Literature DB >> 18855735

Caldesmon as a therapeutic target for proliferative vascular diseases.

Chi-Ming Hai1.   

Abstract

Caldesmon is a negative regulator of cell proliferation, migration, and metalloproteinase release. Caldesmon function is regulated by multiple kinases, targeting multiple phosphorylation sites. Recently, overexpression of caldesmon has been shown to inhibit neointimal formation after experimental angioplasty, suggesting that caldesmon may be a potential therapeutic target for proliferative vascular diseases.

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Year:  2008        PMID: 18855735      PMCID: PMC4322390          DOI: 10.2174/138955708786140981

Source DB:  PubMed          Journal:  Mini Rev Med Chem        ISSN: 1389-5575            Impact factor:   3.862


  84 in total

1.  Phosphorylation of caldesmon by p21-activated kinase. Implications for the Ca(2+) sensitivity of smooth muscle contraction.

Authors:  D B Foster; L H Shen; J Kelly; P Thibault; J E Van Eyk; A S Mak
Journal:  J Biol Chem       Date:  2000-01-21       Impact factor: 5.157

Review 2.  Cell cycle in vasculoproliferative diseases: potential interventions and routes of delivery.

Authors:  V Sriram; C Patterson
Journal:  Circulation       Date:  2001-05-15       Impact factor: 29.690

Review 3.  Targeting the protein kinase C family: are we there yet?

Authors:  Helen J Mackay; Christopher J Twelves
Journal:  Nat Rev Cancer       Date:  2007-07       Impact factor: 60.716

4.  Phosphorylation of smooth muscle caldesmon by calmodulin-dependent protein kinase II. Identification of the phosphorylation sites.

Authors:  M Ikebe; S Reardon
Journal:  J Biol Chem       Date:  1990-10-15       Impact factor: 5.157

5.  Phosphorylation by casein kinase II affects the interaction of caldesmon with smooth muscle myosin and tropomyosin.

Authors:  N V Bogatcheva; A V Vorotnikov; K G Birukov; V P Shirinsky; N B Gusev
Journal:  Biochem J       Date:  1993-03-01       Impact factor: 3.857

6.  Modulation of actin mechanics by caldesmon and tropomyosin.

Authors:  M J Greenberg; C-L A Wang; W Lehman; J R Moore
Journal:  Cell Motil Cytoskeleton       Date:  2008-02

7.  Genomic structure of the human caldesmon gene.

Authors:  K Hayashi; H Yano; T Hashida; R Takeuchi; O Takeda; K Asada; E Takahashi; I Kato; K Sobue
Journal:  Proc Natl Acad Sci U S A       Date:  1992-12-15       Impact factor: 11.205

8.  Dual mechanism of a natural CaMKII inhibitor.

Authors:  Rebekah S Vest; Kurtis D Davies; Heather O'Leary; J David Port; K Ulrich Bayer
Journal:  Mol Biol Cell       Date:  2007-10-17       Impact factor: 4.138

9.  Caldesmon suppresses cancer cell invasion by regulating podosome/invadopodium formation.

Authors:  T Yoshio; T Morita; Y Kimura; M Tsujii; N Hayashi; K Sobue
Journal:  FEBS Lett       Date:  2007-07-05       Impact factor: 4.124

10.  Localization of caldesmon and its dephosphorylation during cell division.

Authors:  N Hosoya; H Hosoya; S Yamashiro; H Mohri; F Matsumura
Journal:  J Cell Biol       Date:  1993-06       Impact factor: 10.539

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  1 in total

1.  Forkhead box O member FOXO1 regulates the majority of follicle-stimulating hormone responsive genes in ovarian granulosa cells.

Authors:  Maria K Herndon; Nathan C Law; Elyse M Donaubauer; Brandon Kyriss; Mary Hunzicker-Dunn
Journal:  Mol Cell Endocrinol       Date:  2016-06-17       Impact factor: 4.102

  1 in total

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