabbit growth plate chondrocytes and its responsiveness to growth stimuli in vitro [11].
• Bovine chondromodulin-I (ChM-I) purified from fetal cartilage stimulated the matrix synthesis of chondrocytes, and inhibited the growth of vascular endothelial cells in vitro [9].
• ChM-I actually inhibited vascular invasion into cartilage that was ectopically induced by demineralized bone matrix in nude mice, leading to the suppression of replacement of cartilage by bone in vivo [10].
• It is homologous with the neutrophil chemokine, chondromodulin II, which stimulates proliferation of osteoblasts and chondrocytes [12].

Associations of LECT1 with chemical compounds

• We showed that chondromodulin-I is cleaved intracellularly at the predicted cleavage site, and that the mature glycopeptide is rapidly secreted immediately after processing [1].
• In the present study, we isolated rabbit ChM-I precursor CDNA by reverse transcription-polymerase chain reactions [11].
• These results suggested that the expression of ChM-I gene in CS has no direct role in tumorigenesis but rather reflects the site of tumor development and therefore precursor of tumor cells [13].
• 5-Carboxymethyl-2-hydroxymuconate isomerase (CHMI) and 4-oxalocrotonate tautomerase (4-OT) are enzymes that catalyze the isomerization of unsaturated ketones [14].
• To evaluate the effect of ChM-I on ectopic bone formation, guanidine extracts of demineralized bone matrix were mixed with the ChM-I-bound heparin-Sepharose beads and were implanted onto the fasciae of back muscle of 6-week old nude mice [15].

Regulatory relationships of LECT1

• On the other hand, all of four central CSs without extramedullary lesions were negative, and the ChM-I negative tumors expressed the parathyroid hormone-related peptide gene at the lower level and the COL10A1 genes at the higher level than articular cartilage cells [13].

Other interactions of LECT1

• To elucidate whether ChM-I plays an essential role in angio-inhibition during endochondral ossification in man, we investigated the expression and localization of ChM-I in comparison with those of angiogenic factors and the endothelial cell marker CD34 in human neonatal vertebral tissues [16].
• The putative roles of these proteins range from involvement in matrix organization or matrix-cell signaling (PRELP, chondroadherin, cartilage oligomeric protein and cartilage matrix protein) through to molecules that are likely to be involved with modulation of the chondrocyte phenotype (CD-RAP, CDMPs, chondromodulin and pleiotrophin) [17].
• Type II collagen and aggrecan were immunolocalized throughout the matrix around lacuna cells of the chondroid element (100%, 91.7%), and ChM-I was infrequently immunolocalized to the spindle-shaped myoepithelial cells in the myxoid element (37.5%) [4].
• Angiogenesis inhibitors localized in hypovascular mesenchymal tissues: chondromodulin-I and tenomodulin [18].
• Immunohistochemical analysis revealed co-expression of ChM-I and BMP-6 in canine mammary tumors [19].

Analytical, diagnostic and therapeutic context of LECT1

• Methylation-specific sequence analyses revealed that the extent of methylation in the core-promoter region of the ChM-I gene was correlated inversely with the expression of the ChM-I gene in OS primary tumors and cell lines [2].
• Northern blotting and in situ hybridization indicated a specific expression of ChM-I mRNA in cartilage [9].
• Northern blot analysis revealed that the expression of ChM-I mRNA occurred in a tissue-specific manner in cartilage [11].
• Molecular cloning of human chondromodulin-I, a cartilage-derived growth modulating factor, and its expression in Chinese hamster ovary cells [9].
• We first identified a genomic DNA fragment which encoded the N-terminus of the ChM-I precursor, and then isolated human ChM-I cDNA from chondrosarcoma tissue by PCR [9].

References