title: Proteomics of old world camelid (Camelus dromedarius): Better understanding the interplay between homeostasis and desert environment.
abstract: Life is the interplay between structural-functional integrity of biological systems and the influence of the external environment. To understand this interplay, it is useful to examine an animal model that competes with harsh environment. The dromedary camel is the best model that thrives under severe environment with considerable durability. The current proteomic study on dromedary organs explains a number of cellular mysteries providing functional correlates to arid living. Proteome profiling of camel organs suggests a marked increased expression of various cytoskeleton proteins that promote intracellular trafficking and communication. The comparative overexpression of α-actinin of dromedary heart when compared with rat heart suggests an adaptive peculiarity to sustain hemoconcentration-hemodilution episodes associated with alternative drought-rehydration periods. Moreover, increased expression of the small heat shock protein, α B-crystallin facilitates protein folding and cellular regenerative capacity in dromedary heart. The observed unbalanced expression of different energy related dependent mitochondrial enzymes suggests the possibility of mitochondrial uncoupling in the heart in this species. The evidence of increased expression of H+-ATPase subunit in camel brain guarantees a rapidly usable energy supply. Interestingly, the guanidinoacetate methyltransferase in camel liver has a renovation effect on high energy phosphate with possible concomitant intercession of ion homeostasis. Surprisingly, both hump fat tissue and kidney proteomes share the altered physical distribution of proteins that favor cellular acidosis. Furthermore, the study suggests a vibrant nature for adipose tissue of camel hump by the up-regulation of vimentin in adipocytes, augmenting lipoprotein translocation, blood glucose trapping, and challenging external physical extra-stress. The results obtained provide new evidence of homeostasis in the arid habitat suitable for this mammal.
authors: Department of Biochemistry, Faculty of Veterinary Medicine, Cairo University, Giza, Egypt ; Biotechnology Center for Services and Researches, Cairo University, Giza, Egypt.
authors: Mohamad
authors: M
authors: Warda
authors: Department of Biochemistry, Faculty of Veterinary Medicine, Cairo University, Giza, Egypt.
authors: Abdelbary
authors: A
authors: Prince
authors: National Research Laboratory for Mitochondrial Signaling, Department of Physiology, Cardiovascular and Metabolic Disease Center, Inje University, Busan 614-735, Republic of Korea.
authors: Hyoung Kyu
authors: HK
authors: Kim
authors: Animal Health Research Institute, Dokki, Giza, Egypt.
authors: Nagwa
authors: N
authors: Khafaga
authors: Field Investigation Department, Animal Reproduction Research Institute, Giza, Egypt.
authors: Tarek
authors: T
authors: Scholkamy
authors: Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USA.
authors: Robert J
authors: RJ
authors: Linhardt
authors: National Research Laboratory for Mitochondrial Signaling, Department of Physiology, Cardiovascular and Metabolic Disease Center, Inje University, Busan 614-735, Republic of Korea.
authors: Han
authors: H
authors: Jin
keywords: 2D, two-dimensional; ACTH, adrenocorticotropic hormone; Actin; CHAPS, 3-(3-cholamidopropyl)-dimethylammoniopropane sulfonate; CHCA, α-cyano-4-signal-to-noise; Camel; Crystallin; DAPLE, Dvl-associating protein with a high frequency of leucine residues; DTT, dithiothreitol; Dvl, dishevelled: scaffold protein involved in the regulation of the Wnt signaling pathway; IPG, immobilized pH gradient; MALDI, matrix assisted laser desorption ionization; MAPK, map kinase; MS, mass spectrometry; Metabolism; PAGE, polyacrylamide gel electrophoresis; PDB, protein database; PMF, peptide mass finger printing; Proteome; SDS, sodium dodecylsulfate; TFA, trifluoracetic acid; TOF, time of flight; Vimentin; hsp, heat shock protein; pI, isoelectric point