Connective tissue activation. XXXIII. Biologically active cleavage products of CTAP-III from human platelets |
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| Authors: | C W Castor D A Walz C G Ragsdale P A Hossler E M Smith M C Bignall B P Aaron K Mountjoy |
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| Institution: | Rackham Arthritis Research Unit, Department of Internal Medicine, University of Michigan Medical School, Ann Arbor 49109-0358. |
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| Abstract: | Evidence for three new isoforms of CTAP-III from human platelets is presented; two NH2-terminal cleavage products were identified, CTAP-III (des 1-13) and CTAP-III (des 1-15). CTAP-III (des 1-13) has a pI of 8.6 and is a relatively stable proteolytic cleavage product that retains the capacity to stimulate 14C]GAG synthesis in human synovial cell cultures. CTAP-III (des 1-15) appears to be an elastase or chymotrypsin cleavage product and identical to NAP-2, an entity thought to have neutrophil activating properties. |
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