Human alpha and beta parvalbumins. Structure and tissue-specific expression.
alpha and beta parvalbumins are Ca(2+)-binding proteins of the EF-hand type. We determined the protein sequence of human brain alpha parvalbumin by mass spectrometry and cloned human beta parvalbumin (or oncomodulin) from genomic DNA and preterm placental cDNA. beta parvalbumin differs in 54 positions from alpha parvalbumin and lacks the C-terminal amino acid 109. From MS analyses of alpha and beta parvalbumins we conclude that parvalbumins generally lack posttranslational modifications. alpha and beta parvalbumins were differently expressed in human tissues when analyzed by immunoblotting and polymerase-chain-reaction techniques. Whereas alpha parvalbumin was found in a number of adult human tissues, beta parvalbumin was restricted to preterm placenta. The pattern of alpha parvalbumin expression also differs in man compared to other vertebrates. For example, in rat, alpha parvalbumin was found in extrafusal and intrafusal skeletal-muscle fibres whereas, in man, alpha parvalbumin was restricted to the muscle spindles. Different functions for alpha and beta parvalbumins are discussed.
Föhr
U G
UG
Department of Pediatrics, University of Zurich, Switzerland.
Weber
B R
BR
Müntener
M
M
Staudenmann
W
W
Hughes
G J
GJ
Frutiger
S
S
Banville
D
D
Schäfer
B W
BW
Heizmann
C W
CW
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001921:Brain / Q000378:metabolism; D003001:Cloning, Molecular; D004247:DNA; D006801:Humans; D007150:Immunohistochemistry; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D009132:Muscles / Q000378:metabolism; D010320:Parvalbumins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics*; D010920:Placenta / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D051381:Rats; D017386:Sequence Homology, Amino Acid
D010320:Parvalbumins; D004247:DNA