Membrane fluidity on the surface of Hymenolepis diminuta (Cestoda): immunological implications

Parasitology ◽  
1997 ◽  
Vol 115 (6) ◽  
pp. 667-671 ◽  
Author(s):  
K. TAYLOR ◽  
J. R. KUSEL ◽  
D. HOOLE
Keyword(s):  
Membrane Fluidity ◽  
Regional Differences ◽  
Fluorescence Recovery After Photobleaching ◽  
Surface Membrane ◽  
Neck Region ◽  
Hymenolepis Diminuta ◽  
C Reactive Protein ◽  
Rat Serum ◽  
Reactive Protein ◽  
Normal Rat

Regional differences of Hymenolepis diminuta to immune lysis have been investigated by monitoring surface membrane fluidity utilizing fluorescence recovery after photobleaching (FRAP). Although the surface membrane of the newly excysted stage was completely immobile the molecular fluidity of the strobila membrane of 4-day-old parasites was greater than that associated with the scolex/neck region. Significant differences (P>0·001) occurred in the mobility of the strobila membrane of 4-day-old H. diminuta from 100-worm infections compared with 7- and 21-day-old parasites and 4-day-old individuals from 10-worm infections. Exposure to 50% normal rat serum and 1 mg/ml rat C reactive protein decreased or eliminated membrane fluidity. The significance of membrane mobility is discussed with reference to resistance to complement-mediated lysis and destrobilation.

Immunochemical detection of an acute-phase protein in rat serum

1965 ◽  
Vol 209 (4) ◽  
pp. 736-744 ◽  
Author(s):  
Henry E. Weimer ◽  
David C. Benjamin
Keyword(s):  
Acute Phase ◽  
Acute Phase Protein ◽  
C Reactive Protein ◽  
Agar Gel ◽  
Rat Serum ◽  
Reactive Protein ◽  
Immunochemical Detection ◽  
Normal Rat ◽  
Starch Gels ◽  
New Protein

A new protein designated α2-AP (acute phase) globulin, not present in normal rat serum, has been detected by immunochemical methods in a wide variety of pathologic states. The protein is a carbohydrate-containing euglobulin and migrates with the mobility of an α2-globulin in filter paper and agar gel. In acrylamide and starch gels it exhibits a very low mobility suggestive of a macroglobulin. It is not related antigenically to C-reactive protein or Cx-reactive protein. Possible factors responsible for the production of the protein were discussed. It was concluded that the appearance of the protein in the circulation represents a systemic manifestation of the acute inflammatory response, and that the synthesis of the protein is stimulated by substances released from injured or necrotic cells.

Repair ofHymenolepis diminutaafter complement-mediated damage

Parasitology ◽  
1989 ◽  
Vol 99 (3) ◽  
pp. 437-443 ◽  
Author(s):  
J. Andreassen ◽  
D. Hoole
Keyword(s):  
Neck Region ◽  
Regenerative Process ◽  
Hymenolepis Diminuta ◽  
Embryological Development ◽  
Rat Serum ◽  
Ultrastructural Studies ◽  
Normal Rat ◽  
Electron Lucent

SummarySeven and 56-day-oldHymenolepis diminutawere exposed to complement by incubation in 50% normal rat serum (NRS) in modified Hanks' saline. Ultrastructural studies revealed that the scolex/neck region remained relatively intact whilst in the strobila region microthrix denudation and loss of distal cytoplasm were observed. When complement-mediated damaged worms were incubated in vitro in 50% heat-inactivated normal rat serum (hiNRS) plus M199 or implanted into the duodenum of NMRI mice repair occurred, although destrobilated parasites were only foundin vivo. The regions undergoing repair contained tegumental protrusions, vesicles, large electron-lucent areas and large quantities of lipid. Microtriches were formed parallel to the parasite surface and were raised into a perpendicular position. It is suggested that the regenerative process exhibited after complement-mediated damage does not mimic totally the embryological development of the surface layer.

Interactions between rat C-reactive protein and adult Hymenolepis diminuta

Parasitology ◽  
1997 ◽  
Vol 115 (3) ◽  
pp. 297-302 ◽  
Author(s):  
K. TAYLOR ◽  
D. HOOLE
Keyword(s):  
Regional Distribution ◽  
Serum Levels ◽  
Hymenolepis Diminuta ◽  
C Reactive Protein ◽  
Reactive Protein ◽  
Secondary Infections ◽  
Elisa Technique ◽  
Electron Microscopical

Interactions between adult Hymenolepis diminuta and rat C-reactive protein (CRP) were investigated in vivo and in vitro. Using an ELISA technique, serum levels of CRP were monitored in rats infected with 100 cysticercoids. Although infection increased the level of this protein in the early stages of parasitization, the increase was not significant until 35 days post-infection (p.i.). Secondary infections did not enhance the response. When H. diminuta was cultured in the presence of CRP, reduced worm motility and opaque areas were observed and electron microscopical studies revealed shedding of microtriches and lysis of the tegument. Initially, damage was restricted to the strobila which correlated with the regional distribution of phosphorylcholine as visualized using immunofluorescence.

scholarly journals Amino acid sequence homology between rat and human C-reactive protein

1984 ◽  
Vol 221 (3) ◽  
pp. 903-906 ◽  
Author(s):  
J A Taylor ◽  
C J Bruton ◽  
J K Anderson ◽  
J E Mole ◽  
F C De Beer ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Binding Protein ◽  
C Reactive Protein ◽  
Rat Serum ◽  
Reactive Protein ◽  
Phosphoryl Choline ◽  
Serum Amyloid P Component ◽  
C Terminus ◽  
Amyloid P

The rat serum protein that undergoes Ca2+-dependent binding to pneumococcal C-polysaccharide and to phosphocholine residues, and that is evidently a member of the pentraxin family of proteins by virtue of its appearance under the electron microscope, has been variously designated as rat C-reactive protein (CRP) [de Beer, Baltz, Munn, Feinstein, Taylor, Bruton, Clamp & Pepys (1982) Immunology 45, 55-70], ‘phosphoryl choline-binding protein’ [Nagpurkar & Mookerjea (1981) J. Biol. Chem. 256, 7440-7448] and rat serum amyloid P component (SAP) [Pontet, D'Asnieres, Gache, Escaig & Engler (1981) Biochim. Biophys. Acta 671, 202-210]. The partial amino acid sequence (45 residues) towards the C-terminus of this protein was determined, and it showed 71.7% identity with the known sequence of human CRP but only 54.3% identity with human SAP. Since human CRP and SAP are themselves approximately 50% homologous, the level of identity between the rat protein and human SAP is evidence only of membership of the pentraxin family. In contrast, the much greater resemblance to human CRP confirms that the rat C-polysaccharide-binding/phosphocholine-binding protein is in fact rat CRP.

scholarly journals Associations between High-Sensitivity C-Reactive Protein and Membrane Fluidity of Red Blood Cells in Hypertensive Elderly Men: An Electron Spin Resonance Study

2012 ◽  
Vol 2012 ◽  
pp. 1-5 ◽  
Author(s):  
Kazushi Tsuda
Keyword(s):  
Electron Spin Resonance ◽  
Membrane Fluidity ◽  
Electron Spin ◽  
Blood Cells ◽  
High Sensitivity ◽  
C Reactive Protein ◽  
Elderly Men ◽  
Reactive Protein ◽  
Spin Resonance ◽  
Hs Crp

Recent evidence indicates that high-sensitivity C-reactive protein (hs-CRP), an acute phase of an inflammatory marker, might be associated with atherosclerosis, hypertension, and other cardiovascular diseases. The present study was performed to assess the possible link between plasma hs-CRP and membrane fluidity (a reciprocal value of membrane microviscosity) in hypertensive elderly men. We measured the membrane fluidity of red blood cells (RBCs) in hypertensive and normotensive elderly men using an electron spin resonance and spin-labeling method. Membrane fluidity of RBCs was decreased in hypertensive elderly men compared with normotensive elderly men. Plasma hs-CRP levels were significantly higher in hypertensive elderly men than in normotensive elderly men. In contrast, plasma nitric-oxide- (NO-) metabolite levels were lower in hypertensive elderly men than in normotensive elderly men. The reduced membrane fluidity of RBCs was associated with increased plasma hs-CRP and decreased plasma NO-metabolite levels. In a multivariate regression analysis, plasma hs-CRP was an independent determinant of membrane fluidity of RBCs after adjustment for general risk factors. The results suggest that CRP might have a close correlation with the rheologic behavior of RBCs and the microcirculation and would contribute, at least in part, to the circulatory dysfunction and vascular complications in hypertensive elderly men.

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