Dermatopontin is a protein that in humans is encoded by the DPTgene.[1][2]
Function
Dermatopontin is an extracellular matrix protein with possible functions in cell-matrix interactions and matrix assembly. The protein is found in various tissues and many of its tyrosine residues are sulphated. Dermatopontin is postulated to modify the behavior of TGF beta through interaction with decorin.[2]
References
↑Superti-Furga A, Rocchi M, Schafer BW, Gitzelmann R (Oct 1993). "Complementary DNA sequence and chromosomal mapping of a human proteoglycan-binding cell-adhesion protein (dermatopontin)". Genomics. 17 (2): 463–7. doi:10.1006/geno.1993.1348. PMID8104875.
Pochampally RR, Ylostalo J, Penfornis P, et al. (2007). "Histamine receptor H1 and dermatopontin: new downstream targets of the vitamin D receptor". J. Bone Miner. Res. 22 (9): 1338–49. doi:10.1359/jbmr.070605. PMID17547532.
Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. doi:10.1038/nature04727. PMID16710414.
Shaheduzzaman S, Krishnan V, Petrovic A, et al. (2002). "Effects of HIV-1 Nef on cellular gene expression profiles". J. Biomed. Sci. 9 (1): 82–96. doi:10.1007/BF02256581. PMID11810028.
Kuroda K, Okamoto O, Shinkai H (1999). "Dermatopontin expression is decreased in hypertrophic scar and systemic sclerosis skin fibroblasts and is regulated by transforming growth factor-beta1, interleukin-4, and matrix collagen". J. Invest. Dermatol. 112 (5): 706–10. doi:10.1046/j.1523-1747.1999.00563.x. PMID10233760.
Forbes EG, Cronshaw AD, MacBeath JR, Hulmes DJ (1994). "Tyrosine-rich acidic matrix protein (TRAMP) is a tyrosine-sulphated and widely distributed protein of the extracellular matrix". FEBS Lett. 351 (3): 433–6. doi:10.1016/0014-5793(94)00907-4. PMID8082810.