Open AccessHuman α and β parvalbumins
Author(s) -
FÖHR Ursula G.,
WEBER Barbara R.,
MÜNTENER Markus,
STAUDENMANN Werner,
HUGHES Graham J.,
FRUTIGER Séverine,
BANVILLE Denis,
SCHÄFER Beat W.,
HEIZMANN Claus W.
Publication year - 1993
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1993.tb18084.x
Subject(s) - parvalbumin , alpha (finance) , biology , microbiology and biotechnology , complementary dna , beta (programming language) , peptide sequence , biochemistry , gene , genetics , medicine , construct validity , nursing , computer science , patient satisfaction , programming language
α and β parvalbumins are Ca 2+ ‐binding proteins of the EF‐hand type. We determined the protein sequence of human brain α parvalbumin by mass spectrometry and cloned human β parvalbumin (or oncomodulin) from genomic DNA and preterm placental cDNA. β parvalbumin differs in 54 positions from α parvalbumin and lacks the C‐terminal amino acid 109. From MS analyses of α and β parvalbumins we conclude that parvalbumins generally lack posttranslational modifications. α and β parvalbumins were differently expressed in human tissues when analyzed by immunoblotting and polymerase‐chain‐reaction techniques. Whereas α parvalbumin was found in a number of adult human tissues, β parvalbumin was restricted to preterm placenta. The pattern of α parvalbumin expression also differs in man compared to other vertebrates. For example, in rat, α parvalbumin was found in extrafusal and intrafusal skeletal‐muscle fibres whereas, in man, α parvalbumin was restricted to the muscle spindles. Different functions for α and β parvalbumins are discussed.