title: Evolution of herbivory in a carnivorous clade of minnows (teleostei: cyprinidae): effects on gut size and digestive physiology.
abstract: We constructed a phylogeny for 10 minnow species (family Cyprinidae) previously revealed to be members of sister genera with different dietary affinities and used the phylogeny to examine whether the evolution of digestive tract size and physiology is correlated with the evolution of diet in these fishes. We studied a total of 11 taxa: four herbivorous species in the genus Campostoma and six largely carnivorous species in the genus Nocomis, including two populations of Nocomis leptocephalus, the carnivorous Chattahoochee River drainage population and the herbivorous Altamaha River drainage population. Thus, we were able to compare digestive tract size and physiology among sister genera (Campostoma and Nocomis) and among sister taxa (N. leptocephalus Chattahoochee and N. leptocephalus Altamaha) in dietary and phylogenetic contexts. The herbivorous taxa had longer digestive tracts and higher activity of the carbohydrases amylase and laminarinase in their guts, whereas the carnivorous species had higher chitinase activity. Phylogenetic independent-contrast analysis suggested that the evolution of amylase and chitinase activities was correlated with the evolution of diet in these species, whereas trypsin and lipase activities showed no pattern associated with diet or phylogenetic history. Concentrations of short-chain fatty acids were low in all taxa, indicating that these fishes rely largely on endogenous digestive mechanisms to subsist on their respective diets. Subtle differences in tooth shape were observed between species in the two genera. Overall, our results suggest that dietary specialization can be observed on the level of anatomy and physiology of the digestive tracts of fishes but that such differences are most appropriately viewed in comparisons of closely related species with different diets.
authors.affiliation: Department of Biology, University of Florida, Gainesville, Florida 32611, USA. dgerman@uci.edu
authors.forename: Donovan P
authors.initials: DP
authors.lastname: German
authors.forename: Brett C
authors.initials: BC
authors.lastname: Nagle
authors.forename: Jennette M
authors.initials: JM
authors.lastname: Villeda
authors.forename: Ana M
authors.initials: AM
authors.lastname: Ruiz
authors.forename: Alfred W
authors.initials: AW
authors.lastname: Thomson
authors.forename: Salvador
authors.initials: S
authors.lastname: Contreras Balderas
authors.forename: David H
authors.initials: DH
authors.lastname: Evans
mesh_terms: D000681:Amylases / Q000502:physiology; D000818:Animals; D044602:Cellulases / Q000502:physiology; D002688:Chitinases / Q000502:physiology; D003530:Cyprinidae / Q000033:anatomy & histology / Q000235:genetics / Q000502:physiology*; D045303:Cytochromes b / Q000737:chemistry / Q000235:genetics; D004247:DNA / Q000737:chemistry / Q000235:genetics; D004068:Digestive System Physiological Phenomena / Q000235:genetics; D019143:Evolution, Molecular; D005136:Eye Proteins / Q000737:chemistry / Q000235:genetics; D005766:Gastrointestinal Contents / Q000737:chemistry / Q000201:enzymology; D041981:Gastrointestinal Tract / Q000033:anatomy & histology / Q000201:enzymology / Q000502:physiology*; D008855:Microscopy, Electron, Scanning; D010802:Phylogeny; D016133:Polymerase Chain Reaction; D012177:Retinol-Binding Proteins / Q000737:chemistry / Q000235:genetics; D012243:Rhodopsin / Q000737:chemistry / Q000235:genetics; D017422:Sequence Analysis, DNA; D014070:Tooth / Q000033:anatomy & histology / Q000648:ultrastructure; D000099214:Retinol-Binding Proteins, Interstitial
chemical_list: D000681:Amylases; D044602:Cellulases; D002688:Chitinases; D045303:Cytochromes b; D004247:DNA; D005136:Eye Proteins; D012177:Retinol-Binding Proteins; D012243:Rhodopsin; D000099214:Retinol-Binding Proteins, Interstitial