Biochemical analysis of jejunal brush border membrane of golden hamster: pathogenic modulations due to ancylostomiasis.
The common hookworm (Ancylostoma ceylanicum) infection of humans was studied in golden hamsters model system. Significant biochemical modulations were observed in hamster jejunal brush border membrane (BBM), the primary site of infection. Analysis of BBM at the peak of infection (3-weeks) revealed a marked decrease in the activities of sucrase, lactase and maltase, while activities of alkaline phosphatase, (Ca2+ + Mg2+)-ATPase and gamma-glutamyl transpeptidase were increased. Kinetic studies conducted with maltase, a superficially localised enzyme of jejunal BBM, revealed loss of enzyme active site during the infection. Among other constituents, the levels of cholesterol and triglycerides were significantly decreased with slight increase in phospholipid content in the infected animals. The hookworm infection also caused a decline in total hexose content indicating an altered membrane glycocalyx. Conversely, there was significant enhancement of hydroxyproline and sialic acid contents. SDS-PAGE analysis showed an enhancement in both low and high molecular weight proteins in jejunal BBM preparations of the infected group. Gel electrophoresis of glycoproteins further revealed the appearance of two additional peaks in the low molecular weight region and concomitant disappearance of a peak in the high molecular weight region. These results strongly support the view that the hookworm infection causes severe damage not to the site of attachment alone but also to the entire cell lining of the jejunum and therefore could influence overall digestion and absorption.
Mukerjee
S
S
Biochemistry Division, Central Drug Research Institute, Lucknow, India.
Upreti
R K
RK
Tekwani
B L
BL
Kidwai
A M
AM
D000724:Ancylostomiasis / Q000201:enzymology / Q000209:etiology*; D000818:Animals; D006224:Cricetinae; D007583:Jejunum / Q000201:enzymology* / Q000469:parasitology; D008297:Male; D008647:Mesocricetus; D008871:Microvilli / Q000201:enzymology / Q000469:parasitology