Distinctive protein profiles obtained from extracts of normal and atherosclerotic human aorta

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      Specific areas of fourteen autopsied abdominal aortas were layer-dissected, histologically graded and solubilized with SDS, dilute saline or SDS-urea and β-mercaptoethanol. Comparisons were made between intima, media, lesions of progressive severity and an in-vivo thrombus. Apparent molecular weights were calculated from the Coomassie blue stained gels of these extracts and each band's contribution estimated by integrative densitometry. Four minor high molecular weight bands and six medium to low molecular weight bands were detected in the arterial extracts. Band intensity stain patterns of normal intima are easily distinguished from normal media. Extracts of minor lesions resemble normal media; higher grade lesions demonstrate increased amounts of characteristic intimal bands. The major medial band is also seen on gels of thrombus extracts. Both of the bands most characteristic of atherosclerotic lesions stain for carbohydrate. Isolation and characterization of these (glyco)proteins will provide material for binding studies. Quantitation of characteristic lesion proteins may provide insights into the proliferative phase of this disease.


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        • Spencer A.
        • Stahlman M.A.
        Variation in proteins of single lesions from the intima of the aorta from a human patient with severe atherosclerosis.
        Atherosclerosis. 1977; 26: 139
        • Reynolds J.A.
        • Tanford C.
        The gross conformation of sodium dodecyl sulphate complexes.
        J. Biol. Chem. 1970; 245: 5161
        • Lowry O.H.
        • Rosenbrough N.J.
        • Farr A.L.
        • Randall R.J.
        Protein measurement with the Folln phenol reagent.
        J. Biol. Chem. 1951; 193: 265
        • Weber K.
        • Osborn M.
        The reliability of molecular weight determinations by dodecyl sulphatepolyacrylamide gel electrophoresis.
        J. Biol. Chem. 1969; 244: 4406
        • Holbrook I.B.
        • Leaver A.G.
        A procedure to increase the sensitivity of staining by Coomassie brilliant blue G-250-perchloric acid solution.
        Anal. Biochem. 1976; 75: 634
        • Zacharius R.M.
        • Zell T.E.
        Glycoprotein staining following electrophoresis in acrylamide gels.
        Anal. Biochem. 1969; 30: 148
        • Yamada K.M.
        • Weston J.A.
        Isolation of a major cell surface glycoprotein from fibroblasts.
        in: Proc. Nat. Acad. Sci.71. 1974: 3492
      1. Gilbert, D.B. and Tsai, C., Unpublished data.

        • Hollander W.
        • Colombo M.A.
        • Kramsch D.M.
        • Kirkpatrick B.
        Immunological aspects of atherosclerosis.
        Adv. Cardiol. 1974; 13: 192
        • Muir L.W.
        • Bornstein P.
        • Ross R.
        A presumptive subunit of elastic fiber microfibrils secreted by arterial smooth-muscle cells in culture.
        Europ. J. Biochem. 1976; 64: 105
        • Ferguson E.W.
        • Fretto L.J.
        • McKee P.A.
        A re-examination of the cleavage of fibrinogen and fibrin by plasmin.
        J. Biol. Chem. 1975; 250: 7210
        • Kao V.C.Y.
        • Wissler R.W.
        A study of the immunohistochemical localization of serum lipoproteins and other plasma proteins in human atherosclerosic lesions.
        Exp. Mol. Path. 1965; 4: 465
        • Dayhoff M.O.
        Atlas of Protein Sequence and Structure. 1976; 5: 254
        • Dayhoff M.O.
        Atlas of Protein Sequence and Structure. 5. National Biomedical Research Foundation, Silver Spring, MD1976: S-78
        • Keski-Oja J.
        • Vaheri A.
        • Ruoslahti E.
        Fibroblast surface antigen (SF): the external glycoprotein lost in proteolytic stimulation and malignant transformation.
        Int. J. Cancer. 1976; 17: 261
        • Jaffee E.A.
        • Hoyer L.W.
        • Nachman R.L.
        Synthesis of antihemophilic factor antigen by cultured human endothelial cells.
        J. Clin. Invest. 1973; 52: 2757
        • Gafney P.J.
        • Bradsher M.
        • Lord K.
        • Strachan C.J.L.
        • Wilkinson A.R.
        • Kakkar V.V.
        • Scully M.F.
        Fibrin subunits in venous and arterial thrombo-embolism.
        Cardiovasc. Res. 1976; 10: 421
        • Kramsch D.M.
        • Hollander W.
        The interaction of serum and arterial lipoproteins with elastin of the arterial intima and its role in lipid accumulation in atherosclerosic plaques.
        J. Clin. Invest. 1973; 52: 236
        • Srinivasan S.R.
        • Dolan P.
        • Radhakrishnamurty B.
        • Berenson G.S.
        Isolation of lipoprotein-acid mucopolysaccharide complexes from fatty streaks of human aortas.
        Atherosclerosis. 1972; 16: 95
        • Iverius P.-H.
        The interaction between human plasma lipoproteins and connective tissue glycosaminoglycans.
        J. Biol. Chem. 1972; 247: 2607
        • Camejo G.
        • Lopez A.
        • Vegas H.
        • Paoli H.
        The participation of aortic proteins in the formation of complexes between low density lipoproteins and intima-media extracts.
        Atherosclerosis. 1975; 21: 77
        • Pizzo S.V.
        • Taylor L.M.
        • Schwartz M.L.
        • Hill R.L.
        • McKee P.A.
        Subunit structure of fragment D from fibrinogen and cross-linked fibrin.
        J. Biol. Chem. 1973; 248: 4584