Haemopoietic colony stimulation factors promote cell survival by suppressing apoptosis

Article Abstract:

Hemopoietic precursor cells, or stem cells, develop into mature blood cells, including both red cells and white blood cells. The development, growth, and survival of the precursor cells depend on factors or molecules known as colony stimulating factors (CSFs). It has been shown that CSFs promote cell survival by the suppression of apoptosis, or self-destruction of the cells. Apoptosis is characterized at the cellular level by: degradation of DNA, deoxyribose nucleic acid, the material of genes; condensation of chromatin, the material from which chromosomes (the structural units which contain the genes of the cell) are formed; and loss of the microvilli, or tiny projections of the plasma membrane of the cell. Apoptosis is an active process which, in many systems, is dependent on the synthesis of proteins involved in cell death. This study demonstrates that apoptosis is suppressed by a number of the CSFs including IL-3 (interleukin-3), GM-CSF (granulocyte-macrophage colony stimulating factor), and G-CSF (granulocyte colony stimulating factor). If these factors are removed from the medium in which the cells grow, the cells undergo apoptosis. Therefore, CSFs regulate the survival of precursor cells. CSFs can be used to regulate or stimulate normal hematopoiesis in patients whose precursor cells, or stem cells, have been destroyed by various conditions such as radiation. The removal or inhibition of CSFs can also as be used to suppress cell growth in various cancers affecting precursor blood cells. (Consumer Summary produced by Reliance Medical Information, Inc.)

Cancer research, Growth, Cancer, Hematopoietic stem cells, Blood cells, Colony-stimulating factors (Physiology), Colony-stimulating factors, Interleukin-3

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Regulation of cell adhesion and anchorage-dependent growth by a new beta1-integrin-linked protein kinase

Article Abstract:

A beta1-integrin-linked kinase (ILK) modulates integrin-mediated signal transduction, affects extracellular matrix cell adhesion, and increases anchorage-dependent growth. A two-hybrid screen to separate genes coding proteins interacting with the beta-1-integrin region gives a novel serine/threonine protein kinase. The protein has four ankyrin-like repeats, and phosphorylates a beta-1-integrin cytoplasmic peptide. The kinase coimmunoprecipitates with beta-1 in lysates of mammalian cells.

Molecular biology, Protein kinases, Cell adhesion

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A central control for cell growth

Article Abstract:

Graves and colleagues have described a previously unknown link between an enzyme essential in nucleotide synthesis and a growth factor induced signal transduction pathway. The activity of the enzyme carbamoyl phosphate synthetase II (CPS II) was found to increase after cells were exposed to the epidermal growth factor. Extracellular-signal-regulated kinase (ERK) mitogen-activated protein (MAP) is shown to be responsible for these effects.

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