Maternal omega-3 polyunsaturated fatty acids supplementation in pregnancy decreases MMP-1 levels in breastmilk: a cross-sectional study

References

• Kverka M, Burianova J, Lodinova-Zadnikova R, et al. Cytokine profiling in human colostrum and milk by protein array. Clin Chem. 2007;53(5):955–962.
   PubMed Web of Science ®Google Scholar
• Carlson SJ, Fallon EM, Kalish BT, et al. The role of the ω-3 fatty acid DHA in the human life cycle. J Parenter Enteral Nutr. 2013;37(1):15–22.
   PubMed Web of Science ®Google Scholar
• Manson WG, Weaver LT. Fat digestion in the neonate. Arch Dis Child. 1997;76(3):F206–F211.
   Web of Science ®Google Scholar
• Giovanni M, Riva E, Agostoni C. Fatty acids in pediatric nutrition. Pediatr Clin North Am. 1995;42(4):861–877.
   PubMed Web of Science ®Google Scholar
• Small DM. The effects of glyceride structure on absorption and metabolism. Annu Rev Nutr. 1991;11:413–434.
   PubMed Web of Science ®Google Scholar
• Xie Y, Mustafa A, Yerzhan A, et al. Nuclear matrix metalloproteinases: functions resemble the evolution from the intercellular to the extracellular compartment. Cell Death Discov. 2017;3:17036.
   PubMed Web of Science ®Google Scholar
• Otto-Buczkowska E, Chobot A. Role of ghrelin and leptin in the regulation of carbohydrate metabolism. Part II. Leptin. Postepy Hig Med Dosw (Online). 2012;66:799–803.
   PubMedGoogle Scholar
• Gorden P, Gavrilova O. The clinical uses of leptin. Curr Opin Pharmacol. 2003;3(6):655–659.
   PubMed Web of Science ®Google Scholar
• Yis U, Ozturk Y, Sisman AR, et al. The relation of serum ghrelin, leptin and insülin levels to the growth patterns and feding caharacteritics in breast-fed versus formula-fed infants. Turk J Pediatr. 2010;52:35–41.
   PubMed Web of Science ®Google Scholar
• Martos-Moreno GA, Barrios V, Saenz de Pipaon M, et al. Influence of prematurity and growth restriction on the adipokine profile, IGF1, and ghrelin levels in cord blood: relationship with glucose metabolism. Eur J Endocrinol. 2009;161(3):381–389.
   PubMed Web of Science ®Google Scholar
• Moon HS, Lee HG, Seo JH, et al. Leptin-induced matrix metalloproteinase-2 secretion is suppressed by trans-10,cis-12 conjugated linoleic acid. Biochem Biophys Res Commun. 2007;356(4):955–956.
   PubMed Web of Science ®Google Scholar
• Schram K, Wong MM, Palanivel R, et al. Increased expression and cell surface localization of MT1-MMP plays a role in stimulation of MMP-2 activity by leptin in neonatal rat cardiac myofibroblasts. J Mol Cell Cardiol. 2008;44(5):874–881.
   PubMed Web of Science ®Google Scholar
• Liu R, Chen B, Chen J, et al. Leptin upregulates smooth muscle cell expression of MMP-9 to promote plaque destabilization by activating AP-1 via the leptin receptor/MAPK/ERK signaling pathways. Exp Ther Med. 2018;16(6):5327–5333.
   PubMed Web of Science ®Google Scholar
• Liberale L, Bonaventura A, Carbone F, et al. Early reduction of matrix metalloproteinase-8 serum levels is associated with leptin drop and predicts diabetes remission after bariatric surgery. Int J Cardiol. 2017;245:257–262.
   PubMed Web of Science ®Google Scholar
• Lafrance V, Inoue W, Kan B, et al. Leptin modulates cell morphology and cytokine release in microglia. Brain Behav Immun. 2010;24:350–365.
   PubMed Web of Science ®Google Scholar
• Hui W, Litherland GJI, Elias MS, et al. Leptin produced by joint White adipose tissue induces cartilage degradation via upregulation and activation of matrix metalloproteinases. Ann Rheum Dis. 2012;71(3):455–462.
   PubMed Web of Science ®Google Scholar
• Berenhauser AC, Pinheiro do Prado AC, Da Silva RC, Gioielli LA, et al. Fatty acid composition in preterm and term breast milk. Int J Food Sci Nutr. 2012; 63(3):318–325.
   PubMed Web of Science ®Google Scholar
• Holton TA, Vijayakumar V, Dallas DC, et al. Following the digestion of milk proteins from mother to baby. J Proteome Res. 2014;13(12):5777–5783.
   PubMed Web of Science ®Google Scholar
• Dallas DC, Underwood MA, Zivkovic AM, et al. Digestion of protein in premature and term infants. J Nutr Disord Ther. 2012;2(3):112–121.
   PubMedGoogle Scholar
• Lubetzky R, Mandel D, Mimouni FB, et al. MMP-2 and MMP-9 and their tissue inhibitor in preterm human milk. J Pediatr Gastroenterol Nutr. 2010;51(2):210–212.
   PubMed Web of Science ®Google Scholar
• Curtis CL, Rees SG, Cramp J, et al. Effects of n-3 fatty acids on cartilage metabolism. Proc Nutr Soc. 2002;61(3):381–389.
   PubMed Web of Science ®Google Scholar
• Harris MA, Hansen RA, Vidsudhiphan P, et al. Effects of conjugated linoleic acids and docosahexaenoic acid on rat liver and reproductive tissue fatty acids, prostaglandins and matrix mettalloproteinase production. Prostaglandins Leucotrienes Essential Fatty Acids. 2001;65(1):23–29.
   PubMed Web of Science ®Google Scholar
• McCabe AJ, Wallace J, Gilmore WS, et al. The effect of eicosapentaenoic acid on matrixmetalloproteinase gene expression. Lipids. 1999;34(S1):S217–S218.
   PubMed Web of Science ®Google Scholar
• Kim HH, Shin CM, Park CH, et al. J. Eicosapentaenoic acid inhibits UV-induced MMP-1 expression in human dermal fibroblasts. J Lipid Res. 2005;46(8):1712–1720.
   PubMed Web of Science ®Google Scholar
• Wang P, Zhu F, Konstantopulos K. Prostaglandin E2 induces interleukin-6 expression in human chondrocytes via cAMP/protein kinase A- and phosphatidylinositol 3-kinase-dependent NF-kappaB activation. Am J Physiol Cell Physiol. 2010;298(6):C1445–C1456.
   Google Scholar
• Liu XH, Kirschenbaum A, Yao S, et al. The role of the interleukin-6/gp130 signaling pathway in bone metabolism. Vitam Horm. 2006;74:341–355.
   PubMed Web of Science ®Google Scholar
• Iacobellis G, Lonn E, Lamy A, et al. Epicardial fat thickness and coronary artery disease correlate independently of obesity. Int J Cardiol. 2011;146(3):452–454.
   PubMed Web of Science ®Google Scholar
• Miksztowicz V, Morales C, Barchuk M, et al. Metalloproteinase 2 and 9 activity increase in epicardial adipose tissue of patients with coronary artery disease. Curr Vasc Pharmacol. 2017;15(2):135–143.
   PubMed Web of Science ®Google Scholar
• Mazor R, Friedmann-Morvinski D., Alsaigh T, Kleifeld O, et al. Cleavage of the leptin receptor by matrix metalloproteinase-2 promotes leptin resistance and obesity in mice. Sci Transl Med. 2018;10(455):eaah6324.
   PubMed Web of Science ®Google Scholar
• Dallas DC, Murray NM, Gan J. Proteolytic systems in milk: perspectives on the evolutionary function within the mammary gland and the infant. J Mammary Gland Biol Neoplasia. 2015;20(3-4):133–147.
   PubMed Web of Science ®Google Scholar
• Manicone AM, Mc Guire JK. Matrix metalloproteinases as modulators of inflammation. Semin Cell Dev Biol. 2008;19(1):34–41.
   PubMed Web of Science ®Google Scholar
• Ra HJ, Parks WC. Control of matrix metalloproteinase catalytic activity. Matrix Biol. 2007;26(8):587–596.
   PubMed Web of Science ®Google Scholar
• Newby AC, George SJ, Ismail Y, et al. Do metalloproteinases destabilize vulnerable atherosclertotic plaque?. Curr Opin Lipidol. 2006;17:556–561.
   PubMed Web of Science ®Google Scholar
• Trujillo ME, Sullivan S, Harten I, Schneider SH, et al. Interleukin-6 regulates human adipose tissue lipid metabolism and leptin production in vitro. J Clin Endocrinol Metab. 2004;89(11):5577–5582.
   PubMed Web of Science ®Google Scholar
• Park HS, Park JY, Yu R. Relationship of obesity and visceral adiposity with serum concentrations of CRP, TNF-alpha and IL-6. Diabetes Res Clin Pract. 2005;69(1):29–35.
   PubMed Web of Science ®Google Scholar
• Wang W, Song X, Chen Y, et al. The long-term influence of tissue inhibitor of matrix metalloproteinase-1 in patients with mild to moderate coronary artery lesions in a Chinese population: a 7-year follow-up study. Cardiology. 2015;132(3):151–158.
   PubMed Web of Science ®Google Scholar
• Ries C. Cytokine functions of TIMP-1. Cell Mol Life Sci. 2014;71(4):659–672.
   PubMed Web of Science ®Google Scholar