Aptamer-Based Electrochemical Detection of Picomolar Platelet-Derived Growth Factor Directly in Blood Serum

Competition between 125I-labeled platelet-derived growth factor (PDGF) and unlabeled PDGF forms the basis of a specific "radio-receptor assay" for quantifying PDGF in clotted blood serum. Human clotted blood serum contains 15 ng/ml of PDGF by radio-receptor assay; this corresponds to a PDGF content of approximately 7.5 x 10(-5) pg per circulating platelet, a figure which is corroborated by purification data. Clotted blood sera from mammals, lower vertebrates and marine invertebrates were screened for homologues of human PDGF by radio-receptor assay. All tested specimens from phylum Chordata contain a mitogenic agent that competes with human PDGF for receptor binding. Sera from tunicates down on the chordate line of evolution and sera from all tested animals on the arthropod line of development were negative. The phylogenetic distribution of PDGF homologue does not correlate with platelet distribution since platelets and their precursor cell--the bone marrow megacaryocyte--are unique to the mammalian hematopoietic system. One anatomical feature appearing coordinately with PDGF on the vertebrate line of development is a pressurized circulatory system. The coincidental appearance of these features may lend support to the hypothesis that PDGF plays a role in maintenance and repair of the vascular lining in vivo.

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Role of serum components in density-dependent inhibition of growth of cells in culture. Platelet-derived growth factor is the major serum determinant of saturation density

The Journal of Cell Biology ◽

10.1083/jcb.85.2.377 ◽

1980 ◽

Vol 85 (2) ◽

pp. 377-385 ◽

Cited By ~ 67

Author(s):

A Vogel ◽

R Ross ◽

E Raines

Keyword(s):

Growth Factors ◽

Growth Factor ◽

Blood Serum ◽

Cell Density ◽

Whole Blood ◽

Saturation Density ◽

Platelet Derived Growth Factor ◽

3T3 Cells ◽

Density Dependent ◽

Dependent Inhibition

The effects of platelet-derived growth factor and plasma components on saturation density in cultures of 3T3 cells were investigated. Both of these components of whole blood serum affect saturation density; however, when 3T3 cells become quiescent at high density in medium containing whole blood serum, only platelet-derived growth factor and fresh whole blood serum are capable of stimulating proliferation. Addition of fresh plasma- derived serum has little effect on cell growth. These results suggest that the platelet factor is the major determinant of saturation density in cultures of 3T3 cells maintained in medium supplemented with whole blood serum. Experiments were performed to investigate the mechanism by which platelet-derived growth factor regulates saturation density. We investigated the possibilities of inactivation of growth factors by proliferating cells, and the effects of cell density on the response of 3T3 cells to platelet-derived growth factor. The amount of platelet- derived growth factor required to initiated DNA synthesis increases with increasing cell density. Some inactivation of growth factors by growing cells was detected, but this depletion was only evident at high cell density. We propose that density-dependent inhibition in cultured 3T3 cells is the result both of an increased requirement for the platelet- derived growth factor as the cultures become more crowded and of inactivation of growth factor activity by growing cells.

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Comparison between Vascular Endothelial Growth Factor and Platelet-Derived Growth Factor Levels in Rhegmatogenous Retinal Detachment

Journal of Ophthalmology ◽

10.1155/2021/2688837 ◽

2021 ◽

Vol 2021 ◽

pp. 1-7

Author(s):

Andi Muhammad Ichsan ◽

Dyah Ayu Windy ◽

Habibah Setyawati Muhiddin ◽

Budu ◽

Muhammad Nasrum Massi ◽

...

Keyword(s):

Vascular Endothelial Growth Factor ◽

Growth Factor ◽

Retinal Detachment ◽

Blood Serum ◽

Rhegmatogenous Retinal Detachment ◽

Platelet Derived Growth Factor ◽

Enzyme Linked Immunosorbent Assay ◽

Vascular Endothelial ◽

The Mean ◽

Endothelial Growth Factor

Introduction. This study aimed to assess vascular endothelial growth factor (VEGF) and platelet-derived growth factor (PDGF) levels within vitreous and blood serum samples of patients with rhegmatogenous retinal detachment (RRD) and their relationship to the development of proliferative vitreoretinopathy (PVR). Methods. Seventeen eyes of patients with RRD were included in the RRD group and divided into three subgroups: RRD without PVR, RRD with PVR grades A and B, and RRD with PVR grade C. Five control eyes (nucleus and intraocular lens drop) were included in this study. Blood serum and vitreous samples were collected during vitrectomy. VEGF-A and PDGF-AA levels were determined by enzyme-linked immunosorbent assay. Results. The mean vitreous VEGF-A level in the RRD group was 131.71 ± 58.25 pg/mL, and the mean vitreous PDGF-AA level was 174.62 ± 65.17 pg/mL. Both levels were significantly higher in the RRD group compared with the control group ( p < 0.05 ). Vitreous VEGF-A and PDGF-AA levels were the highest in RRD with PVR grade C subgroup, with mean levels of 179.87 ± 21.02 pg/mL and 229.44 ± 14.09 pg/mL, respectively ( p < 0.05 ). The vitreous VEGF-A/PDGF-AA ratios in the RRD subgroups were completely different. Conclusion. Based on the tendency of VEGF-A and PDGF-AA levels, RRD surgery has to be performed as soon as possible prior to retinal cell death and membrane proliferative formation.

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Dual signal amplification strategy for electrochemical detection of platelet-derived growth factor BB

Analytical Methods ◽

10.1039/c7ay02513k ◽

2017 ◽

Vol 9 (46) ◽

pp. 6569-6573 ◽

Cited By ~ 5

Author(s):

Bin Xie ◽

Ning Zhou ◽

Rong Ding ◽

Yuanchao Zhao ◽

Bohan Zhang ◽

...

Keyword(s):

Alkaline Phosphatase ◽

Growth Factor ◽

Electrochemical Detection ◽

Signal Amplification ◽

Electrochemical Immunosensor ◽

Platelet Derived Growth Factor ◽

Amplification Strategy ◽

Dual Signal Amplification

An electrochemical immunosensor for the platelet-derived growth factor BB (PDGF-BB) is reported based on dual signal amplification of aptamers and alkaline phosphatase.

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