Document Detail


A serum-derived hyaluronan-associated protein (SHAP) is the heavy chain of the inter alpha-trypsin inhibitor.
MedLine Citation:
PMID:  7504674     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
We showed previously that hyaluronan (HA) synthesized by cultured fibroblasts firmly bound 85-kDa proteins. The proteins were derived from serum used for the culture and appeared to be covalently linked to HA (Yoneda, M., Suzuki, S., and Kimata, K. (1990) J. Biol. Chem. 265, 5247-5257). In these regards, we named this molecule SHAP (serum-derived HA associated proteins). Incubation of serum with exogenous HA under physiological conditions enabled us to prepare SHAP.HA complex without cell cultivation. The complex thus obtained from bovine or human serum was served for the characterization of SHAP. Digestion with HA-lyase and subsequent separation on SDS-polyacrylamide gel electrophoresis yielded two components, X and Y. Because of the block of their NH2 termini, peptides were obtained by the digestion of X and Y with V8 protease, separated on SDS-polyacryl-amide gel electrophoresis and then subjected to the analysis. Peptides from X and Y showed a high degree of sequence similarity to the two heavy chains, HC2 and HC1, of human inter-alpha-trypsin inhibitor (ITI), respectively (over 80% with bovine SHAP and essentially 100% with human SHAP). Cross-reactivity with antibodies against ITI supported the findings. Direct digestion of the complex with V8 protease and the subsequent purification of the HA-resistant fragment complex were performed to identify the HA-binding domains. NH2-terminal sequences of the fragments suggested the participation of the COOH-terminal half of ITI with an amphipathic alpha helix structure in the HA binding.
Authors:
L Huang; M Yoneda; K Kimata
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  268     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1993 Dec 
Date Detail:
Created Date:  1994-01-13     Completed Date:  1994-01-13     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  26725-30     Citation Subset:  IM    
Affiliation:
Institute for Molecular Science of Medicine, Aichi Medical University, Japan.
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MeSH Terms
Descriptor/Qualifier:
Alpha-Globulins / chemistry*,  immunology
Amino Acid Sequence
Animals
Blood
Cattle
Cells, Cultured
Humans
Hyaluronic Acid / metabolism
Molecular Sequence Data
Peptide Mapping
Sequence Homology, Amino Acid
Chemical
Reg. No./Substance:
0/Alpha-Globulins; 39346-44-6/inter-alpha-inhibitor; 9004-61-9/Hyaluronic Acid

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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