Characterization and expression of a novel human fatty acid-binding protein: the epidermal type (E-FABP).
Biochem Biophys Res Commun
; 190(2): 482-7, 1993 Jan 29.
Article
in En
| MEDLINE
| ID: mdl-8427590
ABSTRACT
Using PAGE--Autoradioblotting technique we have characterized an E--FABP in human epidermal cells that is distinct from liver-, heart-, intestine- and adipose tissue-FABPs. FABP radiobinding analysis was performed directly on protein extracts without prior partial purification. E-FABP has a Mr of approximately 15 kDa and binds oleic acid with high affinity but does not bind all-trans-, 13-cis- and 9-cis-retinoic acid nor all-trans-retinol. Expression levels of E-FABP were low in normal epidermis, higher in human cultured keratinocytes and still higher in psoriasis, a disease characterized by abnormal epidermal differentiation. These findings suggest that epidermal cells may have a distinct fatty acid metabolism compared to other tissues.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Carrier Proteins
/
Tumor Suppressor Proteins
/
Epidermis
/
Neoplasm Proteins
Limits:
Humans
Language:
En
Journal:
Biochem Biophys Res Commun
Year:
1993
Document type:
Article
Affiliation country: