(Ciencias de Joseleg)(Biología)(Introducción y biología
celular)(La
sangre)(Introducción)(Historia)(El
citosol y otros fluidos intracelulares)(Diferentes
tipos de sangre)(Los
colores de la sangre)(Las
funciones de la sangre)(Plasma
sanguíneo y sus componentes)(Propiedades
de la sangre total y su análisis)(Sistema
de grupos sanguíneos)(Glóbulos
rojos o eritrocitos)(Glóbulos
blancos o leucocitos)(Las
plaquetas o trolbocitos)(Hematopoyesis)(Origen
de otros componentes de la sangre)(Referencias
bibliográficas)(Versión
documento word)
Abedin, M., & King, N. (2010). Diverse evolutionary paths to cell
adhesion. Trends in Cell Biology, 20(12), 734–742.
Adams, S. L. (1989). The medicinal
leech: historical perspectives. In Seminars in thrombosis and hemostasis
(Vol. 15, pp. 261–264). Copyright© 1989 by Thieme Medical Publishers, Inc.
Alberts, B., Bray, D., Hopkin, K.,
Johnson, A., Lewis, J., & Raff, M. (2004). Tissues and cancer. Essential
Cell Biology. New York, 698–706.
Angelini, P., Villason, S., Chan Jr,
A. V, & Diez, J. (1999). Normal and Anomalous Coronary Arteries in Humans.
Part 1: Historical Background.
Antonova, O., Yossifova, L., Staneva,
R., Stevanovic, S., Dolashka, P., & Toncheva, D. (2015). Changes in the
gene expression profile of the bladder cancer cell lines after treatment with
Helix lucorum and Rapana venosa hemocyanin. J. BUON, 20(1),
180–187.
Aw, T. Y. (1999). Intracellular
compartmentation of organelles and gradients of low molecular weight species. International
Review of Cytology, 192, 223–253.
Azizi, M.-H., Nayernouri, T., &
Azizi, F. (2008). A brief history of the discovery of the circulation of blood
in the human body. Arch Iran Med, 11(3), 345–350.
Bashkin, P., Doctrow, S., Klagsbrun,
M., Svahn, C. M., Folkman, J., & Vlodavsky, I. (1989). Basic fibroblast
growth factor binds to subendothelial extracellular matrix and is released by
heparitinase and heparin-like molecules. Biochemistry, 28(4),
1737–1743.
Berg, J. M., Tymoczko, J. L., &
Stryer, L. (2002). Biochemical evolution. In Biochemistry (5th ed., pp.
56–82). Freeman. Retrieved from
https://docs.google.com/file/d/0B0HRqdV3D7xIZGNlNmRmY2YtZGY3NS00YmJiLTkyYzQtNWFkOWYwMWVlNjA1/edit
Boyanova, O., Dolashka, P., Toncheva,
D., Rammensee, H., & Stevanović, S. (2013). In vitro effect of molluscan
hemocyanins on CAL‑29 and T‑24 bladder cancer cell lines. Biomedical Reports,
1(2), 235–238.
Bremer, P., Flint, S., Brooks, J.,
& Palmer, J. (2015). Introduction to Biofilms. Biofilms in the Dairy
Industry, 1–16.
Brewer, D. B. (2006). Max Schultze
(1865), G. Bizzozero (1882) and the discovery of the platelet. British
Journal of Haematology, 133(3), 251–258.
Bright, G. R., Fisher, G. W.,
Rogowska, J., & Taylor, D. L. (1987). Fluorescence ratio imaging
microscopy: temporal and spatial measurements of cytoplasmic pH. The Journal
of Cell Biology, 104(4), 1019–1033.
Brownlee, C. (2002). Role of the
extracellular matrix in cell–cell signalling: paracrine paradigms. Current
Opinion in Plant Biology, 5(5), 396–401.
Brusca, R., Brusca, G. J., &
Haver, N. J. (2003). Invertebrates (2nd ed.). Sinauer Associates.
Burmester, T., & Hankeln, T.
(2004). Neuroglobin: a respiratory protein of the nervous system. Physiology,
19(3), 110–113.
Burmester, T., Weich, B., Reinhardt,
S., & Hankeln, T. (2000). A vertebrate globin expressed in the brain. Nature,
407(6803), 520–523.
Campbell, M. K., & Farrell, S. O.
(2012). Biochemistry (7th ed.). Canadá: Brooks/Cole.
Cate, J. H. D. (2001). Construction
of low-resolution x-ray crystallographic electron density maps of the ribosome.
Elsevier.
Clegg, J. S. (1984). Properties and
metabolism of the aqueous cytoplasm and its boundaries. American Journal of
Physiology-Regulatory, Integrative and Comparative Physiology, 246(2),
R133–R151.
Coates, C. J., & Nairn, J.
(2014). Diverse immune functions of hemocyanins. Developmental & Comparative Immunology, 45(1), 43–55.
Dalla Bona, F.
(2004). Dolci pagine: la pasticceria napoletana nell´ opera di Matilde Serao. Revista
de Italianística, (9), 149–154.
Daniels, G. (2008). Human blood
groups. John Wiley & Sons.
De Duve, C.,
& Pizano, M. (1995). Polvo vital: origen y evolución de la vida en la
tierra. Norma, Bogotá.
Donlan, R. M. (2016). Microbial
biofilms. Centers for Disease Control and Prevention.
Doolittle, R. F. (1984). The plasma
proteins.
Doyle, L. (1989). Gabriel Andral
(1797-1876) and the first reports of lymphangitis carcinomatosa. Journal of
the Royal Society of Medicine, 82(8), 491.
Ellis, R. J. (2001a). Macromolecular
crowding: an important but neglected aspect of the intracellular environment. Current
Opinion in Structural Biology, 11(1), 114–119.
Ellis, R. J. (2001b). Macromolecular
crowding: obvious but underappreciated. Trends in Biochemical Sciences, 26(10),
597–604.
Elsholtz, J.-S. (1966). Clysmatica
nova: sive ratio, qua in venam sectam medicamenta immitti possunt... ex
Officina G. Schultzi.
Friedman, M. T., West, K. A., &
Bizargity, P. (2016). Immunohematology and Transfusion Medicine.
Springer.
Fröls, S. (2013). Archaeal biofilms:
widespread and complex. Portland Press Limited.
Gallagher, J. T., & Lyon, M.
(2000). Molecular structure of heparan sulfate and interactions with growth
factors and morphogens. Proteoglycans: Structure, Biology and Molecular
Interactions, 27–59.
Giangrande, P. L. F. (2000). The
history of blood transfusion. British Journal of Haematology, 110(4),
758–767.
Góngora-Biachi, R. A. (2005). La sangre en la historia de la humanidad. Rev Biomed, 16(4), 281–288.
Goodenough, J., & McGuire, B.
(2012). Biology of Humans, Concepts, Applications and Issues (4th ed.).
San Francisco: Pearson, Benjamin Cummings.
Guncheva, M., Paunova, K., Ossowicz,
P., Rozwadowski, Z., Janus, E., Idakieva, K., … Apostolova, S. (2016). Rapana
thomasiana hemocyanin modified with ionic liquids with enhanced anti breast
cancer activity. International Journal of Biological Macromolecules, 82,
798–805.
Hart, G. D. (2001). Descriptions of
blood and blood disorders before the advent of laboratory studies. British
Journal of Haematology, 115(4), 719–728.
Harvey, W. (1959). De motu cordis. The
American Journal of the Medical Sciences, 237(4), 543.
Hay, E. D. (2013). Cell biology of
extracellular matrix. Springer Science & Business Media.
Hensch, T. K. (2005). Critical period
mechanisms in developing visual cortex. Current Topics in Developmental
Biology, 69, 215–237.
Huleihel, L., Hussey, G. S., Naranjo,
J. D., Zhang, L., Dziki, J. L., Turner, N. J., … Badylak, S. F. (2016).
Matrix-bound nanovesicles within ECM bioscaffolds. Science Advances, 2(6),
e1600502.
Iozzo, R. V. (1998). Matrix proteoglycans:
from molecular design to cellular function. Annual Review of Biochemistry,
67(1), 609–652.
Ito, J., Parsons, H. T., &
Heazlewood, J. L. (2014). The Arabidopsis cytosolic proteome: the metabolic
heart of the cell.
Izaguirre-Ávila,
R., & de Micheli, A. (2005). Evolución del conocimiento sobre la sangre y
su movimiento: Parte II. El saber sobre su composición. Iatroquímica de la
sangre. Revista de Investigación Clínica, 57(1), 85–97.
Izaguirre, A.
R., & de Micheli, A. (2001). History of blood transfusion. Revista de
Investigacion Clinica; Organo Del Hospital de Enfermedades de La Nutricion,
54(6), 552–558.
Jaenicke, E., Pairet, B., Hartmann,
H., & Decker, H. (2012). Crystallization and preliminary analysis of
crystals of the 24-meric hemocyanin of the emperor scorpion (Pandinus
imperator). PloS One, 7(3), e32548.
Jaffe, L. F. (1993). Classes and
mechanisms of calcium waves. Cell Calcium, 14(10), 736–745.
Jaulin, P., & Lefrère, J. J.
(2010). First French transfusions (1667-1668). Transfusion Clinique et
Biologique: Journal de La Societe Francaise de Transfusion Sanguine, 17(4),
205–217.
Kampen, K. R. (2012). The discovery
and early understanding of leukemia. Leukemia Research, 36(1),
6–13.
Kardong, K. V. (2011). Vertebrates,
comparative anatomy, function, evolution (6th ed.). McGraw-Hill New York.
Kardong, K. V. (2014). Vertebrates:
Comparative Anatomy, Function, Evolution (7th ed.). McGraw-Hill Education.
Karp, G. C. (2013). Cell and
Molecular Biology, Concepts and Experiments (7th ed.). USA: Wiley Online
Library.
Khan, I. A., Daya, S. K., &
Gowda, R. M. (2005). Evolution of the theory of circulation. International
Journal of Cardiology, 98(3), 519–521.
Kholodenko, B. N. (2003).
Four-dimensional organization of protein kinase signaling cascades: the roles
of diffusion, endocytosis and molecular motors. Journal of Experimental
Biology, 206(12), 2073–2082.
Kostakioti, M., Hadjifrangiskou, M.,
& Hultgren, S. J. (2013). Bacterial biofilms: development, dispersal, and
therapeutic strategies in the dawn of the postantibiotic era. Cold Spring
Harbor Perspectives in Medicine, 3(4), a010306.
Kumar, V., Abbas, A. K., Fausto, N.,
& Aster, J. C. (2014). Robbins and Cotran pathologic basis of disease.
Elsevier Health Sciences.
Landau, M., & Fagien, S. (2015).
Science of hyaluronic acid beyond filling: Fibroblasts and their response to
the extracellular matrix. Plastic and Reconstructive Surgery, 136(5S),
188S-195S.
Latzer, Y., Witztum, E., & Stein,
D. (2008). Eating disorders and disordered eating in Israel: An updated review.
European Eating Disorders Review, 16(5), 361–374.
Learoyd, P. (2012). The history of
blood transfusion prior to the 20th century–part 2. Transfusion Medicine,
22(6), 372–376.
Lee, C., Collins-Hall, J., Hendrick,
D., & Brabetz, B. (2016). Hemocyanin; Don’t Get in the Way of Blue Bloods.
Linzen, B. (2013). Invertebrate
oxygen carriers. Springer Science & Business Media.
Love, W. E., Klock, P. A., Lattman,
E. E., Padlan, E. A., Ward, K. B., & Hendrickson, W. A. (1972). The
structures of lamprey and bloodworm hemoglobins in relation to their evolution
and function. In Cold Spring Harbor symposia on quantitative biology
(Vol. 36, pp. 349–357). Cold Spring Harbor Laboratory Press.
Luby-Phelps, K. (1999).
Cytoarchitecture and physical properties of cytoplasm: volume, viscosity,
diffusion, intracellular surface area. International Review of Cytology,
192, 189–221.
Luby-Phelps, K., Castle, P. E.,
Taylor, D. L., & Lanni, F. (1987). Hindered diffusion of inert tracer
particles in the cytoplasm of mouse 3T3 cells. Proceedings of the National
Academy of Sciences, 84(14), 4910–4913.
MARKL, J. (1986). Evolution and
function of structurally diverse subunits in the respiratory protein hemocyanin
from arthropods. The Biological Bulletin, 171(1), 90–115.
Mauseth, J, D. (2012). Botany: An
Introduction to Plant Biology (5th ed.). Jones & Bartlett Learning.
Maxfield, F. R., & Mondal, M.
(2006). Sterol and lipid trafficking in mammalian cells. Portland Press
Limited.
McFadden, D. W., Riggs, D. R.,
Jackson, B. J., & Vona-Davis, L. (2003). Keyhole limpet hemocyanin, a novel
immune stimulant with promising anticancer activity in Barrett’s esophageal
adenocarcinoma. The American Journal of Surgery, 186(5), 552–555.
Michel, G., Tonon, T., Scornet, D.,
Cock, J. M., & Kloareg, B. (2010). The cell wall polysaccharide metabolism
of the brown alga Ectocarpus siliculosus. Insights into the evolution of
extracellular matrix polysaccharides in Eukaryotes. New Phytologist, 188(1),
82–97.
Moore, P. (2003). Blood and
Justice: The 17 Century Parisian Doctor Who Made Blood Transfusion History.
John Wiley & Sons.
Moore, T. (2013). Novel Approach for
Assessment and Mitigation of Heat-Stress Adverse Effects. Auburn University.
Mory, R. N., Mindell, D., &
Bloom, D. A. (2000). The leech and the physician: biology, etymology, and
medical practice with Hirudinea medicinalis. World Journal of Surgery, 24(7),
878–883.
Murray, R. K., Bender, D. A., Botham,
K. M., Kennelly, P. J., Rodwell, V., & Weil, A. (2012). Harpers
Illustrated Biochemistry (29th ed.). McGraw-Hill Medical.
Newquist, H. P. (2012). The Book
of Blood: From Legends and Leeches to Vampires and Veins. Houghton Mifflin
Harcourt.
Orell, A., Fröls, S., & Albers,
S.-V. (2013). Archaeal biofilms: the great unexplored. Annual Review of Microbiology,
67, 337–354.
Orlov, S. N., & Hamet, P. (2006).
Intracellular monovalent ions as second messengers. The Journal of Membrane
Biology, 210(3), 161–172.
Orlova, E. V, Dube, P., Harris, J.
R., Beckman, E., Zemlin, F., Markl, J., & van Heel, M. (1997). Structure of
keyhole limpet hemocyanin type 1 (KLH1) at 15 Å resolution by electron
cryomicroscopy and angular reconstitution. Journal of Molecular Biology,
271(3), 417–437.
Paliwal, S., Fagien, S., Sun, X.,
Holt, T., Kim, T., Hee, C. K., … Messina, D. J. (2014). Skin extracellular
matrix stimulation following injection of a hyaluronic acid–based dermal filler
in a rat model. Plastic and Reconstructive Surgery, 134(6),
1224–1233.
Pearson, H. A. (2002). History of
pediatric hematology oncology. Pediatric Research, 52(6),
979–992.
Pelletier, H., & Kraut, J.
(1992). Crystal Structure of a Complex Between Electron Transfer. Science,
258, 1.
Pesce, A., Bolognesi, M., Bocedi, A.,
Ascenzi, P., Dewilde, S., Moens, L., … Burmester, T. (2002). Neuroglobin and
cytoglobin. EMBO Reports, 3(12), 1146–1151.
Pesce, A., Dewilde, S., Nardini, M.,
Moens, L., Ascenzi, P., Hankeln, T., … Bolognesi, M. (2003). Human brain
neuroglobin structure reveals a distinct mode of controlling oxygen affinity. Structure,
11(9), 1087–1095.
Peters, R. (2006). Introduction to
nucleocytoplasmic transport: molecules and mechanisms. Xenopus Protocols:
Cell Biology and Signal Transduction, 235–258.
Pick, C., Scherbaum, S., Hegedüs, E.,
Meyer, A., Saur, M., Neumann, R., … Burmester, T. (2014). Structure, diversity
and evolution of myriapod hemocyanins. FEBS Journal, 281(7),
1818–1833.
Plopper, G. (2007). The extracellular
matrix and cell adhesion. Cells.
Prewitt, T. (1992). Unholy Anorexia:
Blood Myth and the Signs of the Flesh. Semiotics, 300–319.
Provance, D. W., McDowall, A., Marko,
M., & Luby-Phelps, K. (1993). Cytoarchitecture of size-excluding
compartments in living cells. Journal of Cell Science, 106(2),
565–577.
Race, R. R., Sanger, R., &
Fisher, R. (1962). Blood groups in man (Vol. 142). Blackwell scientific
publications Oxford.
Ratner, V. A., Zharkikh, A. A.,
Kolchanov, N., Rodin, S. N., Solovyov, V. V, & Antonov, A. S. (1996).
Theoretical Analysis of the Evolution of Genes and Proteins. In Molecular
Evolution (pp. 93–145). Springer.
Rhoades, R. A., & Bell, D. R.
(2013). Medical Physiology, Principles for Clinical Medicine (4th ed.).
Baltimore: Lippincott Williams & Wilkins.
Riggs, D. R., Jackson, B.,
Vona-Davis, L., & McFadden, D. (2002). In vitro anticancer effects of a
novel immunostimulant: keyhole limpet hemocyanin. Journal of Surgical
Research, 108(2), 279–284.
Rolleston, H. (1934). The history of
haematology. SAGE Publications.
Roos, A., & Boron, W. F. (1981).
Intracellular pH. Physiological Reviews, 61(2), 296–434.
Ross, M. H., & Pawlina, W.
(2011). Histology a text and atlas (6th ed.). Baltimore: Lippincott
Williams & Wilkins.
Ruoslahti, E. (1996). Brain
extracellular matrix. Glycobiology, 6(5), 489–492.
Scalettar, B. A., Abney, J. R., &
Hackenbrock, C. R. (1991). Dynamics, structure, and function are coupled in the
mitochondrial matrix. Proceedings of the National Academy of Sciences, 88(18),
8057–8061.
Schultheiss, D., & Denil, J.
(2002). History of the microscope and development of microsurgery: a revolution
for reproductive tract surgery. Andrologia, 34(4), 234–241.
Silverthorn, D. U., Bruce, B. R.,
Ober, W. C., Garrison, C. W., & Silverthorn, A. C. (2010). Human
physiology an integrative aproach (5th ed.). San Francisco: Pearson,
Benjamin Cummings.
Starr, D. (2012). Blood: an epic
history of medicine and commerce. Knopf.
Stenzl, A., Dolashki, A., Stevanovic,
S., Voelter, W., Aicher, W., & Dolashka, P. (2016). Cytotoxic Effects of
Rapana venosa Hemocyanin on Bladder Cancer Permanent Cell Lines. Journal of
US-China Medical Science, 13, 179–188.
Stern, K. R., Bidlack, J. E., &
Jansky, S. H. (2008). Introductory Plant Biology (11th ed.). McGraw-Hill
New York.
Storz, J. F., Opazo, J. C., &
Hoffmann, F. G. (2011). Phylogenetic diversification of the globin gene
superfamily in chordates. IUBMB Life, 63(5), 313–322.
Suárez, P. D.,
Rojas, D. V., & Miranda, R. P. (2009). Análisis histórico–epistemológico de
nomenclatura Química Inorgánica. TED: Tecné, Episteme y Didaxis.
Sussich, F., Skopec, C., Brady, J.,
& Cesàro, A. (2001). Reversible dehydration of trehalose and anhydrobiosis:
from solution state to an exotic crystal? Carbohydrate Research, 334(3),
165–176.
Swartz, A. M., Batich, K. A., Fecci,
P. E., & Sampson, J. H. (2015). Peptide vaccines for the treatment of
glioblastoma. Journal of Neuro-Oncology, 123(3), 433–440.
Tam, J. P. (1988). Synthetic peptide
vaccine design: synthesis and properties of a high-density multiple antigenic
peptide system. Proceedings of the National Academy of Sciences, 85(15),
5409–5413.
Tam, J. P., & Lu, Y.-A. (1989).
Vaccine engineering: enhancement of immunogenicity of synthetic peptide
vaccines related to hepatitis in chemically defined models consisting of T-and
B-cell epitopes. Proceedings of the National Academy of Sciences, 86(23),
9084–9088.
Tejero, J., & Gladwin, M. T.
(2014). The globin superfamily: functions in nitric oxide formation and decay. Biological
Chemistry, 395(6), 631–639.
Terwilliger, N. B. (2015). Oxygen
transport proteins in Crustacea: hemocyanin and hemoglobin. Physiology, 4,
359–390.
Thanbichler, M., Wang, S. C., &
Shapiro, L. (2005). The bacterial nucleoid: a highly organized and dynamic
structure. Journal of Cellular Biochemistry, 96(3), 506–521.
Ureta, T.
(1985). Organización del metabolismo: Localización subcelular de enzimas
glicolíticas. Arch. Biol. Med. Exp, 18(9).
Vallone, B., Nienhaus, K., Brunori,
M., & Nienhaus, G. U. (2004). The structure of murine neuroglobin: novel
pathways for ligand migration and binding. Proteins: Structure, Function,
and Bioinformatics, 56(1), 85–92.
Verkman, A. S. (2002). Solute and
macromolecule diffusion in cellular aqueous compartments. Trends in
Biochemical Sciences, 27(1), 27–33.
Voit, R., Feldmaier-Fuchs, G.,
Schweikardt, T., Decker, H., & Burmester, T. (2000). Complete Sequence of
the 24-mer Hemocyanin of the TarantulaEurypelma californicum STRUCTURE AND
INTRAMOLECULAR EVOLUTION OF THE SUBUNITS. Journal of Biological Chemistry,
275(50), 39339–39344.
Wajcman, H., Kiger, L., & Marden,
M. C. (2009). Structure and function evolution in the superfamily of globins. Comptes
Rendus Biologies, 332(2), 273–282.
Wang, Y., Meng, H., Yuan, X., Peng,
J., Guo, Q., Lu, S., & Wang, A. (2014). Fabrication and in vitro evaluation
of an articular cartilage extracellular matrix-hydroxyapatite bilayered
scaffold with low permeability for interface tissue engineering. Biomedical
Engineering Online, 13(1), 80.
Wayne, R. (2009). Plant Cell
Biology (1st ed.). San Diego: Elsevier.
Weisiger, R. A.
(2002). Cytosolic fatty
acid binding proteins catalyze two distinct steps in intracellular transport of
their ligands. In Cellular Lipid Binding Proteins (pp. 35–43). Springer.
Weiss, J. N., & Korge, P. (2001).
The Cytoplasm No Longer a Well-Mixed Bag. Circulation Research, 89,
108–110. Retrieved from http://circres.ahajournals.org/content/89/2/108.full#R1-094537
Whitteridge, G., Pagel, W., &
Keynes, G. (1972). William Harvey and the Circulation of the Blood.
Wiggins, P. M. (1990). Role of water
in some biological processes. Microbiological Reviews, 54(4),
432–449.
Wikipedia, S. (2013). Hemoproteins:
Arc System, Catalase, Chlorocruorin, Chromoprotein, Cytochrome B6f Complex.
University-Press Org.
Winey, M., Mamay, C. L., O’toole, E.
T., Mastronarde, D. N., Giddings Jr, T. H., McDonald, K. L., & McIntosh, J.
R. (1995). Three-dimensional ultrastructural analysis of the Saccharomyces
cerevisiae mitotic spindle. Journal of Cell Biology, 129(6),
1601–1616.
Wittenberg, J. B., & Wittenberg,
B. A. (1990). Mechanisms of cytoplasmic hemoglobin and myoglobin function. Annual
Review of Biophysics and Biophysical Chemistry, 19(1), 217–241.
Yeates, T. O., Crowley, C. S., &
Tanaka, S. (2010). Bacterial microcompartment organelles: protein shell
structure and evolution. Annual Review of
Biophysics, 39, 185–205.