Ultrastructural localization of WGA,RCA I,LFA and SBA binding sites in the seven-day-old mouse embryo |
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Authors: | R Herken B Sander M Hofmann |
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Institution: | (1) Department of Anatomy and Cell Biology, Marburg, Robert-Koch-Str. 6, D-3550 Marburg/Lahn, Federal Republic of Germany |
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Abstract: | Summary Transglutaminases are Ca2+-dependent intra-and extracellular enzymes catalyzing the cross-linking between proteins and/or polyamines, thereby eliciting
divergent physiological effects such as fibrin clot stabilization or hair follicle cross-linking. A secretory transglutaminase
(EC 2.3.2.13) was isolated from the coagulating gland of the rat. The protein is highly glycosylated. A fraction purified
to homogeneity was used as an antigen to raise polyclonal antibodies in rabbits. These antibodies were used to identify the
secretion sites of the protein within the male accessory sex glands as well as to study the immunological relationships of
the respective antigen within different organs of different species. In the rat, the coagulating gland and likewise the dorsal
prostate gave a positive immunoreaction. In the guinea pig, a closely related protein was detected in the anterior prostate.
No cross-reactivity was found with membrane-bound transglutaminase from liver, erythrocytes or blood clotting factor XIIIa.
The intraluminal secretion of the aforementioned glands was only weakly stained. No secretory granules were observed in the
glandular epithelium but instead bleb-like structures reminiscent of apocrine secretion. A slight background stain of the
epithelium remained even in castrated animals where secretion is largely suppressed. The background stain is attributed to
a tissue-type, membrane-bound, non-secretory transglutaminase that is not androgen dependent, but instead synthesized only
after androgen deprivation. |
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