Regulation of chicken α and β actin genes and their hybrids inserted into myogenic mouse cells

Sharp, Sandra B.; Kost, Thomas A.; Hughes, Stephen H.; Davidson, Norman

doi:10.1016/0378-1119(89)90293-x

Cited by 6 publications

(2 citation statements)

References 28 publications

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“…It has been demonstrated that the expression of ANGPTL2 in the skin genetically engineered mice model was responsible for chronic inflammation through the NF-κB cascade. Finally, in ligamentum flavum ANGPTL2 stimulation promoted NF-κB nuclear translocation and induced IL-6 expression and secretion promoting tissue inflammation [ 94 ].…”

Section: Angptl Proteins In Inflammation and Cancermentioning

confidence: 99%

Angiopoietin-Like Proteins in Angiogenesis, Inflammation and Cancer

Carbone

Piro

Merz

et al. 2018

IJMS

170

174

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Altered expression of secreted factors by tumor cells or cells of the tumor microenvironment is a key event in cancer development and progression. In the last decade, emerging evidences supported the autocrine and paracrine activity of the members of the Angiopoietin-like (ANGPTL) protein family in angiogenesis, inflammation and in the regulation of different steps of carcinogenesis and metastasis development. Thus, ANGPTL proteins become attractive either as prognostic or predictive biomarkers, or as novel target for cancer treatment. Here, we outline the current knowledge about the functions of the ANGPTL proteins in angiogenesis, cancer progression and metastasis. Moreover, we discuss the most recent evidences sustaining their role as prognostic or predictive biomarkers for cancer therapy. Although the role of ANGPTL proteins in cancer has not been fully elucidated, increasing evidence suggest their key effects in the proliferative and invasive properties of cancer cells. Moreover, given the common overexpression of ANGPTL proteins in several aggressive solid tumors, and their role in tumor cells and cells of the tumor microenvironment, the field of research about ANGPTL proteins network may highlight new potential targets for the development of future therapeutic strategies.

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Section: Angptl Proteins In Inflammation and Cancermentioning

confidence: 99%

Angiopoietin-Like Proteins in Angiogenesis, Inflammation and Cancer

Carbone

Piro

Merz

et al. 2018

IJMS

170

174

View full text Add to dashboard Cite

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“…The filters were hybridized for 16 h in the same solution containing one of the following random oligonucleotide-labeled [Feinberg and Vogelstein, 19831 [32PldATP probes as indicated in the Results: 1) a gel-purified (Nu-Sieve agarose, FMC Corp., Rockland, ME), 160 bp subfragment from pMctVSM-1 containing only the 3'-UT region sequence from the mouse VSM a-actin cDNA. 2) A gel-purified 688 bp subfragment of pEMSV688SK (J.C. Reeser, Ph.D. thesis) encompassing the 5'-UT region (exon 1) with the adjacent 5'-flanking region and intron 1 sequences from the mouse skeletal a-actin gene [Sharp et al, 1989;Hu et al, 19861. This 688 bp fragment was subcloned from the parent M13 clone 18-5 (generously provided by Dr. Sandra Sharp, California State University at Los Angeles) and placed into pEMSV to facilitate plasmid propagation.…”

Section: Analyses Of Actin Mrnamentioning

confidence: 99%

Density‐Dependent modulatioon of vascular smooth muscle α‐actin biosynthetic processing in differntiated BC3H1 myogenic cells

Strauch

Min

Reeser

et al. 1992

J of Cellular Biochemistry

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The expression of vascular smooth muscle (VSM) alpha-actin mRNA during BC3H1 myogenic cell differentiation is specifically stimulated by conditions of high cell density. Non-proteolytic dissociation of cell-cell and cell-matrix contacts in post-confluent cultures of BC3H1 myocytes using EDTA promotes loss of the differentiated morphological phenotype. EDTA-dispersed myocytes exhibit an undifferentiated fibroblastoid appearance and contained reduced levels of both VSM and skeletal alpha-actin mRNA. Muscle alpha-actin mRNA levels in EDTA-dispersed myocytes were not restored to that observed in confluent myocyte preparations by experimental manipulation of cell density conditions. Pulse-labeling techniques using L-[35S]cysteine to identify muscle actin biosynthetic intermediates revealed that EDTA-dispersed myocytes expressed nascent forms of both the VSM and skeletal muscle alpha-actin polypeptide chains. However EDTA-dispersed myocytes were less efficient in the post-translational processing of immature VSM alpha-actin compared to non-dispersed myocytes. Simple cell-to-cell contact may mediate VSM alpha-actin processing efficiency since high-density preparations of EDTA-dispersed myocytes processed more VSM alpha-actin intermediate than myocytes plated at low density. The actin isoform selectivity of the response to modulation of intercellular contacts suggests that actin biosynthesis in BC3H1 myogenic cells involves mechanisms capable of discriminating between different isoform classes of nascent actin polypeptide chains.

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