scholarly journals EFFECT OF THE AMINO ACIDS AND DIALYZABLE CONSTITUENTS OF EMBRYONIC TISSUE JUICE ON THE GROWTH OF FIBROBLASTS

1926 ◽  
Vol 44 (3) ◽  
pp. 397-407 ◽  
Author(s):  
Lillian E. Baker ◽  
Alexis Carrel
Keyword(s):  
Amino Acids ◽  
Cell Migration ◽  
Active Cell ◽  
Embryonic Tissue ◽  
Tissue Extract ◽  
Considerable Part ◽  
Support Cell ◽  
Cell Life ◽  
Growth Promoting

The ultrafilterable constituents of embryonic tissue extract are unable to support cell life in vitro. They stimulate cell migration and possibly multiplication, without increasing the mass of the tissue. Embryonic tissue extract freed from amino acids by dialysis still retains a considerable part of its growth-promoting properties. The area of growth of tissues in embryonic tissue extract free from amino acids is appreciably less than that with the whole extract, probably owing to the denaturation of part of the protein, or perhaps to the inactivation or loss of an enzyme. The addition of either the ultrafilterable components or an artificial mixture of amino acids to this dialyzed extract increases the area of cell migration but does not restore all the activity lost on dialysis. The observed differences in growth of tissue, due to the addition or removal of dialyzable and ultrafilterable constituents of the extract, prove that the amino acids produce a more active cell migration and possibly multiplication, but no building up of new protoplasm.

scholarly journals ACTION ON FIBROBLASTS OF THE PROTEIN FRACTION OF EMBRYONIC TISSUE EXTRACT

1926 ◽  
Vol 44 (3) ◽  
pp. 387-395 ◽  
Author(s):  
Lillian E. Baker ◽  
Alexis Carrel
Keyword(s):  
Amino Acids ◽  
Protein Fraction ◽  
Nitrogen Concentration ◽  
Embryonic Tissue ◽  
Tissue Extract ◽  
Protein Nitrogen ◽  
Continuous Growth ◽  
Long Time ◽  
Embryo Tissue

The above experiments indicate that the growth-stimulating substance found in embryonic tissue extract, which has been responsible for the continuous growth of fibroblasts in vitro for 14 years, is either protein in nature or closely associated with the protein of the extract and adsorbed by it. If any specific hormone responsible for cell division is present, it is united to the protein or carried along with it in its first precipitation. It seems probable that the tissues utilize this protein for the nitrogen which they build into protoplasm. Whether it is first hydrolyzed before adsorption by the tissues has not been ascertained as yet. It has been shown in other experiments reported in the following paper that the amino acids of the tissue juice do not suffice for the growth of fibroblasts and that hydrolyzed tissue juice is toxic in the same way that a too concentrated mixture of amino acids is toxic. The results of the foregoing experiments may be summarized as follows: 1. Fractionation of embryo tissue juice has shown that it is the protein fraction that contains the activating substance. 2. Tissues continue to grow for a long time in the protein of the extract precipitated by CO2 and at a rate approximately equal to that in the original extract diluted to the same nitrogen concentration. 3. The non-protein nitrogen gives slight stimulation to growth. 4. Purification of the protein by repeated precipitation destroys its growth-promoting properties, but whether this is due to a denaturing of the protein,—which occurs very readily,—or to loss of some substance possibly an enzyme attached to it, has not been ascertained. 5. Preparations of purified proteins from embryonic tissue and egg white have shown no marked nutritive or stimulating action. A number of other pure substances have been tried without effect.

Necessary amino acids and vitamins for the growth of human diploid fibroblasts

1979 ◽  
Vol 40 (1) ◽  
pp. 281-291
Author(s):  
J. Litwin
Keyword(s):  
Amino Acids ◽  
Growth Rate ◽  
Folic Acid ◽  
Cell Growth ◽  
Calf Serum ◽  
Life Time ◽  
Lung Fibroblasts ◽  
Human Diploid Fibroblasts ◽  
Support Cell

Only 2 amino acids and one vitamin were found to be essential for the growth of human embryonic diploid lung fibroblasts when 10% undialysed calf serum was used as a medium supplement. These amino acids were either glutamine + cysteine or serine + homocysteine. Replacing cysteine or homocysteine with cystine or homocystine, respectively, reduced growth. The growth rate in the glutamine + cysteine medium was slightly less than that in Eagle's medium, but the in vitro life time was similar. Folic acid was the only vitamin needed to support cell growth in vitro. The addition of other vitamins had no stimulatory effect with the possible exception of nicotinamide. When other amino acids were added to glutamine + cysteine none showed stimulatory effects but tryptophan was either toxic or inhibitory for the 3 human diploid strains examined. Serine was inhibitory for WI-38 but not for MRC5 cells. Subtle nutritional differences appear to exist between fibroblasts of the same type obtained from different embryos.

scholarly journals NITROGEN METABOLISM OF NORMAL AND SARCOMATOUS FIBROBLASTS IN PURE CULTURES

1928 ◽  
Vol 48 (4) ◽  
pp. 533-547 ◽  
Author(s):  
Lillian E. Baker ◽  
Alexis Carrel
Keyword(s):  
Amino Acids ◽  
Protein Degradation ◽  
Nitrogen Metabolism ◽  
Degradation Products ◽  
Protein Molecule ◽  
Pure Cultures ◽  
Growth Promoting

1. Both normal and sarcomatous fibroblasts of the rat utilize many different fragments of the protein molecule for their growth in vitro. Alpha and beta proteoses have approximately equal growth-promoting power. 2. A mixture of peptones, peptides, and amino acids, containing a negligible quantity of proteose, produces a temporary proliferation of normal fibroblasts, and an unlimited multiplication of sarcomatous fibroblasts, provided these substances are derived from liver which contains products of unknown nature that complete the nutritive effect of the protein degradation products. 3. Amino acids contribute to the nutrition of the cells, but are unable without the addition of peptides or polypeptides to support their life. 4. The proteolytic products are more toxic to normal than to sarcomatous fibroblasts. The hypothesis is suggested that the greater acidity produced by the large glycolysis of the sarcomatous cells may account for this difference through altering the speed of action of protein synthetizing enzymes.

Studies on the Growth of Tissues in vitro

1939 ◽  
Vol 16 (1) ◽  
pp. 60-70
Author(s):  
O. A. TROWELL ◽  
E. N. WILLMER
Keyword(s):  
Bone Marrow ◽  
Tissue Extract ◽  
Brain Extract ◽  
Rate Of Growth ◽  
Tissue Extracts ◽  
Growth Promoting ◽  
Nuclear Content

1. Tissue extracts have been made from several organs of growing and adult fowls, and the growth-promoting properties of these extracts have been tested on periosteal fibroblasts growing in vitro. 2. The growth-promoting properties are most pronounced in brain extract and diminish in the sequence: thyroid, thymus, testis, ovary, bone marrow, liver, kidney and muscle extracts. Extracts made from the spleens of adult cocks were found to be far more efficient growth-promoting agents than extracts made from the spleens of young birds. 3. The growth-promoting power of a tissue extract cannot always be correlated with the age of the tissue from which the extract was made, with the rate of growth of that tissue, nor with its nuclear content.

Neutrophil migration through in vitro interstitial matrix

1992 ◽  
Vol 50 (1) ◽  
pp. 894-895
Author(s):  
J. Roemer ◽  
S.R. Simon
Keyword(s):  
Extracellular Matrix ◽  
Smooth Muscle ◽  
Cell Migration ◽  
Smooth Muscle Cells ◽  
Inflammatory Cell ◽  
Neutrophil Migration ◽  
Culture Conditions ◽  
Aortic Smooth Muscle ◽  
Specific Culture

We are developing an in vitro interstitial extracellular matrix (ECM) system for study of inflammatory cell migration. Falcon brand Cyclopore membrane inserts of various pore sizes are used as a support substrate for production of ECM by R22 rat aortic smooth muscle cells. Under specific culture conditions these cells produce a highly insoluble matrix consisting of typical interstitial ECM components, i.e.: types I and III collagen, elastin, proteoglycans and fibronectin.

The Migration of Human Smooth Muscle Cells In Vitro Is Mediated by Plasminogen Activation and Can Be Inhibited by α2-Macroglobulin Receptor Associated Protein

1997 ◽  
Vol 78 (02) ◽  
pp. 880-886 ◽  
Author(s):  
Monique J Wijnberg ◽  
Paul H A Quax ◽  
Nancy M E Nieuwenbroek ◽  
Jan H Verheijen
Keyword(s):  
Smooth Muscle ◽  
Cell Migration ◽  
Smooth Muscle Cell ◽  
Muscle Cell ◽  
Ldl Receptor ◽  
Migration And Invasion ◽  
Invasion Assay ◽  
Plasminogen Activation ◽  
Smooth Muscle Cell Migration

SummaryThe plasminogen activation system is thought to be important in cell migration processes. A role for this system during smooth muscle cell migration after vascular injury has been suggested from several animal studies. However, not much is known about its involvement in human vascular remodelling. We studied the involvement of the plasminogen activation system in human smooth muscle cell migration in more detail using an in vitro wound assay and a matrix invasion assay. Inhibition of plasmin activity or inhibition of urokinase-type plasminogen activator (u-PA) activity resulted in approximately 40% reduction of migration after 24 h in the wound assay and an even stronger reduction (70-80%) in the matrix invasion assay. Migration of smooth muscle cells in the presence of inhibitory antibodies against tissue-type plasminogen activator (t-PA) was not significantly reduced after 24 h, but after 48 h a 30% reduction of migration was observed, whereas in the matrix invasion assay a 50% reduction in invasion was observed already after 24 h. Prevention of the interaction of u-PA with cell surface receptors by addition of soluble u-PA receptor or α2-macroglobulin receptor associated protein (RAP) to the culture medium, resulted in a similar inhibition of migration and invasion. From these results it can be concluded that both u-PA and t-PA mediated plasminogen activation can contribute to in vitro human smooth muscle cell migration and invasion. Furthermore, the interaction between u-PA and its cell surface receptor appears also to be involved in this migration and invasion process. The inhibitory effects on migration and invasion by the addition of RAP suggests an involvement of a RAP sensitive receptor of the LDL receptor family, possibly the LDL-receptor related protein (LRP) and/or the VLDL receptor.

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