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Evidence of Dipeptidyl Peptidase I Deficiency

William T. Stauber, PhD; Jack E. Riggs, MD; Sidney S. Schochet, Jr, MD; Ludwig Gutmann, MD; Thomas W. Crosby, MD

Arch Neurol. 1986;43(1):39-41.

Abstract
• Fluorescent protease histochemical analysis of muscle biopsy specimens from two patients with nemaline myopathy revealed the apparent absence of one proteolytic enzyme, dipeptidyl peptidase I. Although the function of peptidases in normal muscle is obscure, this abnormality suggests that proteases may participate in posttranslational modification of proteins that are to be assembled into Z lines or, alternatively, in the disassembly and degradation of Z-line material.

Author Affiliations
From the Departments of Physiology (Dr Stauber), Neurology (Drs Stauber, Riggs, Gutmann, and Crosby), and Pathology (Dr Schochet), West Virginia University School of Medicine, Morgantown.

Footnotes
Accepted for publication March 12, 1985.

Read in part at the 36th Annual Meeting of the American Academy of Neurology, Boston, April 10, 1984.

Reprint requests to Department of Physiology, West Virginia University Medical Center, Morgantown, WV 26506 (Dr Stauber).

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