This Article Full Text Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Fortmann, S. P. Articles by Marcovina, S. M. Search for Related Content PubMed PubMed Citation Articles by Fortmann, S. P. Articles by Marcovina, S. M.

(Circulation. 1997;95:295-296.)
© 1997 American Heart Association, Inc.

Articles

Lipoprotein(a), a Clinically Elusive Lipoprotein Particle

Stephen P. Fortmann, MD; Santica M. Marcovina, PhD, ScD

the Center for Research in Disease Prevention, Stanford (Calif) University Medical School and the University of Washington, Department of Medicine, Seattle (S.M.M.).

Correspondence to Santica M. Marcovina, PhD, Department of Medicine, University of Washington, 2121 N 35th St, Seattle, WA 98103.

	Introduction

 
The existence of lipoprotein(a) [Lp(a)] in human plasma was first reported by Berg¹ in 1963 as an antigen associated with LDL. Berg and Mohr² also found in family studies that the presence of Lp(a) was genetically determined by an autosomal mode of inheritance. Later studies provided evidence that Lp(a) is a specific class of lipoprotein particles with a lipid composition very similar to that of LDL. Lp(a) differs from LDL by the presence of a highly glycosylated protein of variable mass, termed apolipoprotein(a) [apo(a)], linked by a covalent bond to apolipoprotein (apo) B-100. The association between Lp(a) and coronary heart disease was first reported in the early 1970s,³ but what triggered a vast train of research on Lp(a) was the discovery in 1987 of the structural homology between apo(a) and plasminogen, a key protein of the coagulation cascade.⁴ Like plasminogen, apo(a) is composed of a kringle-containing domain and a serine protease domain. Apo(a) kringle domain is formed by one copy of plasminogen-like kringle 5 domain and multiple copies of the plasminogen-like kringle 4 (K4) domain. Ten basic K4 types,⁵ designated K4 type 1 through 10, are present in apo(a), all as a single copy, except K4 type 2, which is present in a variable number of copies ranging from 3 to >40.⁶ The varying number of K4 type 2 repeats is the major determinant of apo(a) size heterogeneity,⁷ giving origin to the large number of apo(a) isoforms detected in human plasma.⁸ In addition to apo(a) size heterogeneity, Lp(a) is heterogeneous . . . [Full Text of this Article]

This article has been cited by other articles:

				G. Weidner, C.-W. Kohlmann, M. Horsten, S. P. Wamala, K. Schenck-Gustafsson, M. Hogbom, and K. Orth-Gomer Cardiovascular Reactivity to Mental Stress in the Stockholm Female Coronary Risk Study Psychosom Med, November 1, 2001; 63(6): 917 - 924. [Abstract] [Full Text] [PDF]

				O. T. Raitakari, M. R. Adams, and D. S. Celermajer Effect of Lp(a) on the Early Functional and Structural Changes of Atherosclerosis Arterioscler Thromb Vasc Biol, April 1, 1999; 19(4): 990 - 995. [Abstract] [Full Text] [PDF]

				A. Wehinger, A. Kastrati, S. Elezi, H. Baum, S. Braun, F.-J. Neumann, and A. Schomig Lipoprotein(a) and coronary thrombosis and restenosis after stent placement J. Am. Coll. Cardiol., March 15, 1999; 33(4): 1005 - 1012. [Abstract] [Full Text] [PDF]

				F. Ribichini, G. Steffenino, A. Dellavalle, A. Vado, V. Ferrero, T. Camilla, S. Giubergia, and E. Uslenghi Plasma Lipoprotein(a) Is Not a Predictor for Restenosis After Elective High-Pressure Coronary Stenting Circulation, September 22, 1998; 98(12): 1172 - 1177. [Abstract] [Full Text] [PDF]

				P. W. F. Wilson and W. B. Kannel Should We Measure Lipoprotein Lp(a)? Arch Intern Med, June 9, 1997; 157(11): 1161 - 1162. [Abstract] [PDF]