Document Detail

Alkali-treated collagen retained the triple helical conformation and the ligand activity for the cell adhesion via alpha2beta1 integrin.
MedLine Citation:
PMID:  10101279     Owner:  NLM     Status:  MEDLINE    
Alkaline treatment is a good method for extracting collagen with high recovery even from an aged animal specimen. However, the properties of collagen treated under alkaline conditions have not been well established yet. By the treatment with a solution of 3% sodium hydroxide and 1.9% monomethylamine, the isoelectric point of type I collagen was lowered from 9.3 to 4.8 because of the conversions of Asn and Gln to Asp and Glu. With the acidification of the pI, the denaturation temperature of the collagen was decreased from 42 to 35 degrees C after 20 d treatment, but the collagen-specific triple helical conformation was maintained. Human keratinocytes and fibroblasts adhered to the alkali-treated collagen via the collagen receptor integrin alpha2beta1. This indicates that the alkali-treated collagen maintained its property as a biological adherent molecule. Unlike acid-soluble collagen, alkali-treated collagen lost the ability to form fibrils at neutral pH under physiological conditions. This ability was lost even after 4 h of alkaline treatment, when the denaturation temperature of the collagen did not change. On the other hand, the alkali-treated collagen formed a fibrous precipitate with a uniform diameter of 50-70 nm under acidic conditions at 30 degrees C.
S Hattori; E Adachi; T Ebihara; T Shirai; I Someki; S Irie
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Publication Detail:
Type:  In Vitro; Journal Article    
Journal Detail:
Title:  Journal of biochemistry     Volume:  125     ISSN:  0021-924X     ISO Abbreviation:  J. Biochem.     Publication Date:  1999 Apr 
Date Detail:
Created Date:  1999-08-05     Completed Date:  1999-08-05     Revised Date:  2007-12-19    
Medline Journal Info:
Nlm Unique ID:  0376600     Medline TA:  J Biochem     Country:  JAPAN    
Other Details:
Languages:  eng     Pagination:  676-84     Citation Subset:  IM    
Nippi Research Institute of Biomatrix, Adachi-ku, Tokyo, 120-8601, Japan.
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MeSH Terms
Amino Acid Sequence
Cell Adhesion / physiology
Cells, Cultured
Collagen / chemistry*,  isolation & purification,  metabolism
Fibroblasts / cytology,  metabolism
Hydrogen-Ion Concentration
Integrins / metabolism
Isoelectric Point
Keratinocytes / cytology,  metabolism
Microscopy, Electron
Molecular Sequence Data
Protein Conformation
Protein Denaturation
Receptors, Collagen
Skin / chemistry
Reg. No./Substance:
0/Alkalies; 0/Integrins; 0/Ligands; 0/Receptors, Collagen; 9007-34-5/Collagen

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