Biology:SPARCL1
From HandWiki
Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
SPARC-like protein 1 (SPARCL1 or SC1), also known as hevin (short for high endothelial venule protein), is a secreted protein with high structural similarity to SPARC.[1][2] It interacts with the extracellular matrix to create intermediate states of cell adhesion.[3] Due to its dynamic extracellular roles, being implicated in cancer metastasis and inflammation, it is considered a matricellular protein.[4][5] In humans hevin is encoded by the SPARCL1 gene.[6][7]
Interactions
- CALY (calcyon)[8]
See also
- Thrombospondin
- Tenascin
References
- ↑ "Cloning from purified high endothelial venule cells of hevin, a close relative of the antiadhesive extracellular matrix protein SPARC". Immunity 2 (1): 113–23. January 1995. doi:10.1016/1074-7613(95)90083-7. PMID 7600298.
- ↑ "SC1/hevin. An extracellular calcium-modulated protein that binds collagen I". The Journal of Biological Chemistry 278 (13): 11351–8. March 2003. doi:10.1074/jbc.M212291200. PMID 12538579.
- ↑ "Matricellular hevin regulates decorin production and collagen assembly". The Journal of Biological Chemistry 281 (37): 27621–32. September 2006. doi:10.1074/jbc.M510507200. PMID 16844696.
- ↑ "Matricellular proteins and biomaterials". Matrix Biology 37: 183–91. July 2014. doi:10.1016/j.matbio.2014.03.002. PMID 24657843.
- ↑ "Hevin/SC1, a matricellular glycoprotein and potential tumor-suppressor of the SPARC/BM-40/Osteonectin family". The International Journal of Biochemistry & Cell Biology 36 (6): 991–6. June 2004. doi:10.1016/j.biocel.2004.01.017. PMID 15094114.
- ↑ "cDNA subtraction library construction using a magnet-assisted subtraction technique (MAST)". Trends in Genetics 9 (3): 70–1. March 1993. doi:10.1016/0168-9525(93)90216-5. PMID 8488563.
- ↑ "Entrez Gene: SPARCL1 SPARC-like 1 (mast9, hevin)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8404.
- ↑ "Hevin-calcyon interaction promotes synaptic reorganization after brain injury". Cell Death and Differentiation 28 (9): 2571–2588. March 2021. doi:10.1038/s41418-021-00772-5. ISSN 1350-9047. PMID 33753902.
Further reading
- "Modulation of endothelial cell adhesion by hevin, an acidic protein associated with high endothelial venules". The Journal of Biological Chemistry 271 (8): 4511–7. February 1996. doi:10.1074/jbc.271.8.4511. PMID 8626806.
- "Hevin is down-regulated in many cancers and is a negative regulator of cell growth and proliferation". British Journal of Cancer 82 (6): 1123–30. March 2000. doi:10.1054/bjoc.1999.1051. PMID 10735494.
- "Time-controlled transcardiac perfusion cross-linking for the study of protein interactions in complex tissues". Nature Biotechnology 22 (6): 724–31. June 2004. doi:10.1038/nbt969. PMID 15146195.
- "Functional proteomics mapping of a human signaling pathway". Genome Research 14 (7): 1324–32. July 2004. doi:10.1101/gr.2334104. PMID 15231748.
- "Interaction of myocilin with the C-terminal region of hevin". Biochemical and Biophysical Research Communications 339 (3): 797–804. January 2006. doi:10.1016/j.bbrc.2005.11.082. PMID 16316624.
- "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry". Journal of Proteome Research 4 (6): 2070–80. 2006. doi:10.1021/pr0502065. PMID 16335952.
- "Candidate gene analysis of SPARCL1 gene in patients with multiple sclerosis". Neuroscience Letters 425 (3): 173–6. October 2007. doi:10.1016/j.neulet.2007.08.020. PMID 17825989.
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