Disease relevance of PF4V1

• Thus, activated platelets release CXCL4L1, a potent regulator of endothelial cell biology, which affects angiogenesis and vascular diseases [1].

High impact information on PF4V1

• Northern blot and primer extension studies show that steady-state platelet PF4 mRNA levels are approximately one magnitude greater than PF4alt mRNA levels [2].
• This pyrimidine-rich region is absent from the PF4alt gene; however, DNA homology exists between the two human genes in the 5'- and 3'-flanking regions and extends for over 3.6 kb [2].
• PF4alt contains three amino acid substitutions (P58----L, K66----E, and L67----H) near the C-terminus, in a region known to be critical for PF4 function [2].
• Rat PF4 and human PF4var1 genes had identical 18-base sequences 5' to the promoter region [3].
• The gene for PF4var1 consisted of three exons and two introns [3].

Biological context of PF4V1

• Alternating purine/pyrimidine tracts occur both 5' and 3' to PF4 and PF4alt but do not define the endpoints of the gene duplication, which extend beyond these sequences at least at the 5' end [2].
• By comparing the PF4var1 genomic sequence with the known human cDNA and the rat genomic PF4-coding sequences, we identified potential genetic regulatory regions for PF4var1 [3].

Anatomical context of PF4V1

• In vivo, CXCL4L1 was also more effective than CXCL4 in inhibiting bFGF-induced angiogenesis in rat corneas [1].

Associations of PF4V1 with chemical compounds

• However, PF4var1 had amino acid differences at three positions in the lysine-rich carboxy-terminal end that were all conserved among human, bovine, and rat PF4s [3].

Other interactions of PF4V1

• Here, the product of the nonallelic variant gene of CXCL4, PF-4var1/PF-4alt, designated CXCL4L1, was isolated for the first time from thrombin-stimulated human platelets and purified to homogeneity [1].

References