Connective tissue activation. XXXIII. Biologically active cleavage products of CTAP-III from human platelets.
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.
Rackham Arthritis Research Unit, Department of Internal Medicine, University of Michigan Medical School, Ann Arbor 49109-0358.
C W
CW
Castor
D A
DA
Walz
C G
CG
Ragsdale
P A
PA
Hossler
E M
EM
Smith
M C
MC
Bignall
B P
BP
Aaron
K
K
Mountjoy
D000595:Amino Acid Sequence; D001792:Blood Platelets / Q000378:metabolism*; D015153:Blotting, Western; D002850:Chromatography, Gel; D003238:Connective Tissue / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D006868:Hydrolysis; D008969:Molecular Sequence Data; D010455:Peptides / Q000302:isolation & purification*; D013583:Synovial Membrane / Q000166:cytology / Q000378:metabolism
D010455:Peptides; C009862:connective tissue-activating peptide