The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

LECT1  -  leukocyte cell derived chemotaxin 1

Homo sapiens

Synonyms: BRICD3, CHM-I, CHM1, CHMI, Leukocyte cell-derived chemotaxin 1, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

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


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


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


  1. Post-translational processing of bovine chondromodulin-I. Azizan, A., Holaday, N., Neame, P.J. J. Biol. Chem. (2001) [Pubmed]
  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. Aoyama, T., Okamoto, T., Nagayama, S., Nishijo, K., Ishibe, T., Yasura, K., Nakayama, T., Nakamura, T., Toguchida, J. J. Biol. Chem. (2004) [Pubmed]
  3. Specific loss of chondromodulin-I gene expression in chondrosarcoma and the suppression of tumor angiogenesis and growth by its recombinant protein in vivo. Hayami, T., Shukunami, C., Mitsui, K., Endo, N., Tokunaga, K., Kondo, J., Takahashi, H.E., Hiraki, Y. FEBS Lett. (1999) [Pubmed]
  4. Cartilage-specific matrix protein chondromodulin-I is associated with chondroid formation in salivary pleomorphic adenomas: immunohistochemical analysis. Kusafuka, K., Hiraki, Y., Shukunami, C., Yamaguchi, A., Kayano, T., Takemura, T. Am. J. Pathol. (2001) [Pubmed]
  5. Comparison of GC-Lect and modified Thayer-Martin media for isolation of Neisseria gonorrhoeae. Reichart, C.A., Rupkey, L.M., Brady, W.E., Hook, E.W. J. Clin. Microbiol. (1989) [Pubmed]
  6. Overlap in the functional neural systems involved in semantic and episodic memory retrieval. Rajah, M.N., McIntosh, A.R. Journal of cognitive neuroscience. (2005) [Pubmed]
  7. Reading fluent speech from talking faces: typical brain networks and individual differences. Hall, D.A., Fussell, C., Summerfield, A.Q. Journal of cognitive neuroscience. (2005) [Pubmed]
  8. Crystal structure of macrophage migration inhibitory factor from human lymphocyte at 2.1 A resolution. Sugimoto, H., Suzuki, M., Nakagawa, A., Tanaka, I., Nishihira, J. FEBS Lett. (1996) [Pubmed]
  9. Molecular cloning of human chondromodulin-I, a cartilage-derived growth modulating factor, and its expression in Chinese hamster ovary cells. Hiraki, Y., Mitsui, K., Endo, N., Takahashi, K., Hayami, T., Inoue, H., Shukunami, C., Tokunaga, K., Kono, T., Yamada, M., Takahashi, H.E., Kondo, J. Eur. J. Biochem. (1999) [Pubmed]
  10. Chondromodulin-I as a novel cartilage-specific growth-modulating factor. Hiraki, Y., Shukunami, C. Pediatr. Nephrol. (2000) [Pubmed]
  11. Expression of cartilage-specific functional matrix chondromodulin-I mRNA in rabbit growth plate chondrocytes and its responsiveness to growth stimuli in vitro. Shukunami, C., Hiraki, Y. Biochem. Biophys. Res. Commun. (1998) [Pubmed]
  12. Osteoclasts secrete the chemotactic cytokine mim-1. Falany, M.L., Thames, A.M., McDonald, J.M., Blair, H.C., McKenna, M.A., Moore, R.E., Young, M.K., Williams, J.P. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  13. Expression of the chondromodulin-I gene in chondrosarcomas. Aoyama, T., Okamoto, T., Nagayama, S., Nishijo, K., Ishibe, T., Yasura, K., Tsuboyama, T., Nakayama, T., Nakashima, Y., Nakamura, T., Toguchida, J. Cancer Lett. (2004) [Pubmed]
  14. Enzymatic ketonization of 2-hydroxymuconate: specificity and mechanism investigated by the crystal structures of two isomerases. Subramanya, H.S., Roper, D.I., Dauter, Z., Dodson, E.J., Davies, G.J., Wilson, K.S., Wigley, D.B. Biochemistry (1996) [Pubmed]
  15. Role of cartilage-derived anti-angiogenic factor, chondromodulin-I, during endochondral bone formation. Shukunami, C., Hiraki, Y. Osteoarthr. Cartil. (2001) [Pubmed]
  16. Cartilage-specific matrix protein, chondromodulin-I (ChM-I), is a strong angio-inhibitor in endochondral ossification of human neonatal vertebral tissues in vivo: relationship with angiogenic factors in the cartilage. Kusafuka, K., Hiraki, Y., Shukunami, C., Kayano, T., Takemura, T. Acta Histochem. (2002) [Pubmed]
  17. Noncollagenous, nonproteoglycan macromolecules of cartilage. Neame, P.J., Tapp, H., Azizan, A. Cell. Mol. Life Sci. (1999) [Pubmed]
  18. Angiogenesis inhibitors localized in hypovascular mesenchymal tissues: chondromodulin-I and tenomodulin. Hiraki, Y., Shukunami, C. Connect. Tissue Res. (2005) [Pubmed]
  19. Co-localization of chondromodulin-I (ChM-I) and bone morphogenetic protein-6 (BMP-6) in myoepithelial cells of canine mammary tumors. Kawabata, A., Okano, K., Uchida, K., Yamaguchi, R., Hayashi, T., Tateyama, S. J. Vet. Med. Sci. (2005) [Pubmed]
WikiGenes - Universities