Literature DB >> 2783111

Connective tissue activation. XXXIII. Biologically active cleavage products of CTAP-III from human platelets.

C W Castor1, D A Walz, C G Ragsdale, P A Hossler, E M Smith, M C Bignall, B P Aaron, K Mountjoy.   

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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Year:  1989        PMID: 2783111     DOI: 10.1016/0006-291x(89)92330-9

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

1.  Formation of neutrophil-activating peptide 2 from platelet-derived connective-tissue-activating peptide III by different tissue proteinases.

Authors:  B D Car; M Baggiolini; A Walz
Journal:  Biochem J       Date:  1991-05-01       Impact factor: 3.857

2.  Elevated levels of CXC chemokine connective tissue activating peptide (CTAP)-III in lung cancer patients.

Authors:  Gina Lee; Brian K Gardner; David A Elashoff; Colleen M Purcell; Harpavan S Sandha; Jenny T Mao; Kostyantyn Krysan; Jay M Lee; Steven M Dubinett
Journal:  Am J Transl Res       Date:  2011-04-02       Impact factor: 4.060

  2 in total

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