|COPE Homepage||Bottom of page||Previous entry:
egg laying abnormal-15
please show your appreciation
by donating what you can afford.
Hevin is a secreted acidic calcium-binding protein of 664 amino acids that shows 62 % identity with SPARC (Soderling et al, 1997). The protein is known also as SC1 [synaptic cleft-1] a protein identified by a polyclonal antibody specific for glycoproteins in the synaptic junction (Johnston et al, 1997), SPARC-like-1 (abbr. SPARCL1) or MAST9 (Isler et al, 2001; Bendik et al, 1998), RAGS1 antigen [radial glial stop signal molecule 1] (Gongidi et al, 2004), ECM2 [extracellular matrix protein 2], an extracellular matrix protein identified by virtue of its ability to bind to pre-B-cells (Oritani and Kincade, 1996). The quail ortholog has been identified as QR1.
The protein is expressed at high levels in high endothelial venules (HEV) in lymphoid tissues (Girard and Springer, 1995). In normal human and mouse tissues hevin shows a limited expression pattern. Expression is particularly dominant in dermis, ducts, vasculature, muscle, and brain. Hevin (SC1) mRNA is expressed widely in the brain and is present in many types of neurons (Johnston et al, 1997).
Purified Hevin does not support endothelial cell adhesion in vitro and soluble hevin inhibits attachment of endothelial cells to fibronectin substrates (Girard and Springer, 1996). Hevin also inhibits spreading of bovine aortic endothelial cells (Brekken et al, Hambrock et al (2003) have reported that hevin is expressed in osteosarcoma cells and binds collagen type 1.
Nelson et al (1998) have reported that expression of Hevin is downregulated in transformed prostate epithelial cell lines and metastatic prostate adenocarcinoma cells. Expression is downregulated also in non-small cell lung cancers (Bendik et al, 1998). Claeskens et al (2000) have reported that Hevin is downregulated in many cancers and that it acts as a negative regulator of cell growth and proliferation that can inhibit cell cycle progression. Gerritsen et al (2002) have reported that, in contrast to other tumors, Hevin expression is upregulated selectively in renal cell carcinomas.
Gongidi et al (2004) have reported that Hevin is expressed in glial cells and acts as a neuronal guidance molecule. It regulates the terminal phase of neuron migration in the cerebral cortex by providing anti-adhesive signals.
Oritani et al (1997) have reported that Hevin, which they called ECM2 [extracellular matrix protein 2], is a component of the extracellular matrix produced by bone marrow stromal cells and preferentially binds to pre-B-cells and improves the cloning efficiency of IL7 dependent B-cell precursors. The protein has no influence on myeloid progenitor cells. The protein also increases mitogen-dependent proliferation of mature B-cells when expressed as a transmembrane protein on fibroblasts (Oritani and Kincade, 1998).
McKinnon et al (2000) have reported that knock-out mice lacking expression of SC1 are born at the expected ratios, are fertile, and have no obvious histological abnormalities. Also, their long-term survival does not differ from littermate controls. Sullivan et al (2008) have shown that wound healing in hevin knock-out mice is faster than in wild-type animals, as evidenced by enhanced macrophage infiltration of wound beds at early time points and the earlier appearance of mature extracellular matrix. The differences in wound repair between hevin knock-out mice and wild-type animals can be attributed in part to the deadhesive function of hevin and reduced cell migration within dermal wound beds in which this protein is expressed.
Copyright © 2012 by H IBELGAUFTS. All rights reserved.
ENTRY LAST MODIFIED: April 2008
See REFERENCES for entry Hevin.
Click BACKLINKS to see which COPE entries contain the term Hevin .
|COPE Homepage||Top of Page|
|SUPPORT COPE | Intro | Subdictionaries | New Entries | Contribute data | COPE Credentials|
|COPE is interested in contacts with corporate sponsors appreciating and committed to communication biology|