Ruminal epithelial insulin-like growth factor-binding proteins 2, 3, and 6 are associated with epithelial cell proliferation.


Journal

Animal science journal = Nihon chikusan Gakkaiho
ISSN: 1740-0929
Titre abrégé: Anim Sci J
Pays: Australia
ID NLM: 100956805

Informations de publication

Date de publication:
Historique:
received: 09 03 2020
revised: 02 06 2020
accepted: 10 06 2020
entrez: 11 7 2020
pubmed: 11 7 2020
medline: 31 10 2020
Statut: ppublish

Résumé

The aim of this study was to identify factors that regulate ruminal epithelial insulin-like growth factor-binding protein (IGFBP) expression and determine its role in rumen epithelial cell proliferation. Primary bovine rumen epithelial cells (BREC) were incubated with short-chain fatty acids (SCFAs) at pH 7.4 or 5.6, lactate, lipopolysaccharide (LPS), insulin-like growth factor-I (IGF-I), -II (IGF-II), or recombinant bovine IGFBP2 (rbIGFBP2). The mRNA expression levels of IGFBP in BREC were analyzed using quantitative real-time polymerase chain reaction (qRT-PCR). The proliferation rate of BREC was analyzed using a WST-1 assay. IGFBP2 gene expression tended to be lower with SCFA treatment (p < .1), and IGFBP6 gene expression was significantly lower with SCFA treatment (p < .05). IGFBP3 and IGFBP6 gene expression tended to be higher with d-Lactate treatment (p < .1). IGFBP3 gene expression was significantly higher (p < .05) with LPS treatment. BREC treated with IGF-I grew more rapidly than vehicle control-treated cells (p < .01); however, recombinant bovine rbIGFBP2 inhibited IGF-I-induced proliferation. IGF-II and/or rbIGFBP2 did not affect BREC proliferation. Taken together, SCFA treatment decreased IGFBP2 and IGFBP6 expression in rumen epithelial cells, and lower expression of these IGFBP might promote rumen epithelial cell proliferation by facilitating IGF-I.

Identifiants

pubmed: 32648312
doi: 10.1111/asj.13422
doi:

Substances chimiques

Fatty Acids, Volatile 0
Insulin-Like Growth Factor Binding Protein 2 0
Insulin-Like Growth Factor Binding Protein 3 0
Insulin-Like Growth Factor Binding Protein 6 0
RNA, Messenger 0
Insulin-Like Growth Factor I 67763-96-6

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

e13422

Subventions

Organisme : Japan Society for the Promotion of Science
ID : 18H02325
Pays : International
Organisme : Japan Society for the Promotion of Science
ID : 19J12823
Pays : International
Organisme : Rural Development Administration
Pays : International

Informations de copyright

© 2020 Japanese Society of Animal Science.

Références

Austin, K., Imam, N. A., Pintar, J. E., & Brubaker, P. L. (2015). IGF binding protein-4 is required for the growth effects of glucagon-like peptide-2 in murine intestine. Endocrinology, 156, 429-436. https://doi.org/10.1210/en.2014-1829
Bach, L. A., Salemi, R., & Leeding, K. S. (1995). Roles of insulin-like growth factor (IGF) receptors and IGF-binding proteins in IGF-II-induced proliferation and differentiation of L6A1 rat myoblasts. Endocrinology, 136, 5061-5069. https://doi.org/10.1210/endo.136.11.7588242
Chanrot, M., Guo, Y., Dalin, A. M., Persson, E., Bage, R., Svensson, A., … Humblot, P. (2017). Dose related effects of LPS on endometrial epithelial cell populations from dioestrus cows. Animal Reproduction Science, 177, 12-24. https://doi.org/10.1016/j.anireprosci.2016.12.002
Cheng, G. S., Zhang, Y. S., Zhang, T. T., He, L., & Wang, X. Y. (2017). Bone marrow-derived mesenchymal stem cells modified with IGFBP-3 inhibit the proliferation of pulmonary artery smooth muscle cells. International Journal of Molecular Medicine, 39, 223-230. https://doi.org/10.3892/ijmm.2016.2820
Clemmons, D. R. (1998). Role of insulin-like growth factor binding proteins in controlling IGF actions. Molecular and Cellular Endocrinology, 140, 19-24.
Corkins, M. R., Vanderhoof, J. A., Slentz, D. H., MacDonald, R. G., & Park, J. H. (1995). Growth stimulation by transfection of intestinal epithelial cells with an antisense insulin-like growth factor binding protein-2 construct. Biochemical and Biophysical Research Communications, 211, 707-713. https://doi.org/10.1006/bbrc.1995.1870
Dunlop, R. H. (1965). Lactic acids: Chemistry and metabolism. Science, 147, 315-321. https://doi.org/10.1126/science.147.3655.315
Firth, S. M., & Baxter, R. C. (2002). Cellular actions of the insulin-like growth factor binding proteins. Endocrine Reviews, 23, 824-854. https://doi.org/10.1210/er.2001-0033
Gozho, G. N., Krause, D. O., & Plaizier, J. C. (2007). Ruminal lipopolysaccharide concentration and inflammatory response during grain-induced subacute ruminal acidosis in dairy cows. Journal of Dairy Science, 90, 856-866. https://doi.org/10.3168/jds.S0022-0302(07)71569-2
Gozho, G. N., Plaizier, J. C., Krause, D. O., Kennedy, A. D., & Wittenberg, K. M. (2005). Subacute ruminal acidosis induces ruminal lipopolysaccharide endotoxin release and triggers an inflammatory response. Journal of Dairy Science, 88, 1399-1403.
Hoflich, A., Lahm, H., Blum, W., Kolb, H., & Wolf, E. (1998). Insulin-like growth factor-binding protein-2 inhibits proliferation of human embryonic kidney fibroblasts and of IGF-responsive colon carcinoma cell lines. FEBS Letters, 434, 329-334. https://doi.org/10.1016/S0014-5793(98)01011-4
Ichikawa, H., & Sakata, T. (1997). Effect of L-lactic acid, short-chain fatty acids, and pH in cecal infusate on morphometric and cell kinetic parameters of rat cecum. Digestive Diseases and Sciences, 42, 1598-1610. https://doi.org/10.1023/a:1018884625737
Kim, S. C., & Hwang, P. H. (2018). Upregulation of IGF binding protein-3 inhibits colonic inflammatory response. Journal of Korean Medical Science, 33, e110. https://doi.org/10.3346/jkms.2018.33.e110
Kumar, K. N., Shah, V. R., Parikh, B. K., & Sonde, S. (2015). Reversal of severe lactic acidosis with thiamine in a renal allograft recipient. Indian Journal of Critical Care Medicine, 19, 425-428.
Lampe, K. J., Namba, R. M., Silverman, T. R., Bjugstad, K. B., & Mahoney, M. J. (2009). Impact of lactic acid on cell proliferation and free radical-induced cell death in monolayer cultures of neural precursor cells. Biotechnology and Bioengineering, 103, 1214-1223. https://doi.org/10.1002/bit.22352
Liu, L., Sun, D., Mao, S., Zhu, W., & Liu, J. (2019). Infusion of sodium butyrate promotes rumen papillae growth and enhances expression of genes related to rumen epithelial VFA uptake and metabolism in neonatal twin lambs. Journal of Animal Science, 97, 909-921. https://doi.org/10.1093/jas/sky459
Nagaraja, T. G., Bartley, E. E., Fina, L. R., & Anthony, H. D. (1978). Relationship of rumen gram-negative bacteria and free endotoxin to lactic acidosis in cattle. Journal of Animal Science, 47, 1329-1337.
Nagaraja, T. G., & Titgemeyer, E. C. (2007). Ruminal acidosis in beef cattle: The current microbiological and nutritional outlook. Journal of Dairy Science, 90(Suppl 1), E17-E38. https://doi.org/10.3168/jds.2006-478
Nishihara, K., Kato, D., Suzuki, Y., Kim, D., Nakano, M., Yajima, Y. U., … Roh, S.-G. (2018). Comparative transcriptome analysis of rumen papillae in suckling and weaned Japanese Black calves using RNA sequencing. Journal of Animal Science, 96, 2226-2237. https://doi.org/10.1093/jas/skx016
Nishihara, K., Suzuki, Y., Kim, D., & Roh, S. (2019). Growth of rumen papillae in weaned calves is associated with lower expression of insulin-like growth factor-binding proteins 2, 3, and 6. Animal Science Journal, 90, 1287-1292. https://doi.org/10.1111/asj.13270
Roh, S. G., Kuno, M., Hishikawa, D., Hong, Y. H., Katoh, K., Obara, Y., … Sasaki, S. (2007). Identification of differentially expressed transcripts in bovine rumen and abomasum using a differential display method. Journal of Animal Science, 85, 395-403. https://doi.org/10.2527/jas.2006-234
Roh, S. G., Suzuki, Y., Gotoh, T., Tatsumi, R., & Katoh, K. (2016). Physiological roles of adipokines, hepatokines, and myokines in ruuminants. Asian-Australasian Journal of Animal Sciences, 29, 1-15. https://doi.org/10.5713/ajas.16.0001R
Sakata, T., & Tamate, H. (1978). Rumen epithelial cell proliferation accelerated by rapid increase in intraruminal butyrate. Journal of Dairy Science, 61, 1109-1113. https://doi.org/10.3168/jds.S0022-0302(78)83694-7
Steele, M. A., Croom, J., Kahler, M., AlZahal, O., Hook, S. E., Plaizier, K., & McBride, B. W. (2011). Bovine rumen epithelium undergoes rapid structural adaptations during grain-induced subacute ruminal acidosis. American Journal of Physiology-Regulatory, Integrative and Comparative Physiology, 300, R1515-R1523. https://doi.org/10.1152/ajpregu.00120.2010
Tamate, H., McGilliard, A. D., Jacobson, N. L., & Getty, R. (1962). Effect of various dietaries on the anatomical development of the stomach in the calf. Journal of Dairy Science, 45, 408-420. https://doi.org/10.3168/jds.S0022-0302(62)89406-5
Vandesompele, J., De Preter, K., Pattyn, F., Poppe, B., Van Roy, N., De Paepe, A., & Speleman, F. (2002). Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes. Genome Biology, 3, RESEARCH0034. https://doi.org/10.1186/gb-2002-3-7-research0034
Vielfort, K., Weyler, L., Soderholm, N., Engelbrecht, M., Lofmark, S., & Aro, H. (2013). Lactobacillus decelerates cervical epithelial cell cycle progression. PLoS One, 8, e63592. https://doi.org/10.1371/journal.pone.0063592

Auteurs

Koki Nishihara (K)

Laboratory of Animal Physiology, Graduate School of Agricultural Science, Tohoku University, Sendai, Miyagi, Japan.

Yutaka Suzuki (Y)

Research Faculty of Agriculture, Hokkaido University, Sapporo, Hokkaido, Japan.

Sanggun Roh (S)

Laboratory of Animal Physiology, Graduate School of Agricultural Science, Tohoku University, Sendai, Miyagi, Japan.

Articles similaires

Robotic Surgical Procedures Animals Humans Telemedicine Models, Animal

Odour generalisation and detection dog training.

Lyn Caldicott, Thomas W Pike, Helen E Zulch et al.
1.00
Animals Odorants Dogs Generalization, Psychological Smell
Animals TOR Serine-Threonine Kinases Colorectal Neoplasms Colitis Mice
Animals Tail Swine Behavior, Animal Animal Husbandry

Classifications MeSH