2003
DOI: 10.1074/jbc.m212291200
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SC1/Hevin

Abstract: SC1, a member of the BM-40 family of extracellular matrix proteins, was recombinantly expressed in a eukaryotic expression system. The full-length protein as well as truncated versions were purified to homogeneity under non-denaturing conditions. Matrix-assisted laser desorption ionization time-of-flight mass spectrometry of full-length SC1 revealed a mass of 87.8 kDa of which 16.8 kDa is contributed by posttranslational modifications. In electron microscopy, after negative staining, SC1 was revealed as a glob… Show more

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Cited by 76 publications
(35 citation statements)
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References 29 publications
(29 reference statements)
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“…Sparcl1, which was also overexpressed in purified BFCN, is highly expressed in the developing and adult CNS and contains one follistatin domain (49); thus, like noggin, it may interact with BMPs. The rise in Sparcl1 expression upon treatment with BMP9, preceding those of Col1a1 and Hspb8, may not be surprising because SPARC (secreted protein, acidic, cysteine-rich) can bind to collagen type I and regulate its production (50). In this regard, it should be pointed out that BMP9 induced the concerted expression of genes associated with the laying down of extracellular collagen matrix.…”
Section: Discussionmentioning
confidence: 99%
“…Sparcl1, which was also overexpressed in purified BFCN, is highly expressed in the developing and adult CNS and contains one follistatin domain (49); thus, like noggin, it may interact with BMPs. The rise in Sparcl1 expression upon treatment with BMP9, preceding those of Col1a1 and Hspb8, may not be surprising because SPARC (secreted protein, acidic, cysteine-rich) can bind to collagen type I and regulate its production (50). In this regard, it should be pointed out that BMP9 induced the concerted expression of genes associated with the laying down of extracellular collagen matrix.…”
Section: Discussionmentioning
confidence: 99%
“…This hypothesis had been demonstrated by many researches. Hambrock et al reported SPARCL1 in the extracellular matrix (ECM) tethers to the collagen ECM [28]. Hurley et al and his colleagues demonstrate that SPARCL1 in the ECM limited cellular ability to form focal adhesions on the collagen matrix and thereby attenuated corresponding biophysical dynamics of the cytoskeletal framework, which have been shown to potentiate migration [29].…”
Section: Discussionmentioning
confidence: 99%
“…33 SPRL1 is also known to bind collagen-I 34 and can regulate decorin production and collagen assembly. 35 In cancer, the role of SPRL1 remains poorly understood.…”
Section: ■ Discussionmentioning
confidence: 99%