Ultrastructure of the apical part of the epithelial cells of the mucous membrane of the small intestine after extensive experimental enterectomy

1971 ◽  
Vol 72 (2) ◽  
pp. 964-967 ◽  
Author(s):  
S. N. Genyk
1954 ◽  
Vol s3-95 (30) ◽  
pp. 153-158
Author(s):  
W. HEWITT

Experiments are described in which sections from the small intestine of rats, fed on triolein 2¾ hours previously, were examined with Sudan black and the acid haematein test, with and without Sudan red coloration. The histochemical appearances in the epithelial cells of the mucous membrane are described. Lipoid can be observed not only within the epithelial cells and their free border but also as particles between the cells.


1956 ◽  
Vol s3-97 (38) ◽  
pp. 199-203
Author(s):  
W. HEWITT

Studies have been made of the small intestine of rats previously fed with triolein. A previous description of the location of the lipid and phospholipid has been confirmed by using Sudan black and the acid haematein test. In addition histochemical tests have been applied to detect neutral fat and fatty acid. The lipid in the free border of the epithelial cells of the mucous membrane consisted of fatty acid and probably neutral fat, which would support the belief that when neutral fat is absorbed some of it is unhydrolysed. Additional evidence for this is provided by the fact that neutral fat could also be detected between the lateral parts of the cells. Occasionally fatty acid was also detectable in this location. Variable proportions of neutral fat, fatty acid, and phospholipid were to be found inside the epithelial cells and it appeared possible that there was a direct relationship between the amounts of neutral fat and phospholipid present.


2014 ◽  
Vol 71 (1) ◽  
pp. 35-38
Author(s):  
Bin Liu ◽  
Xiaoling Li ◽  
Fulu Ai ◽  
Tianlu Wang ◽  
Yun Chen ◽  
...  

Author(s):  
A. J. Tousimis

The elemental composition of amino acids is similar to that of the major structural components of the epithelial cells of the small intestine and other tissues. Therefore, their subcellular localization and concentration measurements are not possible by x-ray microanalysis. Radioactive isotope labeling: I131-tyrosine, Se75-methionine and S35-methionine have been successfully employed in numerous absorption and transport studies. The latter two have been utilized both in vitro and vivo, with similar results in the hamster and human small intestine. Non-radioactive Selenomethionine, since its absorption/transport behavior is assumed to be the same as that of Se75- methionine and S75-methionine could serve as a compound tracer for this amino acid.


Author(s):  
D.S. Friend ◽  
N. Ghildyal ◽  
M.F. Gurish ◽  
K.F. Austen ◽  
R.L. Stevens

Trichinella spiralis induces a profound mastocytosis and eosinophilia in the small intestine of the infected mouse. Mouse mast cells (MC) store in their granules various combinations of at least five chymotryptic chymases [designated mouse MC protease (mMCP) 1 to 5], two tryptic proteases designated mMCP-6 and mMCP-7 and an exopeptidase, carboxypeptidase A (mMC-CPA). Using antipeptide, protease -specific antibodies to these MC granule proteases, immunohistochemistry was done to determine the distribution, number and protease phenotype of the MCs in the small intestine and spleen 10 to >60 days after Trichinella infection of BALB/c and C3H mice. TEM was performed to evaluate the granule morphology of the MCs between intestinal epithelial cells and in the lamina propria (mucosal MCs) and in the submucosa, muscle and serosa of the intestine (submucosal MCs).As noted in the table below, the number of submucosal MCs remained constant throughout the study. In contrast, on day 14, the number of MCs in the mucosa increased ~25 fold. Increased numbers of MCs were observed between epithelial cells in the mucosal crypts, in the lamina propria and to a lesser extent, between epithelial cells of the intestinal villi.


2006 ◽  
Vol 50 (2) ◽  
pp. 198-200
Author(s):  
Juliana Fariña ◽  
M. Concepción Millana ◽  
M<sup>a</sup> Jesús Fernández-Aceñero ◽  
Vanessa Campo-Ruiz

1989 ◽  
Vol 109 (3) ◽  
pp. 1057-1069 ◽  
Author(s):  
A Marxer ◽  
B Stieger ◽  
A Quaroni ◽  
M Kashgarian ◽  
H P Hauri

The previously produced monoclonal antibody IEC 1/48 against cultured rat intestinal crypt cells (Quaroni, A., and K. J. Isselbacher. 1981. J. Natl. Cancer Inst. 67:1353-1362) was extensively characterized and found to be directed against the beta subunit of (Na+ + K+)-ATPase as assessed by immunological and enzymatic criteria. Under nondenaturing conditions the antibody precipitated the alpha-beta enzyme complex (98,000 and 48,000 Mr). This probe, together with the monoclonal antibody C 62.4 against the alpha subunit (Kashgarian, M., D. Biemesderfer, M. Caplan, and B. Forbush. 1985. Kidney Int. 28:899-913), was used to localize (Na+ + K+)-ATPase in epithelial cells along the rat intestinal tract by immunofluorescence and immunoelectron microscopy. Both antibodies exclusively labeled the basolateral membrane of small intestine and proximal colon epithelial cells. However, in the distal colon, IEC 1/48, but not C 62.4, also labeled the brush border membrane. The cross-reacting beta-subunit-like antigen on the apical cell pole was tightly associated with isolated brush borders but was apparently devoid of (Na+ + K+)-ATPase activity. Subcellular fractionation of colonocytes in conjunction with limited proteolysis and surface radioiodination of intestinal segments suggested that the cross-reacting antigen in the brush border may be very similar to the beta subunit. The results support the notion that in the small intestine and proximal colon the enzyme subunits are exclusively targeted to the basolateral membrane while in the distal colon nonassembled beta subunit or a beta-subunit-like protein is also transported to the apical cell pole.


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