Advertisement

Metabolic response of Acylation Stimulating Protein to an oral fat load.

Open AccessPublished:November 01, 1989DOI:https://doi.org/10.1016/S0022-2275(20)38229-8
      This paper is only available as a PDF. To read, Please Download here.
      Acylation Stimulating Protein (ASP) is a small (mol wt 14,000), basic (pI 9.0) protein present in human plasma. When examined in vitro with normal human cultured skin fibroblasts and adipocytes, ASP appears to be the most potent stimulant of triglyceride synthesis yet described. In this study, a competitive ELISA assay for ASP has been developed using immunospecific polyclonal antibodies, and ASP levels have been measured in seven normal subjects. Following an oral fat load, a sustained significant increase in ASP occurs, whereas after an oral glucose load, ASP levels do not change significantly. These responses are entirely opposite to those of insulin, which rises sharply but transiently after an oral glucose load but is unchanged after an oral fat load. Both the fasting and peak ASP levels were significantly related to the postprandial lipemia. These data provide the first in vivo evidence that Acylation Stimulating Protein may play an important physiological role in the normal response to an oral fat load.

      REFERENCES

        • Patsch J.R.
        • Prasad S.
        • Gotto A.
        • Patsch W.
        High density lipoprotein2: relationship of the plasma levels of this lipoprotein species to its composition, to the magnitude of postprandial lipemia, and to the activities of lipoprotein lipase and hepatic lipase.
        J. Clin. Invest. 1987; 80: 341-347
        • Cianflone K.
        • Walsh M.J.
        • Vu H.
        • Gagnon J.
        • Sniderman A.D.
        • Rodriguez M.A.
        Purification and characterization of ASP.
        J. Biol. Chem. 1989; 265: 426-430
        • Genest J.
        • Sniderman A.D.
        • Cianflone K.
        • Teng B.
        • Wacholder S.
        • Marcel Y.
        • Kwiterovich Jr., P.O.
        Hyperapobetalipoproteinemia: Plasma lipoprotein responses to an oral fat load.
        Arteriosclervsis. 1985; 6: 297-304
        • Lipid Research Clinics Program
        Manual of Laboratory Operations, Vol. I. DHEW publication no. (NIH) 75-6282. National Heart and Lung Institute, Bethesda, MD1975
        • Friedewald W.T.
        • Levy R.I.
        • Fredrickson D.S.
        Estimation of the concentration of low-density lipoprotein cholesterol in plasma without use of the preparation ultracentrifuge.
        Clin. Chem. 1972; 18: 499-502
        • Bradford M.
        A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.
        Anal. Biochem. 1976; 72: 248-254
        • Laemmli U.
        Cleavage of structural proteins during the assembly of the head of bacteriophage T4.
        Nature. 1970; 227: 680-685
        • Reisfeld R.A.
        • Lewis U.J.
        • Williams D.E.
        Disk electrophoresis of basic proteins and peptides on polyacrylamide gels.
        Nature. 1962; 195: 281-283
        • Goding J.N.
        Monoclonal Antibodies: Principles of Practice. Academic Press, Orlando, FL1986: 195-200
        • Markwell M.
        • Haas S.
        • Tollen N.
        • Bieker L.
        Protein determination in membrane and lipoprotein samples: manual and automated procedures.
        Methods Enzymol. 1981; 72: 296-298
        • Cianflone K.
        • Rodriguez M.A.
        • Walsh M.
        • Vu H.
        • Sniderman A.D.
        The effect of a plasma protein fraction on lipid synthesis in cultured skin fibroblasts from normals and patients with hyperapobetalipoproteinemia.
        Clin Invest. Med. 1988; 11: 99-107
        • Cianflone K.
        • Rodriguez M.
        • Walsh M.
        • Vu H.
        • Sniderman A.D.
        Abnormal Acylation Stimulating Proteincell interaction: a potential marker for hyperapobetalipoproteinemia.
        Circulation. 1988; 78: II-159