Hostname: page-component-78c5997874-s2hrs Total loading time: 0 Render date: 2024-11-04T20:13:23.493Z Has data issue: false hasContentIssue false

The effect of maternal nutrition on foetal serum potency in cell culture

Published online by Cambridge University Press:  02 September 2010

M. F. Thomas
Affiliation:
AgResearch, Ruakura Agricultural Research Centre, Private Bag 3123, Hamilton, New Zealand
M. H. Oliver
Affiliation:
AgResearch, Ruakura Agricultural Research Centre, Private Bag 3123, Hamilton, New Zealand
S. C. Hodgkinson
Affiliation:
AgResearch, Ruakura Agricultural Research Centre, Private Bag 3123, Hamilton, New Zealand
Get access

Abstract

The influence of pre-slaughter nutrition on the potency of foetal serum in cell culture was studied. Ewes carrying late-gestation foetuses (120-day gestation) were either fasted for 66 h (F), fasted for 66 h but drenched with Ketol, a propylene glycol preparation, (5 × 120 ml doses; FK), given food ad libitum (A), or given food ad libitum and drenched with Ketol (5 × 120 ml doses; AK). Following slaughter foetal blood was collected for the determination of potency in cell culture using industry-standard cell culture bioassays: cloning efficiency, plating efficiency and a 96 h cell proliferation assay. Foetal serum insulin-like growth factor (IGF) concentrations were also measured. Pre-slaughter fasting or drenching with Ketol had no effect on the potency of foetal serum in any of the cell culture bioassays. Fasting significantly lowered foetal plasma IGF-1 levels (F < 0·01). Foetal IGF-2 levels were unaffected by fasting or drenching with Ketol.

Type
Research Article
Copyright
Copyright © British Society of Animal Science 1997

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Barnes, D. and Sato, G. 1980a. Serum free cell culture: a unifying approach. Cell 22: 649655.Google Scholar
Barnes, D. and Sato, G. 1980b. Methods for growth of cultured cells in serum-free medium. Analytical Biochemistry 102: 255270.CrossRefGoogle ScholarPubMed
Battaglia, F. C. and Meschia, G. 1988. Fetal nutrition. Annual Review of Nutrition 8:4361.CrossRefGoogle ScholarPubMed
Buswell, J. F., Haddy, J. P. and Bywater, R. J. 1986. Treatment of pregnancy toxaemia in sheep using a concentrated oral rehydration solution. The Veterinary Record 118: 208209.Google Scholar
Fant, M., Salafia, C., Baxter, R. C., Schwander, J., Vogel, C., Fezzullo, J. and Moya, F. 1993. Circulating levels of the IGFs and IGF binding proteins in human cord serum: relationships to intrauterine growth. Regulatory Peptides 48: 2939.CrossRefGoogle ScholarPubMed
Gallaher, B. W., Breier, B. H., Oliver, M. H., Harding, J. E. and Gluckman, P. D. 1992. Ontogenic differences in the nutritional regulation of circulating IGF binding proteins in sheep plasma. Acta Endocrinologka 126: 4954.Google Scholar
Harding, J. E., Jones, C. T. and Robertson, J. S. 1985. Studies on experimental growth retardation in sheep. The effects of a small placenta in restricting transport to and growth of the fetus. Journal of Developmental Physiology 7: 427442.Google ScholarPubMed
Harding, J. E., Lui, L., Evans, P. C. and Gluckman, P. D. 1994. IGF-I alters feto-placental protein and carbohydrate metabolism in fetal sheep. Endocrinology 134:15091514.CrossRefGoogle ScholarPubMed
Harrington, W. N. and Godman, G. C. 1980. A selective inhibitor of cell proliferation from normal serum. Proceedings of the National Academy of Science, USA 77: 423427.Google Scholar
Hodgkinson, S. C., Bass, J. J. and Gluckman, P. D. 1991. Plasma IGF-I binding proteins in sheep: effect of recombinant growth hormone treatment and nutritional status. Domestic Animal Endocrinology 8: 343351.CrossRefGoogle ScholarPubMed
Hodgson, J. 1991. Checking sources: the serum supply secret. Bio/Technology 9:13201323.Google ScholarPubMed
Honn, K. V., Singley, J. A. and Chavin, W. 1975. Fetal bovine serum: a multivariate standard. Proceedings of the Society of Experimental Biology and Medicine 149: 344347.Google Scholar
Hua, K. M., Hodgkinson, S. C. and Bass, J. J. 1995. Differential regulation of plasma levels of insulin-like growth factors-I and -II by nutrition, age, and growth hormone treatment in sheep. Journal of Endocrinology 147: 507516.CrossRefGoogle ScholarPubMed
Kohler, N. and Lipton, A. 1974. Platelets as a source of fibroblast growth-promoting activity. Experimental Cell Research 87: 297301.Google Scholar
Life Technologies. 1993. Life Technologies 1993-1994 catalogue and reference guide, pp. 3.33.6. Life Technologies, Grand Island, NY.Google Scholar
Liu, J. P., Baker, J., Perkins, A. S., Robertson, E. J. and Efstratiadis, A. 1993. Mice carrying null mutations of the genes encoding insulin-like growth factor I (Igf-1) and type I IGF receptor (Igflr). Cell 75: 5972.Google Scholar
Lobby, G. E. 1992. Control of the metabolic fate of amino acids in ruminants: a review. Journal of Animal Science 70: 32643275.Google Scholar
McMillan, W. H. 1987. The timing of CIDR withdrawal and ram introduction on ewe fertility. Proceedings of the New Zealand Society of Animal Production 47:139141.Google Scholar
Maurer, H. R. 1986. Towards chemically-defined, serum-free media for mammalian cell culture. In Animal cell culture. A practical approach (ed. Freshney, R. I.), pp. 1331. IRL Press, Washington.Google Scholar
Mellor, D. J. and Murray, L. 1982. Effects on the rate of increase in fetal girth of refeeding ewes after short periods of severe undernutrition during late pregnancy. Research in Veterinary Science 32: 377382.Google Scholar
Oliver, M. H., Harding, J. E., Breier, B. H. and Gluckman, P. D. 1996. Fetal insulin-like growth factor (IGF)-I and IGFII are regulated differently by glucose or insulin in the sheep fetus. Reproduction, Tertility and Development 8: 167172.CrossRefGoogle ScholarPubMed
Oliver, M. H., Harrison, N. K., Bishop, J. E., Cole, P. J. and Laurent, G. J. 1989. A rapid and convenient assay for counting cells cultured in microwell plates: application for assessment of growth factors. Journal of Cell Science 92: 513518.CrossRefGoogle ScholarPubMed
Olmsted, C. A. 1967. A physico-chemical study of fetal calf sera used as tissue culture nutrient correlated with biological tests for toxicity. Experimental Cell Research 48: 283299.Google Scholar
Ross, R., Glomset, J., Kariya, B. and Harker, L. 1974. A platelet-derived serum factor that stimulates the proliferation of arterial smooth muscle cells in vitro. Proceedings of the National Academy of Science, USA 71: 12071210.Google Scholar
Ross, R. and Vogel, A. 1978. The platelet-derived growth factor. Cell 14: 203210.CrossRefGoogle ScholarPubMed
Salacinski, P. R., McLean, C., Sykes, J. E. C., Clement-Jones, V. V. and Lowry, P. J. 1981. Iodination of proteins, glycoproteins and peptides using a solid-phase oxidizing agent 1, 3, 4, 6-tetrachloro-3a, 6a-diphenyl glycoluril (Iodogen). Analytical Biochemistry 117:136146.Google Scholar
Straus, D. S., Ooi, G. T., Orlowski, C. L. and Rechler, M. W. 1991. Expression of the genes for insulin-like growth factor-I (IGF-I), IGF-II, and IGF-binding proteins-1 and -2 in fetal rat under conditions of intrauterine growth retardation caused by maternal fasting. Endocrinology 128: 518525.CrossRefGoogle ScholarPubMed
Towers, N. R. and Stratton, G. C. 1978. Serum gamma-glutamyltransferase as a measure of sporidesmin-induced liver damage in sheep. New Zealand Veterinary Journal 26: 109112.Google Scholar