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J. Biol. Chem., Vol. 281, Issue 25, 20, June 23, 2006

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Ion Transport in the Sarcoplasmic Reticulum: the Work of David H. MacLennan

Purification and Properties of an Adenosine Triphosphatase from Sarcoplasmic Reticulum
(MacLennan, D. H. (1970) J. Biol. Chem. 245, 4508–4518)

David Herman MacLennan was born in Swan River, Manitoba, Canada in 1937. He attended the University of Manitoba, where he earned his B.S.A. in Plant Science in 1959, and Purdue University, where he received his M.S. in Plant Pathology in 1961 and his Ph.D. in Biology in 1963. After graduating, MacLennan went to the Institute for Enzyme Research at the University of Wisconsin, where he first studied as a postdoctoral fellow (1963–1964) and later became an assistant professor (1964–1968). He joined the Banting and Best Department of Medical Research at the University of Toronto in 1969, where he continues his research today. MacLennan served as Department Chairman from 1978 to 1990 and is currently the J. W. Billes Professor of Medical Research and University Professor.

At the University of Toronto, MacLennan started looking at mitochondrial electron transport components and the mitochondrial proton pump. This led him to study the sarcoplasmic reticulum calcium pump. The work, begun in 1969 and continuing today, allowed him to develop a theory on the mode of action of this ATP-dependent calcium pump. MacLennan's initial purification of the pump is the subject of the Journal of Biological Chemistry (JBC) Classic reprinted here.

At the time MacLennan started studying the sarcoplasmic reticulum calcium pump, it was known that a calcium-activated ATPase was part of the system that transported calcium into the sarcoplasmic reticulum. Ca²⁺ was transported when ATP was hydrolyzed. A similar system was known to occur in the mitochondria, and in this system the transport function was separable from the system that hydrolyzed ATP. However, no separation had been achieved in the sarcoplasmic reticulum transport system, suggesting that the ATPase enzyme and the ion transport enzyme were one and the same. In this JBC Classic, MacLennan reports on the purification of the ATPase from sarcoplasmic reticulum via fractionation. Based on several observations, including the fact that the enzyme has sites for both Mg²⁺ and Ca²⁺, the enzyme carries out partial reactions of Ca²⁺ transport, and the enzyme contains phospholipid and can form in membranes, MacLennan concluded that the ATPase is also the calcium transporter.

MacLennan's current research still focuses on ion transport. Specifically, he is studying how normal sarcoplasmic reticulum proteins carry out their functions of calcium transport, sequestration, and release and how mutant forms cause abnormalities or disease. In addition to his research on the sarcoplasmic reticulum, MacLennan has made important contributions to the fields of human and animal health. He and his coworkers defined the genetic basis for three important muscle diseases: malignant hyperthermia, central core disease, and Brody disease.

A Fellow of both the Royal Society of Canada (1985) and Royal Society of London (1994), MacLennan has received many awards including the Canadian Biochemical Society's Ayerst Award in 1974 and the Biophysical Society's National Lectureship Award in 1990, the Gairdner Foundation's International Award in 1991, the Canada Council Izaak Walton Killam Memorial Prize in Health Sciences in 1997, and the Glaxo-Wellcome Prize in 2000. He was an associate editor for the Canadian Journal of Biochemistry from 1972 to 1976 and a member of the JBC editorial board from 1975 to 1980 and 1982 to 1987. In 2001, he was appointed an Officer of the Order of Canada.

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This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Kresge, N. Articles by Hill, R. L. Search for Related Content PubMed Articles by Kresge, N. Articles by Hill, R. L. Related Collections Classic Articles MacLennan 245 (17): 4508 Social Bookmarking                      What's this?