Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.4.21.1 (
chymotrypsin
)
10,938
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Neutrophil-activating peptide 2
(
NAP-2
) is generated by cleavage of two inactive precursors, connective-tissue-activating peptide III (CTAP-III) and
platelet basic protein
(
PBP
), which are stored in the alpha-granules of blood platelets. Using highly purified CTAP-III as the substrate we studied the generation of
NAP-2
by several neutral tissue proteinases. CTAP-III was rapidly cleaved by
chymotrypsin
, cathepsin G and trypsin, yielding products with neutrophil-stimulating activity. This activity remained unchanged for 24 h in the presence of
chymotrypsin
, decreased only slowly in the presence of cathepsin G, but was rapidly destroyed by trypsin. CTAP-III was also degraded by human neutrophil elastase and porcine pancreatic elastase, but no active fragments were obtained. By contrast, no degradation of CTAP-III was observed with thrombin, plasmin or 'granzymes' from cytolytic T-lymphocyte granules. Two active fragments of CTAP-III, generated by
chymotrypsin
or cathepsin G, were purified and partially sequenced, and were found to have the same N-terminal sequence as
NAP-2
. These results indicate that both proteinases cleave preferentially the bond between amino acids 15 (Tyr) and 16 (Ala) of CTAP-III. We conclude that chymotrypsin-like proteolytic activity in the vicinity of activated platelets may generate
NAP-2
intravascularly. Due to its presence in the primary granules of neutrophils and monocytes cathepsin G is likely to be involved in this process.
...
PMID:Formation of neutrophil-activating peptide 2 from platelet-derived connective-tissue-activating peptide III by different tissue proteinases. 203 37
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.
...
PMID:Connective tissue activation. XXXIII. Biologically active cleavage products of CTAP-III from human platelets. 278 11
