Hibernation induces expression of moesin in intestinal epithelial cells.

Identification of proteins that are differentially expressed in mammals that hibernate can provide insight into mechanisms that preserve cellular function at low temperatures. A candidate protein was identified in intestinal brush border membranes of 13-lined ground squirrels. Intestinal brush border membrane proteins were separated using SDS-PAGE and gels were stained with Coomassie blue. We observed a approximately 75-kDa band that was specifically increased in brush border membranes isolated from torpid squirrels compared with summer active squirrels. The 75-kDa band was cut from one-dimensional gels and sequenced. A 17 amino acid sequence was identified of which amino acids 2-17 matched exactly a portion of moesin, a membrane-cytoskeletal linking protein and member of the ERM (ezrin/radixin/moesin) family. The sequence results were confirmed using anti-moesin antibodies that detected strong bands at approximately 75 kDa on Western blots of brush border membranes in torpid squirrels (Tb approximately 7 degreesC) and only faint signals in summer squirrels (Tb approximately 37 degrees C) or aroused hibernators (Tb approximately 37 degrees C). In contrast, signals obtained using anti-ezrin antibodies were uniformly strong in all squirrels, regardless of activity state. Intestinal brush borders of mice and rats expressed ezrin but not moesin. These results provide evidence for the physiological induction of an ERM protein in intestinal epithelial cells of torpid hibernators and support the idea that hibernation involves differential expression of gene products that may facilitate viability of cells at low temperatures.

[1]  S. Martin,et al.  Preservation of intestinal gene expression during hibernation. , 1996, The American journal of physiology.

[2]  M. Toner,et al.  Induction of tolerance to hypothermia by previous heat shock using human fibroblasts in culture. , 1996, Cryobiology.

[3]  É. Carpentier,et al.  Identification and characterization of a low temperature regulated gene encoding an actin‐binding protein from wheat , 1996, FEBS letters.

[4]  P. Epstein,et al.  Thermoregulatory and heat-shock protein response deficits in cold-exposed diabetic mice. , 1996, The American journal of physiology.

[5]  E. Guillery,et al.  Developmental regulation of chloride/formate exchange in guinea pig proximal tubules. , 1995, The American journal of physiology.

[6]  T. Kawula,et al.  Hsc66, an Hsp70 homolog in Escherichia coli, is induced by cold shock but not by heat shock , 1995, Journal of bacteriology.

[7]  G. Perozzi,et al.  Transcriptional regulation of the ezrin gene during rat intestinal development and epithelial differentiation. , 1995, Biochimica et biophysica acta.

[8]  R. Tompkins,et al.  Effects of hypothermia on the function, membrane integrity, and cytoskeletal structure of hepatocytes. , 1995, Cryobiology.

[9]  S. Martin,et al.  alpha 2-Macroglobulin gene expression during hibernation in ground squirrels is independent of acute phase response. , 1995, The American journal of physiology.

[10]  K. Pestonjamasp,et al.  Moesin, ezrin, and p205 are actin-binding proteins associated with neutrophil plasma membranes. , 1995, Molecular biology of the cell.

[11]  J. Landry,et al.  Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27 , 1995, Molecular and cellular biology.

[12]  G. Somero,et al.  Proteins and temperature. , 1995, Annual review of physiology.

[13]  J. Hazel.  Thermal adaptation in biological membranes: is homeoviscous adaptation the explanation? , 1995, Annual review of physiology.

[14]  N. Sato,et al.  ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons , 1994, The Journal of cell biology.

[15]  N. Sato,et al.  Perturbation of cell adhesion and microvilli formation by antisense oligonucleotides to ERM family members , 1994, The Journal of cell biology.

[16]  L. Huang,et al.  Transient cold shock induces the heat shock response upon recovery at 37 degrees C in human cells. , 1994, The Journal of biological chemistry.

[17]  J. Labbé,et al.  Intrinsic microtubule stability in interphase cells , 1994, The Journal of cell biology.

[18]  M. Arpin,et al.  Membrane-actin microfilament connections: an increasing diversity of players related to band 4.1. , 1994, Current opinion in cell biology.

[19]  A. Bretscher,et al.  Ezrin is concentrated in the apical microvilli of a wide variety of epithelial cells whereas moesin is found primarily in endothelial cells. , 1993, Journal of cell science.

[20]  A. Bretscher,et al.  Moesin, like ezrin, colocalizes with actin in the cortical cytoskeleton in cultured cells, but its expression is more variable. , 1993, Journal of cell science.

[21]  N. Sills,et al.  Maintenance of intestinal nutrient transport during hibernation. , 1992, The American journal of physiology.

[22]  S. Martin,et al.  Central role for differential gene expression in mammalian hibernation. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[23]  H. Carey,et al.  Seasonal changes in mucosal structure and function in ground squirrel intestine. , 1990, The American journal of physiology.

[24]  J. K. Raison,et al.  Membrane function in mammalian hibernation. , 1989, Biochimica et biophysica acta.

[25]  A. Hadjioloff,et al.  Seasonal involution of gut-associated lymphoid tissue of the European ground squirrel. , 1987, Developmental and comparative immunology.

[26]  C. P. Lyman.  Hibernation and Torpor in Mammals and Birds , 1983 .

[27]  J. August,et al.  Coprecipitation of heat shock proteins with a cell surface glycoprotein. , 1982, Proceedings of the National Academy of Sciences of the United States of America.

[28]  G. Semenza,et al.  A modified procedure for the rapid preparation of efficiently transporting vesicles from small intestinal brush border membranes. Their use in investigating some properties of D-glucose and choline transport systems. , 1978, Biochimica et biophysica acta.

[29]  K. Fichtelius,et al.  Changes in the concentration of lymphocytes in the intestinal epithelium of hibernating ground squirrels (Citellus tridecemlineatus). , 2009, Acta pathologica et microbiologica Scandinavica.