Abstract: Connective Tissue Activation XXXVIII: Heparin/Heparanase Activity of Human Platelets Resides in a High Molecular Weight Protein, Not in Connective Tissue Activating Peptide III

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Connective Tissue Activation XXXVIII: Heparin/Heparanase Activity of Human Platelets Resides in a High Molecular Weight Protein, Not in Connective Tissue Activating Peptide III

C. WILLIAM CASTOR, ALINA KOTLYAR, and BRIAN E. EDWARDS

ABSTRACT

Objective. Connective tissue activating protein-III (CTAP-III), with molecular weight 9278 Da and isoforms including CTAP-III des 1-15 (neutrophil activating peptide-2, NAP-2) and other amino terminal deletion isoforms, has been isolated from human platelets and characterized. Platelets have also been shown to possess significant heparin/heparanase activity. We investigated whether human platelet heparin/heparanase activity derives from CTAP-III.

Methods. Radial immunodiffusion measurement showed substantial amounts of CTAP-III in plasma from outdated platelet packs. A convenient method for measurement of heparin/heparanase activity is described, and with this method platelet associated plasma was investigated for heparin/heparanase activity assayed against ³H-heparin and ³⁵S-heparan sulfate.

Results. Removal of CTAP-III from platelet associated plasma with an immunospecific immunoaffinity column did not remove the heparin/heparanase activity from the plasma. Highly purified CTAP-III eluted from an immunospecific affinity column lacked heparin/heparanase activity.

Conclusion. Human platelet heparin/heparanase activity resides not in CTAP-III but in a protein or proteins with molecular weight ³ 55 kDa. (J Rheumatol 2002;29:2337-44)

Key Indexing Terms:

HEPARIN/HEPARANASE ACTIVITY
CONNECTIVE TISSUE ACTIVATING PEPTIDE-III
PLATELET FACTOR-4

From the Rackham Arthritis Research Unit and Rheumatology Division, Department of Internal Medicine, The University of Michigan Medical School, Ann Arbor; and the Department of Biochemistry and Molecular Biology, Wayne State University, Detroit, Michigan, USA.

Supported by USPHS grant AR10728 and Multipurpose Arthritis Center grant NIH P60 AR 20551.

C.W. Castor, MD, Professor Emeritus of Internal Medicine; A. Kotlyar, Health Science Research Associate II, University of Michigan Medical School; B.E. Edwards, PhD, Professor of Biochemistry, Wayne State University.

Address reprint requests to Dr. C.W. Castor, University of Michigan Medical Center, Department of Internal Medicine, Division of Rheumatology, 3918 Taubman Center, Box 0358, 1500 East Medical Center Drive, Ann Arbor, MI 48109-0358.

Submitted October 2, 2001; revision accepted May 13, 2002.