Adipocyte differentiation-related protein promotes lipid accumulation in goat mammary epithelial cells

H. B. Shi, K. Yu, J. Luo, J. Li, H. B. Tian, J. J. Zhu, Y. T. Sun, D. W. Yao, H. F. Xu, H. P. Shi, J. J. Loor

Research output: Contribution to journalArticle

Abstract

Milk fat originates from the secretion of cytosolic lipid droplets (CLD) synthesized within mammary epithelial cells. Adipocyte differentiation-related protein (ADRP; gene symbol PLIN2) is a CLD-binding protein that is crucial for synthesis of mature CLD. Our hypothesis was that ADRP regulates CLD production and metabolism in goat mammary epithelial cells (GMEC) and thus plays a role in determining milk fat content. To understand the role of ADRP in ruminant milk fat metabolism, ADRP ( PLIN2) was overexpressed or knocked down in GMEC using an adenovirus system. Immunocytochemical staining revealed that ADRP localized to the surface of CLD. Supplementation with oleic acid (OA) enhanced its colocalization with CLD surface and enhanced lipid accumulation. Overexpression of ADRP increased lipid accumulation and the concentration of triacylglycerol in GMEC. In contrast, morphological examination revealed that knockdown of ADRP decreased lipid accumulation even when OA was supplemented. This response was confirmed by the reduction in mass of cellular TG when ADRP was knocked down. The fact that knockdown of ADRP did not completely eliminate lipid accumulation at a morphological level in GMEC without OA suggests that some other compensatory factors may also aid in the process of CLD formation. The ADRP reversed the decrease of CLD accumulation induced by adipose triglyceride lipase. This is highly suggestive of ADRP promoting triacylglycerol stability within CLD by preventing access to adipose triglyceride lipase. Collectively, these data provide direct in vitro evidence that ADRP plays a key role in CLD formation and stability in GMEC.

Original languageEnglish (US)
Article number73830
Pages (from-to)6954-6964
Number of pages11
JournalJournal of Dairy Science
Volume98
Issue number10
DOIs
StatePublished - Oct 1 2015

Fingerprint

adipocytes
Adipocytes
Goats
breasts
Breast
epithelial cells
Epithelial Cells
goats
Lipids
droplets
lipids
Proteins
proteins
Oleic Acid
Milk
Fats
Lipase
milk fat
oleic acid
Triglycerides

Keywords

  • Hydrolysis
  • Lipid droplet
  • Milk fat
  • Triacylglycerol

ASJC Scopus subject areas

  • Food Science
  • Animal Science and Zoology
  • Genetics

Cite this

Adipocyte differentiation-related protein promotes lipid accumulation in goat mammary epithelial cells. / Shi, H. B.; Yu, K.; Luo, J.; Li, J.; Tian, H. B.; Zhu, J. J.; Sun, Y. T.; Yao, D. W.; Xu, H. F.; Shi, H. P.; Loor, J. J.

In: Journal of Dairy Science, Vol. 98, No. 10, 73830, 01.10.2015, p. 6954-6964.

Research output: Contribution to journalArticle

Shi, HB, Yu, K, Luo, J, Li, J, Tian, HB, Zhu, JJ, Sun, YT, Yao, DW, Xu, HF, Shi, HP & Loor, JJ 2015, 'Adipocyte differentiation-related protein promotes lipid accumulation in goat mammary epithelial cells', Journal of Dairy Science, vol. 98, no. 10, 73830, pp. 6954-6964. https://doi.org/10.3168/jds.2015-9452
Shi, H. B. ; Yu, K. ; Luo, J. ; Li, J. ; Tian, H. B. ; Zhu, J. J. ; Sun, Y. T. ; Yao, D. W. ; Xu, H. F. ; Shi, H. P. ; Loor, J. J. / Adipocyte differentiation-related protein promotes lipid accumulation in goat mammary epithelial cells. In: Journal of Dairy Science. 2015 ; Vol. 98, No. 10. pp. 6954-6964.
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AU - Li, J.

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AU - Zhu, J. J.

AU - Sun, Y. T.

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AU - Xu, H. F.

AU - Shi, H. P.

AU - Loor, J. J.

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AB - Milk fat originates from the secretion of cytosolic lipid droplets (CLD) synthesized within mammary epithelial cells. Adipocyte differentiation-related protein (ADRP; gene symbol PLIN2) is a CLD-binding protein that is crucial for synthesis of mature CLD. Our hypothesis was that ADRP regulates CLD production and metabolism in goat mammary epithelial cells (GMEC) and thus plays a role in determining milk fat content. To understand the role of ADRP in ruminant milk fat metabolism, ADRP ( PLIN2) was overexpressed or knocked down in GMEC using an adenovirus system. Immunocytochemical staining revealed that ADRP localized to the surface of CLD. Supplementation with oleic acid (OA) enhanced its colocalization with CLD surface and enhanced lipid accumulation. Overexpression of ADRP increased lipid accumulation and the concentration of triacylglycerol in GMEC. In contrast, morphological examination revealed that knockdown of ADRP decreased lipid accumulation even when OA was supplemented. This response was confirmed by the reduction in mass of cellular TG when ADRP was knocked down. The fact that knockdown of ADRP did not completely eliminate lipid accumulation at a morphological level in GMEC without OA suggests that some other compensatory factors may also aid in the process of CLD formation. The ADRP reversed the decrease of CLD accumulation induced by adipose triglyceride lipase. This is highly suggestive of ADRP promoting triacylglycerol stability within CLD by preventing access to adipose triglyceride lipase. Collectively, these data provide direct in vitro evidence that ADRP plays a key role in CLD formation and stability in GMEC.

KW - Hydrolysis

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