Advertisement

Research Article Free access | 10.1172/JCI114598

Relationship of one form of human histamine-releasing factor to connective tissue activating peptide-III.

M L Baeza, S R Reddigari, D Kornfeld, N Ramani, E M Smith, P A Hossler, T Fischer, C W Castor, P G Gorevic, and A P Kaplan

Department of Medicine, State University of New York, Stony Brook 11794-8161.

Find articles by Baeza, M. in: PubMed | Google Scholar

Department of Medicine, State University of New York, Stony Brook 11794-8161.

Find articles by Reddigari, S. in: PubMed | Google Scholar

Department of Medicine, State University of New York, Stony Brook 11794-8161.

Find articles by Kornfeld, D. in: PubMed | Google Scholar

Department of Medicine, State University of New York, Stony Brook 11794-8161.

Find articles by Ramani, N. in: PubMed | Google Scholar

Department of Medicine, State University of New York, Stony Brook 11794-8161.

Find articles by Smith, E. in: PubMed | Google Scholar

Department of Medicine, State University of New York, Stony Brook 11794-8161.

Find articles by Hossler, P. in: PubMed | Google Scholar

Department of Medicine, State University of New York, Stony Brook 11794-8161.

Find articles by Fischer, T. in: PubMed | Google Scholar

Department of Medicine, State University of New York, Stony Brook 11794-8161.

Find articles by Castor, C. in: PubMed | Google Scholar

Department of Medicine, State University of New York, Stony Brook 11794-8161.

Find articles by Gorevic, P. in: PubMed | Google Scholar

Department of Medicine, State University of New York, Stony Brook 11794-8161.

Find articles by Kaplan, A. in: PubMed | Google Scholar

Published May 1, 1990 - More info

Published in Volume 85, Issue 5 on May 1, 1990
J Clin Invest. 1990;85(5):1516–1521. https://doi.org/10.1172/JCI114598.
© 1990 The American Society for Clinical Investigation
Published May 1, 1990 - Version history
View PDF
Abstract

We have previously reported purification of three forms of histamine-releasing factors (HRFs) from mixtures of streptokinase-streptodornase stimulated human mononuclear cells and platelets with apparent molecular masses of 10-12, 15-17, and 40-41 kD (1989. J. Clin. Invest. 83:1204-1210). We have also prepared mouse MAbs against the 10-12-kD HRF (1989. J. Allergy Clin. Immunol. 83:281). Affinity-purified 10-12-kD HRF appears as a broad band upon polyacrylamide gel electrophoresis in the presence of SDS. We determined the NH2-terminal amino acid sequence of the top and bottom halves of this broad band. Sequence analysis revealed striking homology between this HRF and connective tissue activating peptide-III (CTAP-III), a platelet-derived 8-10-kD protein known to cause mitogenesis and extracellular matrix formation in fibroblast cultures. 19 of 21 NH2-terminal residues in the top half of the HRF band were identical to the NH2-terminal sequence of CTAP-III. 20 of 21 NH2-terminal residues in the bottom half were identical to the NH2-terminal sequence of neutrophil-activating peptide-2, which is derived from CTAP-III by proteolytic cleavage between residues 15 and 16. Purified CTAP-III also released histamine from basophils. Rabbit antiserum raised against either native or recombinant CTAP-III recognized affinity-purified HRF in immunodot blot assays, and MAb against HRF recognized CTAP-III in both dot blot and microtiter plate based immunoassays. These data demonstrate the first structural, functional, and immunologic relationship between one form of human HRF and a previously described cell product.

Images.

Browse pages

Click on an image below to see the page. View PDF of the complete article

Version history
  • Version 1 (May 1, 1990): No description
Advertisement
Advertisement