Properties and subcellular localization of adenosine diphosphatase in arterial smooth muscle cells in culture

Leake, David S.; Lieberman, G.E.; Peters, Timothy J.

doi:10.1016/0167-4889(83)90116-7

Cited by 27 publications

(1 citation statement)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In physiological conditions, elastin-rich extracellular matrix (ECM) is slowly degraded; however, this process is accelerated during ageing or pathological conditions such as inflammation, atherosclerosis, and carcinogenesis in the breast, skin, and lung [6][7][8][9]. Elastin is degraded by proteolytic enzymes produced by monocytes, thrombocytes, neutrophils, lymphocytes, smooth muscle cells, skin fibroblasts, certain malignant tumour cells, and cells of adipose tissue [10][11][12][13][14][15][16]. As a result of protease activity, elastin hydrolysis occurs, and during this process, elastin-derived peptides (EDPs) are released [17].…”

Section: Introductionmentioning

confidence: 99%

Elastin-derived peptide VGVAPG decreases differentiation of mouse embryo fibroblast (3T3-L1) cells into adipocytes

et al. 2020

View full text Add to dashboard Cite

Elastin is a highly elastic protein present in connective tissue. As a result of protease activity, elastin hydrolysis occurs, and during this process, elastin-derived peptides (EDPs) are released. One of the constitutively repeating elastin and EDP building sequences is the hexapeptide VGVAPG. Therefore, the aim of our research was to define the effect of VGVAPG peptide on adipogenesis in a mouse 3T3-L1 cell line. 3T3-L1 cells were differentiated according to a previously described protocol and exposed to increasing concentrations of VGVAPG or VVGPGA peptide. The obtained results showed that VGVAPG peptide does not stimulate reactive oxygen species (ROS) production, caspase-1 activation, and 3T3-L1 cell proliferation. In the second part of the experiments, it was proved that VGVAPG peptide decreased lipid accumulation as measured by oil red O staining, which was confirmed by the profile of increased expression markers of undifferentiated preadipocytes. In our experiments, 10 nM VGVAPG added for differentiating to adipocytes increased the expression of Pref-1, serpin E1, and adiponectin as compared to rosiglitazone (PPARγ agonist)-treated group and simultaneously decreased the expression of VEGF and resistin as compared to the rosiglitazone-treated group. The obtained results show that VGVAPG peptide sustains 3T3 cells in undifferentiated state.

show abstract

Section: Introductionmentioning

confidence: 99%

Elastin-derived peptide VGVAPG decreases differentiation of mouse embryo fibroblast (3T3-L1) cells into adipocytes

et al. 2020

View full text Add to dashboard Cite

show abstract

Subcellular localization of recently‐absorbed iron in mouse duodenal enterocytes: Identification of a basolateral membrane iron‐binding site

Snape

Simpson

1990

Cell Biochemistry & Function

View full text Add to dashboard Cite

The subcellular distribution of newly absorbed iron in isolated mouse duodenal enterocytes was investigated by analytical subcellular fractionation using sucrose density gradient centifugation. Two major peaks of mucosal 59Fe activity were observed: one soluble and one particulate (density 1.18-1.20 g ml-1). The latter was increased following prior exposure of animals to chronic hypoxia. The particulate 59Fe was localized to the basolateral membranes using the marker enzyme Na+, K+ activated, Mg2+ dependent, ATPase and by washing intact enterocytes with the selective plasma membrane perturbant digitonin. The basolateral membrane can be selectively labelled by in vitro incubation of intact enterocytes at 0 degrees C with 59Fe(III)-nitrilotriacetate complex, confirming the presence of a 59Fe binding site on this membrane. No significant difference in in vitro iron binding to this site was observed between normal and chronically hypoxic animals. Iron binding to the basolateral membrane was significantly higher in disrupted, compared to intact enterocytes, indicating that this site is present on both sides of the basolateral membrane. It is therefore suggested that the increased labelling of this site in hypoxia, in vivo, is a consequence of an increase in a mucosal Fe pool which is available for binding to a membrane receptor.

show abstract

Ectonucleotidases

Pearson

1985

Methods Used in Adenosine Research

View full text Add to dashboard Cite

Properties and subcellular localization of adenosine diphosphatase in arterial smooth muscle cells in culture

Cited by 27 publications

References 25 publications

Elastin-derived peptide VGVAPG decreases differentiation of mouse embryo fibroblast (3T3-L1) cells into adipocytes

Elastin-derived peptide VGVAPG decreases differentiation of mouse embryo fibroblast (3T3-L1) cells into adipocytes

Subcellular localization of recently‐absorbed iron in mouse duodenal enterocytes: Identification of a basolateral membrane iron‐binding site

Ectonucleotidases

Contact Info

Product

Resources

About