Keeping the blood flowing-plasminogen activator genes and feeding behavior in vampire bats.
The blood feeding vampire bats emerged from New World leaf-nosed bats that fed on fruit and insects. Plasminogen activator, a serine protease that regulates blood coagulation, is known to be expressed in the saliva of Desmodus rotundus (common vampire bat) and is thought to be a key enzyme for the emergence of blood feeding in vampire bats. To better understand the evolution of this biological function, we studied the plasminogen activator (PA) genes from all vampire bat species in light of their feeding transition to bird and subsequently mammalian blood. We include the rare species Diphylla ecaudata and Diaemus youngi, where plasminogen activator had not previously been studied and demonstrate that PA gene duplication observed in Desmodus is not essential to the vampire phenotype, but relates to the emergence of predominant mammalian blood feeding in this species. Plasminogen activator has evolved through gene duplication, domain loss, and sequence evolution leading to change in fibrin-specificity and susceptibility to plasminogen activator inhibitor-1. Before undertaking this study, only the four plasminogen activator isoforms from Desmodus were known. The evolution of vampire bat plasminogen activators can now be linked phylogenetically to the transition in feeding behavior among vampire bat species from bird to mammalian blood.
Tellgren-Roth
Asa
A
Department of Molecular Biology, University of Wyoming, Laramie, WY, 82071, USA.
Dittmar
Katharina
K
Massey
Steven E
SE
Kemi
Cecilia
C
Tellgren-Roth
Christian
C
Savolainen
Peter
P
Lyons
Leslie A
LA
Liberles
David A
DA
D000818:Animals; D001783:Blood Flow Velocity / Q000235:genetics; D002685:Chiroptera / Q000097:blood / Q000235:genetics* / Q000502:physiology; D003001:Cloning, Molecular; D005091:Exons / Q000235:genetics; D005247:Feeding Behavior / Q000502:physiology*; D008957:Models, Genetic; D010802:Phylogeny; D010960:Plasminogen Activators / Q000235:genetics*; D011336:Probability; D020133:Reverse Transcriptase Polymerase Chain Reaction
D010960:Plasminogen Activators
J Biol Chem. 1998 Jul 17;273(29):18292-9
9660794
J Struct Funct Genomics. 2003;3(1-4):35-44
12836683
J Thromb Haemost. 2007 Apr;5(4):804-11
17408411
Nature. 1994 Mar 31;368(6470):419-24
8133887
Mol Biol Evol. 2001 Nov;18(11):2040-7
11606700
Gene. 1991 Sep 15;105(2):229-37
1937019
Ann N Y Acad Sci. 1992 Dec 4;667:395-403
1309059
J Exp Biol. 1997 Dec;200(Pt 23):3003-12
9359889
Mol Biol Evol. 2005 Dec;22(12):2472-9
16107592
Thromb Haemost. 2005 Apr;93(4):631-40
15841306
Bioinformatics. 2005 Mar 1;21(5):676-9
15509596
Biochemistry (Mosc). 2002 Jan;67(1):143-50
11841349
Syst Biol. 2004 Oct;53(5):793-808
15545256
Nature. 1966 Jul 23;211(5047):434-5
5967844
Thromb Haemost. 2004 Nov;92(5):956-65
15543321
J Biol Chem. 1991 Mar 15;266(8):5191-201
1900516
J Biochem. 1992 Feb;111(2):244-8
1314812
Mol Biol Evol. 2007 Aug;24(8):1586-91
17483113
J Mol Evol. 2007 Nov;65(5):574-88
17957399
Stroke. 2003 Feb;34(2):537-43
12574572
Mol Biol Evol. 2005 Apr;22(4):1107-18
15689528
J Biol Chem. 1989 Oct 25;264(30):17947-52
2509450
Syst Biol. 2003 Oct;52(5):696-704
14530136
Mol Biol Evol. 1998 May;15(5):568-73
9580986
Bioinformatics. 1998;14(9):817-8
9918953
Curr Opin Struct Biol. 1997 Dec;7(6):865-72
9434908
Bioinformatics. 2003 Aug 12;19(12):1572-4
12912839
J Exp Zool B Mol Dev Evol. 2007 Jan 15;308(1):58-73
16838295
Biochemistry. 1997 Nov 4;36(44):13483-93
9354616
Nucleic Acids Res. 2005 Jan 20;33(2):511-8
15661851