Biomaterial Database

Quantitative alteration of some aortic intima proteins in fatty streaks and fibro-fatty lesions. 1992

J J Stastny, and E Fosslien

Department of Pathology, University of Illinois, College of Medicine, Chicago 60612.

Proteins from grossly and histologically normal human aortic intimas and human aortic intima with fatty streaks or fibro-fatty lesions were extracted with 9 M urea mixture. Protein extracts were mixed with an internal absorbance calibrator (carbonic anhydrase) and subsequently separated by two-dimensional gel electrophoresis, silver stained, and quantitated by a laser beam densitometer. The vascular-origin proteins actin, tropomyosin-like proteins, tubulin, glycoprotein G35, and two myosin light chains were present in the highest amounts in normal aortic intima (27-year-old male). Quantitation of vascular-origin proteins in aortic intima with a fibro-fatty lesion from the same subject showed a slight decrease in relative amount of these proteins as compared to the normal intima. Several polypeptides (P15, P18, P60, P110b) and plasma-derived proteins not observed in the normal intima were found in fibro-fatty lesion (albumin, haptoglobin beta-chain, fibrinogen beta-chain, alpha 1-HS-glycoprotein). Other proteins which were present in very low amounts in the normal intima (transferrin, alpha 1-antitrypsin, apolipoprotein A-1, P56, P190) were found to be major proteins of intima with fibro-fatty lesion. Differences in relative amount of plasma-derived and vascular-origin proteins between normal intima and intima with fatty streaks, studied in a large number of specimens from 38 thoracic intimas and 18 paired abdominal intimas (16-34 years old) were less prominent. Statistically significant increases of the albumin/actin ratio were found in fatty streaks as compared to paired normal intimas as well as in the mean value of albumin/actin ratio in the group of fibro-fatty lesions (mean = 6.1) as compared to the group of fatty streaks (mean = 1.7) or normal intima (mean = 0.7). Several lesion unique proteins were observed; however, the frequency of the occurrence of these proteins in 41 specimens with lesion was low. No significant differences were observed in intima protein pattern and quantities of selected intima proteins between paired thoracic and abdominal aortas.

UI	MeSH Term	Description	Entries
D008297	Male		Males
D009131	Muscle, Smooth, Vascular	The nonstriated involuntary muscle tissue of blood vessels.	Vascular Smooth Muscle,Muscle, Vascular Smooth,Muscles, Vascular Smooth,Smooth Muscle, Vascular,Smooth Muscles, Vascular,Vascular Smooth Muscles
D009218	Myosins	A diverse superfamily of proteins that function as translocating proteins. They share the common characteristics of being able to bind ACTINS and hydrolyze MgATP. Myosins generally consist of heavy chains which are involved in locomotion, and light chains which are involved in regulation. Within the structure of myosin heavy chain are three domains: the head, the neck and the tail. The head region of the heavy chain contains the actin binding domain and MgATPase domain which provides energy for locomotion. The neck region is involved in binding the light-chains. The tail region provides the anchoring point that maintains the position of the heavy chain. The superfamily of myosins is organized into structural classes based upon the type and arrangement of the subunits they contain.	Myosin ATPase,ATPase, Actin-Activated,ATPase, Actomyosin,ATPase, Myosin,Actin-Activated ATPase,Actomyosin ATPase,Actomyosin Adenosinetriphosphatase,Adenosine Triphosphatase, Myosin,Adenosinetriphosphatase, Actomyosin,Adenosinetriphosphatase, Myosin,Myosin,Myosin Adenosinetriphosphatase,ATPase, Actin Activated,Actin Activated ATPase,Myosin Adenosine Triphosphatase
D001798	Blood Proteins	Proteins that are present in blood serum, including SERUM ALBUMIN; BLOOD COAGULATION FACTORS; and many other types of proteins.	Blood Protein,Plasma Protein,Plasma Proteins,Serum Protein,Serum Proteins,Protein, Blood,Protein, Plasma,Protein, Serum,Proteins, Blood,Proteins, Plasma,Proteins, Serum
D002256	Carbonic Anhydrases	A family of zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide. They play an important role in the transport of CARBON DIOXIDE from the tissues to the LUNG. EC 4.2.1.1.	Carbonate Dehydratase,Carbonic Anhydrase,Anhydrases, Carbonic,Dehydratase, Carbonate
D003285	Contractile Proteins	Proteins which participate in contractile processes. They include MUSCLE PROTEINS as well as those found in other cells and tissues. In the latter, these proteins participate in localized contractile events in the cytoplasm, in motile activity, and in cell aggregation phenomena.	Contractile Protein,Protein, Contractile,Proteins, Contractile
D003720	Densitometry	The measurement of the density of a material by measuring the amount of light or radiation passing through (or absorbed by) the material.	Densitometries
D004591	Electrophoresis, Polyacrylamide Gel	Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.	Polyacrylamide Gel Electrophoresis,SDS-PAGE,Sodium Dodecyl Sulfate-PAGE,Gel Electrophoresis, Polyacrylamide,SDS PAGE,Sodium Dodecyl Sulfate PAGE,Sodium Dodecyl Sulfate-PAGEs
D005260	Female		Females
D005340	Fibrinogen	Plasma glycoprotein clotted by thrombin, composed of a dimer of three non-identical pairs of polypeptide chains (alpha, beta, gamma) held together by disulfide bonds. Fibrinogen clotting is a sol-gel change involving complex molecular arrangements: whereas fibrinogen is cleaved by thrombin to form polypeptides A and B, the proteolytic action of other enzymes yields different fibrinogen degradation products.	Coagulation Factor I,Factor I,Blood Coagulation Factor I,gamma-Fibrinogen,Factor I, Coagulation,gamma Fibrinogen