Literature DB >> 8606489

SM-20 is a novel 40-kd protein whose expression in the arterial wall is restricted to smooth muscle.

S D Wax1, L Tsao, M E Lieb, J T Fallon, M B Taubman.   

Abstract

We have previously reported the identification of a novel cDNA, SM-20, whose corresponding mRNA levels are regulated by growth factors in rat aortic smooth muscle cell (SMC) culture. Affinity-purified polyclonal and monoclonal antibodies were made against a 230 amino acid region of the SM-20 putative peptide expressed in the bacterial vector, pET-3b. Western blot analyses of rat and human SMC lysates detected a single protein species of approximately 40 kd. SM-20 was not detected in concentrates of the culture medium. By immunohistochemistry, SM-20 was localized to filaments in the cytoplasm of cultured SMC. Like SM-20 mRNA, levels of SM-20 protein were increased 1-3 hours after serum stimulation of rat aortic SMC. In rat tissues, SM-20 antigen was detected in abundance in smooth, cardiac, and skeletal muscle. SM-20 was also detected in some epithelial cells of the kidney, pancreas, gastrointestinal tract, and skin, but was not found in the parenchyma of the liver, spleen, or testis. In the rat arterial wall, SM-20 antigen was restricted to the SMC of the media and, after balloon arterial injury, was found most abundantly in the neointima. In human atherosclerotic coronary arteries, SM-20 antigen predominated in the SMC of the intimal plaques and was not detected in macrophages, endothelium, or adventitial cells. Thus, SM-20 encodes a protein which serves as a novel SMC-specific marker within the vessel wall.

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Year:  1996        PMID: 8606489

Source DB:  PubMed          Journal:  Lab Invest        ISSN: 0023-6837            Impact factor:   5.662


  9 in total

1.  SM-20 is a novel growth factor-responsive gene regulated during skeletal muscle development and differentiation.

Authors:  M C Moschella; K Menzies; L Tsao; M A Lieb; J D Kohtz; D S Kohtz; M B Taubman
Journal:  Gene Expr       Date:  1999

2.  Prolyl hydroxylase PHD3 activates oxygen-dependent protein aggregation.

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Authors:  C Darby; C L Cosma; J H Thomas; C Manoil
Journal:  Proc Natl Acad Sci U S A       Date:  1999-12-21       Impact factor: 11.205

4.  Characterization of different isoforms of the HIF prolyl hydroxylase PHD1 generated by alternative initiation.

Authors:  Ya-Min Tian; David R Mole; Peter J Ratcliffe; Jonathan M Gleadle
Journal:  Biochem J       Date:  2006-07-01       Impact factor: 3.857

Review 5.  Hypoxia, hypoxia-inducible factors (HIF), HIF hydroxylases and oxygen sensing.

Authors:  James D Webb; Mathew L Coleman; Christopher W Pugh
Journal:  Cell Mol Life Sci       Date:  2009-09-12       Impact factor: 9.261

6.  Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor.

Authors:  Mircea Ivan; Thomas Haberberger; David C Gervasi; Kristen S Michelson; Volkmar Günzler; Keiichi Kondo; Haifeng Yang; Irina Sorokina; Ronald C Conaway; Joan W Conaway; William G Kaelin
Journal:  Proc Natl Acad Sci U S A       Date:  2002-09-26       Impact factor: 11.205

Review 7.  The role of HIF prolyl hydroxylases in tumour growth.

Authors:  Terhi Jokilehto; Panu M Jaakkola
Journal:  J Cell Mol Med       Date:  2010-02-22       Impact factor: 5.310

8.  Loss of PHD3 in myeloid cells dampens the inflammatory response and fibrosis after hind-limb ischemia.

Authors:  Angelika Beneke; Annemarie Guentsch; Annette Hillemann; Anke Zieseniss; Lija Swain; Dörthe M Katschinski
Journal:  Cell Death Dis       Date:  2017-08-10       Impact factor: 8.469

Review 9.  Neuronal apoptosis by prolyl hydroxylation: implication in nervous system tumours and the Warburg conundrum.

Authors:  Susanne Schlisio
Journal:  J Cell Mol Med       Date:  2009-08-19       Impact factor: 5.310

  9 in total

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